{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T15:51:45Z","timestamp":1791474705719,"version":"4.3.4"},"reference-count":341,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2020,11,12]],"date-time":"2020-11-12T00:00:00Z","timestamp":1605139200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100007336","name":"Universitatea din Bucure\u0219ti","doi-asserted-by":"publisher","award":["PN-III-P4-ID-PCCF-2016-0114 POSCCE (RADAR), PN-III-P1-1.1-PD-2016-1798 (PD-148)"],"award-info":[{"award-number":["PN-III-P4-ID-PCCF-2016-0114 POSCCE (RADAR), PN-III-P1-1.1-PD-2016-1798 (PD-148)"]}],"id":[{"id":"10.13039\/501100007336","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007336","name":"Universitatea din Bucure\u0219ti","doi-asserted-by":"publisher","award":["PN-III-P1-1.1-PD-2016-2137"],"award-info":[{"award-number":["PN-III-P1-1.1-PD-2016-2137"]}],"id":[{"id":"10.13039\/501100007336","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Since the discovery of penicillin by Alexander Fleming in 1929 as a therapeutic agent against staphylococci, \u03b2-lactam antibiotics (BLAs) remained the most successful antibiotic classes against the majority of bacterial strains, reaching a percentage of 65% of all medical prescriptions. Unfortunately, the emergence and diversification of \u03b2-lactamases pose indefinite health issues, limiting the clinical effectiveness of all current BLAs. One solution is to develop \u03b2-lactamase inhibitors (BLIs) capable of restoring the activity of \u03b2-lactam drugs. In this review, we will briefly present the older and new BLAs classes, their mechanisms of action, and an update of the BLIs capable of restoring the activity of \u03b2-lactam drugs against ESKAPE (Enterococcus spp., Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Enterobacter spp.) pathogens. Subsequently, we will discuss several promising alternative approaches such as bacteriophages, antimicrobial peptides, nanoparticles, CRISPR (clustered regularly interspaced short palindromic repeats) cas technology, or vaccination developed to limit antimicrobial resistance in this endless fight against Gram-negative pathogens.<\/jats:p>","DOI":"10.3390\/ijms21228527","type":"journal-article","created":{"date-parts":[[2020,11,12]],"date-time":"2020-11-12T10:00:32Z","timestamp":1605175232000},"page":"8527","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":54,"title":["Emerging Strategies to Combat \u03b2-Lactamase Producing ESKAPE Pathogens"],"prefix":"10.3390","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2409-0966","authenticated-orcid":false,"given":"Corneliu Ovidiu","family":"Vrancianu","sequence":"first","affiliation":[{"name":"Microbiology Immunology Department and The Research Institute of the University of Bucharest, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irina","family":"Gheorghe","sequence":"additional","affiliation":[{"name":"Microbiology Immunology Department and The Research Institute of the University of Bucharest, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6464-381X","authenticated-orcid":false,"given":"Elena-Georgiana","family":"Dobre","sequence":"additional","affiliation":[{"name":"Microbiology Immunology Department and The Research Institute of the University of Bucharest, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilda Czobor","family":"Barbu","sequence":"additional","affiliation":[{"name":"Microbiology Immunology Department and The Research Institute of the University of Bucharest, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roxana Elena","family":"Cristian","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcela","family":"Popa","sequence":"additional","affiliation":[{"name":"Microbiology Immunology Department and The Research Institute of the University of Bucharest, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5660-7122","authenticated-orcid":false,"given":"Sang Hee","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Myongji University, 03674 Myongjiro, Yongin 449-728, Gyeonggido, Korea"},{"name":"National Leading Research Laboratory, Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin 17058, Gyeonggido, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carmen","family":"Limban","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, \u201cCarol Davila\u201d University of Medicine and Pharmacy, Traian Vuia no.6, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilinca Margareta","family":"Vlad","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, \u201cCarol Davila\u201d University of Medicine and Pharmacy, Traian Vuia no.6, 020956 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6098-1857","authenticated-orcid":false,"given":"Mariana Carmen","family":"Chifiriuc","sequence":"additional","affiliation":[{"name":"Microbiology Immunology Department and The Research Institute of the University of Bucharest, Faculty of Biology, University of Bucharest, 020956 Bucharest, Romania"},{"name":"Academy of Romanian Scientists, 030167 Bucharest, Romania"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,11,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"a025247","DOI":"10.1101\/cshperspect.a025247","article-title":"\u03b2-Lactams and \u03b2-Lactamase Inhibitors: An Overview","volume":"6","author":"Bush","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1073\/pnas.54.4.1133","article-title":"Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine","volume":"54","author":"Tipper","year":"1965","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_3","first-page":"299","article-title":"Penicillin-sensitive enzymes in peptidoglycan biosynthesis","volume":"11","author":"Joris","year":"1985","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"16808","DOI":"10.1073\/pnas.1300118110","article-title":"How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function","volume":"110","author":"Otero","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1038\/nchembio.1911","article-title":"Synergistic, collaterally sensitive \u03b2-lactam combinations suppress resistance in MRSA","volume":"11","author":"Gonzales","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Sykes, J.E., and Papich, M.G. (2013). Antibacterial Drugs. Canine Feline Infect. Dis., 66\u201386.","DOI":"10.1016\/B978-1-4377-0795-3.00008-9"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"a000414","DOI":"10.1101\/cshperspect.a000414","article-title":"The bacterial cell envelope","volume":"2","author":"Silhavy","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"8852","DOI":"10.1073\/pnas.1812779115","article-title":"The bacterial outer membrane is an evolving antibiotic barrier","volume":"115","author":"May","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e01541-16","DOI":"10.1128\/mBio.01541-16","article-title":"Antibiotic Resistance and Regulation of the Gram-Negative Bacterial Outer Membrane Barrier by Host Innate Immune Molecules","volume":"7","author":"Miller","year":"2016","journal-title":"MBio"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/s41579-019-0294-2","article-title":"Porins and small-molecule translocation across the outer membrane of Gram-negative bacteria","volume":"18","author":"Vergalli","year":"2020","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"539","DOI":"10.3389\/fmicb.2019.00539","article-title":"Emerging Strategies to Combat ESKAPE Pathogens in the Era of Antimicrobial Resistance: A Review","volume":"10","author":"Mulani","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1128\/CMR.00037-09","article-title":"Three decades of beta-lactamase inhibitors","volume":"23","author":"Drawz","year":"2010","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_13","first-page":"9519718","article-title":"The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases","volume":"2018","author":"Ali","year":"2018","journal-title":"Biomed Res. Int."},{"key":"ref_14","first-page":"S2","article-title":"beta-Lactamases: Quality and resistance","volume":"3","author":"Medeiros","year":"1997","journal-title":"Clin. Microbiol. Infect. Off. Publ. Eur. Soc. Clin. Microbiol. Infect. Dis."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"e01076-18","DOI":"10.1128\/AAC.01076-18","article-title":"Past and Present Perspectives on \u03b2-Lactamases","volume":"62","author":"Bush","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.2147\/IDR.S250591","article-title":"Plasmid Profiling and Occurrence of \u03b2-Lactamase Enzymes in Multidrug-Resistant Uropathogenic Escherichia coli in Kathmandu, Nepal","volume":"13","author":"Shrestha","year":"2020","journal-title":"Infect. Drug Resist."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/AAC.42.1.1","article-title":"Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases","volume":"42","author":"Massova","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1128\/AAC.18.5.834","article-title":"Binding of beta-lactam antibiotics to penicillin-binding proteins of Staphylococcus aureus and Streptococcus faecalis: Relation to antibacterial activity","volume":"18","author":"Georgopapadakou","year":"1980","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/S1526-9523(02)00330-6","article-title":"The penicillins: A review and update","volume":"47","author":"Miller","year":"2002","journal-title":"J. Midwifery Women\u2019s Health"},{"key":"ref_20","first-page":"611","article-title":"Appropriate prescribing of oral beta-lactam antibiotics","volume":"62","author":"Holten","year":"2000","journal-title":"Am. Fam. Physician"},{"key":"ref_21","first-page":"3","article-title":"The importance of the development of antibiotic resistance in Staphylococcus aureus","volume":"12","author":"Schito","year":"2006","journal-title":"Clin. Microbiol. Infect. Off. Publ. Eur. Soc. Clin. Microbiol. Infect. Dis."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1002\/iub.1289","article-title":"Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus","volume":"66","author":"Fishovitz","year":"2014","journal-title":"IUBMB Life"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Balsalobre, L., Blanco, A., and Alarc\u00f3n, T. (2019). Beta-Lactams. Antibiotic Drug Resistance, John Wiley & Sons, Ltd.","DOI":"10.1002\/9781119282549.ch3"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1586\/14787210.5.3.365","article-title":"Piperacillin-tazobactam: A beta-lactam\/beta-lactamase inhibitor combination","volume":"5","author":"Gin","year":"2007","journal-title":"Expert Rev. Anti. Infect. Ther."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1111\/j.1469-0691.2007.01858.x","article-title":"Orthodox and unorthodox clavulanate combinations against extended-spectrum beta-lactamase producers","volume":"14","author":"Livermore","year":"2008","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_26","unstructured":"Brunton, L.L., Hilal-Dandan, R., and Knollmannn, B.C. (2017). Penicillins, Cephalosporins, and other \u03b2-lactam antibiotics. The Pharmacological Basis of Therapeutics, McGraw-Hill Education."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Chaudhry, S.B., Veve, M.P., and Wagner, J.L. (2019). Cephalosporins: A Focus on Side Chains and \u03b2-Lactam Cross-Reactivity. Pharmacy, 7.","DOI":"10.3390\/pharmacy7030103"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1080\/10408410902733979","article-title":"Beta-lactams and beta-lactamase-inhibitors in current- or potential-clinical practice: A comprehensive update","volume":"35","author":"Shahid","year":"2009","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_29","first-page":"195","article-title":"Clinical practice guidelines for antimicrobial prophylaxis in surgery","volume":"70","author":"Bratzler","year":"2013","journal-title":"Am. J. Health Pharm. AJHP Off. J. Am. Soc. Health Pharm."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1128\/CMR.8.4.557","article-title":"beta-Lactamases in laboratory and clinical resistance","volume":"8","author":"Livermore","year":"1995","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1161\/CIRCULATIONAHA.106.183095","article-title":"Prevention of infective endocarditis: Guidelines from the American Heart Association: A guideline from the American Heart Association Rheumatic Fever, Endocarditis, and Kawasaki Disease Committee, Council on Cardiovascular Disease in the Young, and the C","volume":"116","author":"Wilson","year":"2007","journal-title":"Circulation"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1212\/01.wnl.0000265517.66976.28","article-title":"Practice parameter: Treatment of nervous system Lyme disease (an evidence-based review): Report of the Quality Standards Subcommittee of the American Academy of Neurology","volume":"69","author":"Halperin","year":"2007","journal-title":"Neurology"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"e83","DOI":"10.1093\/cid\/ciz021","article-title":"Clinical Practice Guideline for the Management of Asymptomatic Bacteriuria: 2019 Update by the Infectious Diseases Society of America","volume":"68","author":"Nicolle","year":"2019","journal-title":"Clin. Infect. Dis."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1086\/649554","article-title":"Diagnosis and management of complicated intra-abdominal infection in adults and children: Guidelines by the Surgical Infection Society and the Infectious Diseases Society of America","volume":"50","author":"Solomkin","year":"2010","journal-title":"Clin. Infect. Dis."},{"key":"ref_35","first-page":"1","article-title":"Sexually transmitted diseases treatment guidelines, 2015","volume":"64","author":"Workowski","year":"2015","journal-title":"MMWR. Recomm. Rep. Morb. Mortal. Wkly. Rep. Recomm. Rep."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1128\/AAC.34.2.337","article-title":"Outer membrane permeability and beta-lactamase stability of dipolar ionic cephalosporins containing methoxyimino substituents","volume":"34","author":"Nikaido","year":"1990","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1128\/AAC.35.1.68","article-title":"Novel method for measurement of outer membrane permeability to new beta-lactams in intact Enterobacter cloacae cells","volume":"35","author":"Bellido","year":"1991","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"e10","DOI":"10.1093\/cid\/ciu296","article-title":"Practice guidelines for the diagnosis and management of skin and soft tissue infections: 2014 update by the Infectious Diseases Society of America","volume":"59","author":"Stevens","year":"2014","journal-title":"Clin. Infect. Dis."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1128\/AAC.01787-10","article-title":"In vitro activity of ceftaroline against gram-positive and gram-negative pathogens isolated from patients in Canadian hospitals in 2009","volume":"55","author":"Karlowsky","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1128\/AAC.45.3.825-836.2001","article-title":"In vitro and in vivo properties of Ro 63-9141, a novel broad-spectrum cephalosporin with activity against methicillin-resistant staphylococci","volume":"45","author":"Hebeisen","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2530","DOI":"10.1128\/AAC.00238-06","article-title":"Activities of ceftobiprole and other beta-lactams against Streptococcus pneumoniae clinical isolates from the United States with defined substitutions in penicillin-binding proteins PBP 1a, PBP 2b, and PBP 2x","volume":"50","author":"Davies","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"32096","DOI":"10.1074\/jbc.M112.355644","article-title":"Structural insights into the anti-methicillin-resistant Staphylococcus aureus (MRSA) activity of ceftobiprole","volume":"287","author":"Lovering","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"3089","DOI":"10.1128\/AAC.00218-07","article-title":"Interactions of ceftobiprole with beta-lactamases from molecular classes A to D","volume":"51","author":"Queenan","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s40265-013-0168-2","article-title":"Ceftolozane\/tazobactam: A novel cephalosporin\/\u03b2-lactamase inhibitor combination with activity against multidrug-resistant gram-negative bacilli","volume":"74","author":"Zhanel","year":"2014","journal-title":"Drugs"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1128\/AAC.01695-15","article-title":"In Vitro Antimicrobial Activity of a Siderophore Cephalosporin, S-649266, against Enterobacteriaceae Clinical Isolates, Including Carbapenem-Resistant Strains","volume":"60","author":"Kohira","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/s40265-019-1055-2","article-title":"Cefiderocol: A Siderophore Cephalosporin with Activity Against Carbapenem-Resistant and Multidrug-Resistant Gram-Negative Bacilli","volume":"79","author":"Zhanel","year":"2019","journal-title":"Drugs"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"e01801-18","DOI":"10.1128\/AAC.01801-18","article-title":"ARGONAUT-I: Activity of Cefiderocol (S-649266), a Siderophore Cephalosporin, against Gram-Negative Bacteria, Including Carbapenem-Resistant Nonfermenters and Enterobacteriaceae with Defined Extended-Spectrum \u03b2-Lactamases and Carbapenemases","volume":"63","author":"Jacobs","year":"2019","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1093\/jac\/dky425","article-title":"In vitro activities of cefiderocol, ceftolozane\/tazobactam, ceftazidime\/avibactam and other comparative drugs against imipenem-resistant Pseudomonas aeruginosa and Acinetobacter baumannii, and Stenotrophomonas maltophilia, all associated with bloodstream","volume":"74","author":"Hsueh","year":"2019","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4197","DOI":"10.1128\/AAC.00629-13","article-title":"Adaptation-based resistance to siderophore-conjugated antibacterial agents by Pseudomonas aeruginosa","volume":"57","author":"Tomaras","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1128\/AAC.21.1.85","article-title":"Azthreonam (SQ 26,776), a synthetic monobactam specifically active against aerobic gram-negative bacteria","volume":"21","author":"Sykes","year":"1982","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/S0891-5520(05)70256-7","article-title":"Cephalosporins, carbapenems, and monobactams","volume":"14","author":"Asbel","year":"2000","journal-title":"Infect. Dis. Clin. N. Am."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Rodr\u00edguez-Ba\u00f1o, J., Guti\u00e9rrez-Guti\u00e9rrez, B., Machuca, I., and Pascual, A. (2018). Treatment of Infections Caused by Extended-Spectrum-Beta-Lactamase-, AmpC-, and Carbapenemase-Producing Enterobacteriaceae. Clin. Microbiol. Rev., 31.","DOI":"10.1128\/CMR.00079-17"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.diagmicrobio.2015.02.003","article-title":"Activities of ceftazidime, ceftaroline, and aztreonam alone and combined with avibactam against isogenic Escherichia coli strains expressing selected single \u03b2-lactamases","volume":"82","author":"Bajaksouzian","year":"2015","journal-title":"Diagn. Microbiol. Infect. Dis."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"El-Shorbagi, A.N., and Chaudhary, S. (2019). Monobactams: A Unique Natural Scaffold of Four-Membered Ring Skeleton, Recent Development to Clinically Overcome Infections by Multidrug- Resistant Microbes. Lett. Drug Des. Discov., 16.","DOI":"10.2174\/1570180816666190516113202"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1128\/AAC.01525-09","article-title":"In vitro properties of BAL30072, a novel siderophore sulfactam with activity against multiresistant gram-negative bacilli","volume":"54","author":"Page","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1021\/ml200012f","article-title":"Preparation, gram-negative antibacterial activity, and hydrolytic stability of novel siderophore-conjugated monocarbam diols","volume":"2","author":"Flanagan","year":"2011","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"4943","DOI":"10.1128\/AAC.00296-11","article-title":"Carbapenems: Past, present, and future","volume":"55","author":"Endimiani","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_58","first-page":"2015","article-title":"Doripenem: A new carbapenem antibiotic","volume":"67","author":"Chahine","year":"2010","journal-title":"Am. J. Heal. Pharm. AJHP Off. J. Am. Soc. Health Pharm."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"S1","DOI":"10.1086\/599809","article-title":"Doripenem: A new carbapenem in the treatment of nosocomial infection","volume":"49","author":"Mandell","year":"2009","journal-title":"Clin. Infect. Dis."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Codjoe, F.S., and Donkor, E.S. (2017). Carbapenem Resistance: A Review. Med. Sci., 6.","DOI":"10.3390\/medsci6010001"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1128\/AAC.49.2.776-778.2005","article-title":"Detection of KPC carbapenem-hydrolyzing enzymes in Enterobacter spp. from Brooklyn, New York","volume":"49","author":"Bratu","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.jgar.2017.10.023","article-title":"Spread of Klebsiella pneumoniae ST395 non-susceptible to carbapenems and resistant to fluoroquinolones in North-Eastern France","volume":"13","author":"Muggeo","year":"2018","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1128\/AAC.45.4.1151-1161.2001","article-title":"Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae","volume":"45","author":"Yigit","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1086\/421495","article-title":"Emergence of carbapenem-resistant Klebsiella species possessing the class A carbapenem-hydrolyzing KPC-2 and inhibitor-resistant TEM-30 beta-lactamases in New York City","volume":"39","author":"Bradford","year":"2004","journal-title":"Clin. Infect. Dis."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1001\/archinte.165.12.1430","article-title":"Rapid spread of carbapenem-resistant Klebsiella pneumoniae in New York City: A new threat to our antibiotic armamentarium","volume":"165","author":"Bratu","year":"2005","journal-title":"Arch. Intern. Med."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1089\/mdr.2014.0087","article-title":"First report in China of Enterobacteriaceae clinical isolates coharboring blaNDM-1 and blaIMP-4 drug resistance genes","volume":"21","author":"Chen","year":"2015","journal-title":"Microb. Drug Resist."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2519","DOI":"10.1128\/AAC.03053-15","article-title":"Genomic Characterization of Enterobacter cloacae Isolates from China That Coproduce KPC-3 and NDM-1 Carbapenemases","volume":"60","author":"Du","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Wang, J., Yuan, M., Chen, H., Chen, X., Jia, Y., Zhu, X., Bai, L., Bai, X., Fanning, S., and Lu, J. (2017). First Report of Klebsiella oxytoca Strain Simultaneously Producing NDM-1, IMP-4, and KPC-2 Carbapenemases. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.00877-17"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.diagmicrobio.2017.10.007","article-title":"Occurrence of Enterobacter hormaechei carrying bla(NDM-1) and bla(KPC-2) in China","volume":"90","author":"Yang","year":"2018","journal-title":"Diagn. Microbiol. Infect. Dis."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1128\/AAC.01051-12","article-title":"Novel carbapenem antibiotics for parenteral and oral applications: In vitro and in vivo activities of 2-aryl carbapenems and their pharmacokinetics in laboratory animals","volume":"57","author":"Fujimoto","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s40560-020-0429-6","article-title":"Molecular diversity of extended-spectrum \u03b2-lactamases and carbapenemases, and antimicrobial resistance","volume":"8","author":"Sawa","year":"2020","journal-title":"J. Intensive Care"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1038\/146837a0","article-title":"An Enzyme from Bacteria able to Destroy Penicillin","volume":"146","author":"Abraham","year":"1940","journal-title":"Nature"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1099\/00221287-94-1-55","article-title":"Identification of beta-lactamases by analytical isoelectric focusing: Correlation with bacterial taxonomy","volume":"94","author":"Matthew","year":"1976","journal-title":"J. Gen. Microbiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1172\/JCI111042","article-title":"Transferable beta-lactamase. A new mechanism for in vitro penicillin resistance in Streptococcus faecalis","volume":"72","author":"Murray","year":"1983","journal-title":"J. Clin. Investig."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1093\/jac\/9.suppl_B.11","article-title":"\u03b2-Lactamases and their clinical significance","volume":"9","year":"1982","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_76","first-page":"111","article-title":"Evolution of the serine beta-lactamases: Past, present and future","volume":"7","author":"Hall","year":"2004","journal-title":"Drug Resist. Updates Rev. Comment. Antimicrob. Anticancer Chemother."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/nature10388","article-title":"Antibiotic resistance is ancient","volume":"477","author":"King","year":"2011","journal-title":"Nature"},{"key":"ref_78","first-page":"172","article-title":"Molecular characterization of TEM-type beta-lactamases identified in cold-seep sediments of Edison Seamount (south of Lihir Island, Papua New Guinea)","volume":"43","author":"Song","year":"2005","journal-title":"J. Microbiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1111\/1758-2229.12453","article-title":"Exploring divergent antibiotic resistance genes in ancient metagenomes and discovery of a novel beta-lactamase family","volume":"8","author":"Rascovan","year":"2016","journal-title":"Environ. Microbiol. Rep."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1111\/1758-2229.12011","article-title":"Distribution of antibiotic resistance genes in glacier environments","volume":"5","author":"Segawa","year":"2013","journal-title":"Environ. Microbiol. Rep."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.ijantimicag.2008.07.029","article-title":"Antibiotic resistance in a very remote Amazonas community","volume":"33","author":"Bartoloni","year":"2009","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/0014-5793(79)80248-3","article-title":"Penicillinase active sites: Labelling of serine-44 in beta-lactamase I by 6beta-bromopenicillanic acid","volume":"99","author":"Waley","year":"1979","journal-title":"FEBS Lett."},{"key":"ref_83","first-page":"2574","article-title":"Crystal structure of NDM-1 reveals a common \u03b2-lactam hydrolysis mechanism","volume":"25","author":"Zhang","year":"2011","journal-title":"FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1111\/j.1348-0421.1968.tb00415.x","article-title":"Drug resistance of enteric bacteria. XIV. Comparison of beta-lactamases in gram-negative rod bacteria resistant to alpha-aminobenzylpenicillin","volume":"12","author":"Sawai","year":"1968","journal-title":"Jpn. J. Microbiol."},{"key":"ref_85","first-page":"321","article-title":"The structure of beta-lactamases","volume":"289","author":"Ambler","year":"1980","journal-title":"Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1093\/jac\/5.4.349","article-title":"Plasmid-mediated beta-lactamases of Gram-negative bacteria: Properties and distribution","volume":"5","author":"Matthew","year":"1979","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1128\/AAC.17.6.929","article-title":"Principal beta-lactamases responsible for resistance to beta-lactam antibiotics in urinary tract infections","volume":"17","author":"Simpson","year":"1980","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1093\/jac\/12.5.507","article-title":"Plasmid-determined beta-lactamases identified in a group of 204 ampicillin-resistant Enterobacteriaceae","volume":"12","author":"Roy","year":"1983","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1093\/oxfordjournals.bmb.a071942","article-title":"Beta-lactamases","volume":"40","author":"Medeiros","year":"1984","journal-title":"Br. Med. Bull."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1007\/BF02013586","article-title":"Frequency of plasmid-determined beta-lactamases in 680 consecutively isolated strains of Enterobacteriaceae","volume":"4","author":"Roy","year":"1985","journal-title":"Eur. J. Clin. Microbiol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1128\/JCM.06025-11","article-title":"Molecular epidemiology over an 11-year period (2000 to 2010) of extended-spectrum \u03b2-lactamase-producing Escherichia coli causing bacteremia in a centralized Canadian region","volume":"50","author":"Peirano","year":"2012","journal-title":"J. Clin. Microbiol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.jgar.2017.06.008","article-title":"ESBL-producing Escherichia coli and Klebsiella pneumoniae: The most prevalent clinical isolates obtained between 2005 and 2012 in Mexico","volume":"10","author":"Barrios","year":"2017","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1128\/AAC.27.4.555","article-title":"Resistance caused by decreased penetration of beta-lactam antibiotics into Enterobacter cloacae","volume":"27","author":"Bush","year":"1985","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1093\/jac\/46.6.895","article-title":"Emergence of imipenem resistance in Klebsiella pneumoniae owing to combination of plasmid-mediated CMY-4 and permeability alteration","volume":"46","author":"Cao","year":"2000","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1159\/000238757","article-title":"Heterogeneity of beta-lactamase production in Pseudomonas maltophilia, a nosocomial pathogen","volume":"36","author":"Cullmann","year":"1990","journal-title":"Chemotherapy"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1128\/AAC.37.5.939","article-title":"Biochemical properties of a carbapenem-hydrolyzing beta-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli","volume":"37","author":"Nordmann","year":"1993","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1128\/AAC.35.1.147","article-title":"Transferable imipenem resistance in Pseudomonas aeruginosa","volume":"35","author":"Watanabe","year":"1991","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1584","DOI":"10.1128\/AAC.43.7.1584","article-title":"Cloning and characterization of blaVIM, a new integron-borne metallo-beta-lactamase gene from a Pseudomonas aeruginosa clinical isolate","volume":"43","author":"Lauretti","year":"1999","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1086\/508841","article-title":"Large outbreak of infection and colonization with gram-negative pathogens carrying the metallo- beta -lactamase gene blaIMP-4 at a 320-bed tertiary hospital in Australia","volume":"28","author":"Herbert","year":"2007","journal-title":"Infect. Control Hosp. Epidemiol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"2622","DOI":"10.1128\/JCM.00505-15","article-title":"High-Resolution Analysis by Whole-Genome Sequencing of an International Lineage (Sequence Type 111) of Pseudomonas aeruginosa Associated with Metallo-Carbapenemases in the United Kingdom","volume":"53","author":"Turton","year":"2015","journal-title":"J. Clin. Microbiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3365","DOI":"10.1128\/AAC.00126-09","article-title":"Molecular epidemiology of KPC-producing Klebsiella pneumoniae isolates in the United States: Clonal expansion of multilocus sequence type 258","volume":"53","author":"Kitchel","year":"2009","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"5873","DOI":"10.1128\/AAC.01019-15","article-title":"Carbapenemase-Producing Klebsiella pneumoniae, a Key Pathogen Set for Global Nosocomial Dominance","volume":"59","author":"Pitout","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"e1","DOI":"10.1016\/j.cmi.2015.08.001","article-title":"Risk factors for bloodstream infections due to colistin-resistant KPC-producing Klebsiella pneumoniae: Results from a multicenter case-control-control study","volume":"21","author":"Giacobbe","year":"2015","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"787","DOI":"10.12998\/wjcc.v2.i12.787","article-title":"Antimicrobial resistance in Acinetobacter baumannii: From bench to bedside","volume":"2","author":"Lin","year":"2014","journal-title":"World J. Clin. Cases"},{"key":"ref_105","first-page":"61","article-title":"Acinetobacter baumannii: Biology and drug resistance\u2014Role of carbapenemases","volume":"54","author":"Nowak","year":"2016","journal-title":"Folia Histochem. Cytobiol."},{"key":"ref_106","first-page":"895","article-title":"Imipenem\/cilastatin: The first carbapenem antibiotic","volume":"19","author":"Lyon","year":"1985","journal-title":"Drug Intell. Clin. Pharm."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1128\/AAC.01261-13","article-title":"Identification of 50 class D \u03b2-lactamases and 65 Acinetobacter-derived cephalosporinases in Acinetobacter spp.","volume":"58","author":"Goussard","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.3906\/sag-1607-91","article-title":"Investigation of class-d beta-lactamases causing carbapenem resistance in clinical Acinetobacter baumannii isolates","volume":"47","author":"Davandeh","year":"2017","journal-title":"Turk. J. Med. Sci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1128\/CMR.00117-13","article-title":"OXA \u03b2-lactamases","volume":"27","author":"Evans","year":"2014","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1128\/AAC.44.1.196-199.2000","article-title":"Sequence analysis of ARI-1, a novel OXA beta-lactamase, responsible for imipenem resistance in Acinetobacter baumannii 6B92","volume":"44","author":"Donald","year":"2000","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_111","first-page":"348","article-title":"Prevalence of bla (Oxacillinase-23)and bla (Oxacillinase-24\/40-)type Carbapenemases in Pseudomonas aeruginosa Species Isolated From Patients with Nosocomial and Non-nosocomial Infections in the West of Iran","volume":"13","author":"Rouhi","year":"2018","journal-title":"Iran. J. Pathol."},{"key":"ref_112","first-page":"143","article-title":"Role of outer membrane permeability, efflux mechanism, and carbapenemases in carbapenem-nonsusceptible Pseudomonas aeruginosa from Dubai hospitals: Results of the first cross-sectional survey","volume":"84","author":"Akkawi","year":"2019","journal-title":"Int. J. Infect. Dis. IJID Off. Publ. Int. Soc. Infect. Dis."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"iv32","DOI":"10.1093\/jac\/dkz285","article-title":"Characterization of carbapenem-resistant and XDR Pseudomonas aeruginosa in Canada: Results of the CANWARD 2007-16 study","volume":"74","author":"McCracken","year":"2019","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1089\/mdr.2014.0171","article-title":"Coproduction of NDM-1 and KPC-2 in Enterobacter hormaechei from Brazil","volume":"21","author":"Pereira","year":"2015","journal-title":"Microb. Drug Resist."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"3632","DOI":"10.1093\/jac\/dkz394","article-title":"Emergence of Klebsiella pneumoniae and Enterobacter cloacae producing OXA-48 carbapenemases from retail meats in China, 2018","volume":"74","author":"Zhuang","year":"2019","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.3201\/eid2406.171648","article-title":"Genomic Epidemiology of Global Carbapenemase-Producing Enterobacter spp., 2008\u20132014","volume":"24","author":"Peirano","year":"2018","journal-title":"Emerg. Infect. Dis."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1556\/1886.2018.00033","article-title":"Screening for Carbapenemases in Ertapenem-Resistant Enterobacteriaceae Collected at a Tunisian Hospital Between 2014 and 2018","volume":"9","author":"Kollenda","year":"2019","journal-title":"Eur. J. Microbiol. Immunol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"2675","DOI":"10.1093\/jac\/dky257","article-title":"VIM\/IMP carbapenemase-producing Enterobacteriaceae in Poland: Epidemic Enterobacter hormaechei and Klebsiella oxytoca lineages","volume":"73","author":"Izdebski","year":"2018","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1128\/AAC.39.6.1211","article-title":"A functional classification scheme for beta-lactamases and its correlation with molecular structure","volume":"39","author":"Bush","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1128\/AAC.01009-09","article-title":"Updated functional classification of beta-lactamases","volume":"54","author":"Bush","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1128\/JCM.01215-17","article-title":"High-Stringency Evaluation of the Automated BD Phoenix CPO Detect and Rapidec Carba NP Tests for Detection and Classification of Carbapenemases","volume":"55","author":"Thomson","year":"2017","journal-title":"J. Clin. Microbiol."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Lee, D., Das, S., Dawson, N.L., Dobrijevic, D., Ward, J., and Orengo, C. (2016). Novel Computational Protocols for Functionally Classifying and Characterising Serine Beta-Lactamases. PLoS Comput. Biol., 12.","DOI":"10.1371\/journal.pcbi.1004926"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1111\/nyas.12023","article-title":"Proliferation and significance of clinically relevant \u03b2-lactamases","volume":"1277","author":"Bush","year":"2013","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_124","first-page":"700","article-title":"Prediction of antibiotic resistance from antibiotic resistance genes detected in antibiotic-resistant commensal Escherichia coli using PCR or WGS","volume":"72","author":"Moran","year":"2017","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1128\/AAC.11.5.852","article-title":"Clavulanic acid: A beta-lactamase-inhiting beta-lactam from Streptomyces clavuligerus","volume":"11","author":"Reading","year":"1977","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"i3","DOI":"10.1093\/jac\/dkh050","article-title":"Augmentin (amoxicillin\/clavulanate) in the treatment of community-acquired respiratory tract infection: A review of the continuing development of an innovative antimicrobial agent","volume":"53","author":"White","year":"2004","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/s40265-013-0013-7","article-title":"Ceftazidime-avibactam: A novel cephalosporin\/\u03b2-lactamase inhibitor combination","volume":"73","author":"Zhanel","year":"2013","journal-title":"Drugs"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"11663","DOI":"10.1073\/pnas.1205073109","article-title":"Avibactam is a covalent, reversible, non-\u03b2-lactam \u03b2-lactamase inhibitor","volume":"109","author":"Ehmann","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1007\/s15010-017-1096-y","article-title":"Pharmacological aspects and spectrum of action of ceftazidime-avibactam: A systematic review","volume":"46","author":"Tuon","year":"2018","journal-title":"Infection"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"4067","DOI":"10.1021\/acs.jmedchem.8b00091","article-title":"Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using \u03b2-Lactamase Inhibitors and \u03b2-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234","volume":"61","author":"Nguyen","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Moya, B., Barcelo, I.M., Bhagwat, S., Patel, M., Bou, G., Papp-Wallace, K.M., Bonomo, R.A., and Oliver, A. (2017). WCK 5107 (Zidebactam) and WCK 5153 Are Novel Inhibitors of PBP2 Showing Potent \u201c\u03b2-Lactam Enhancer\u201d Activity against Pseudomonas aeruginosa, Including Multidrug-Resistant Metallo-\u03b2-Lactamase-Producing High-Risk Clones. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.02529-16"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"17104","DOI":"10.1038\/nmicrobiol.2017.104","article-title":"ETX2514 is a broad-spectrum \u03b2-lactamase inhibitor for the treatment of drug-resistant Gram-negative bacteria including Acinetobacter baumannii","volume":"2","author":"Guler","year":"2017","journal-title":"Nat. Microbiol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"290","DOI":"10.4065\/74.3.290","article-title":"The penicillins","volume":"74","author":"Wright","year":"1999","journal-title":"Mayo Clin. Proc."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1093\/femsre\/fuz014","article-title":"Antibiotic resistance breakers: Current approaches and future directions","volume":"43","author":"Laws","year":"2019","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1128\/AAC.38.4.767","article-title":"Comparative activities of clavulanic acid, sulbactam, and tazobactam against clinically important beta-lactamases","volume":"38","author":"Payne","year":"1994","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1128\/AAC.04808-14","article-title":"Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii","volume":"59","author":"Penwell","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1586\/eri.09.11","article-title":"Linezolid for patients with neutropenia: Are bacteriostatic agents appropriate?","volume":"7","author":"Rafailidis","year":"2009","journal-title":"Expert Rev. Anti Infect. Ther."},{"key":"ref_138","first-page":"425","article-title":"Comparative in vitro activity of beta-lactam\/beta-lactamase inhibitor combinations against gram negative bacteria","volume":"122","author":"Mohanty","year":"2005","journal-title":"Indian J. Med. Res."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1002\/phar.1609","article-title":"Ceftolozane\/Tazobactam: A Novel Cephalosporin\/\u03b2-Lactamase Inhibitor Combination","volume":"35","author":"Cho","year":"2015","journal-title":"Pharmacotherapy"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1093\/jac\/27.1.29","article-title":"In-vitro evaluation of ampicillin\/brobactam and comparison with other beta-lactam antibiotics","volume":"27","author":"Melchior","year":"1991","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Thomson, K.S., AbdelGhani, S., Snyder, J.W., and Thomson, G.K. (2019). Activity of Cefepime-Zidebactam against Multidrug-Resistant (MDR) Gram-Negative Pathogens. Antibiotics, 8.","DOI":"10.3390\/antibiotics8010032"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Moya, B., Barcelo, I.M., Bhagwat, S., Patel, M., Bou, G., Papp-Wallace, K.M., Bonomo, R.A., and Oliver, A. (2017). Potent \u03b2-Lactam Enhancer Activity of Zidebactam and WCK 5153 against Acinetobacter baumannii, Including Carbapenemase-Producing Clinical Isolates. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.01238-17"},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Isler, B., Doi, Y., Bonomo, R.A., and Paterson, D.L. (2019). New Treatment Options against Carbapenem-Resistant Acinetobacter baumannii Infections. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.01110-18"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"5454","DOI":"10.1128\/AAC.00711-16","article-title":"Effect of the \u03b2-Lactamase Inhibitor Vaborbactam Combined with Meropenem against Serine Carbapenemase-Producing Enterobacteriaceae","volume":"60","author":"Castanheira","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Nguyen, L.P., Pinto, N.A., Vu, T.N., Lee, H., Cho, Y.L., Byun, J.H., D\u2019Souza, R., and Yong, D. (2020). In Vitro Activity of a Novel Siderophore-Cephalosporin, GT-1 and Serine-Type \u03b2-Lactamase Inhibitor, GT-055, against Escherichia coli, Klebsiella pneumoniae and Acinetobacter spp. Panel Strains. Antibiotics, 9.","DOI":"10.3390\/antibiotics9050267"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1007\/s40265-018-0902-x","article-title":"Ceftazidime-Avibactam: A Review in the Treatment of Serious Gram-Negative Bacterial Infections","volume":"78","author":"Shirley","year":"2018","journal-title":"Drugs"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"5704","DOI":"10.1128\/AAC.03057-14","article-title":"Avibactam and class C \u03b2-lactamases: Mechanism of inhibition, conservation of the binding pocket, and implications for resistance","volume":"58","author":"Lahiri","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1128\/AAC.00826-13","article-title":"New \u03b2-lactamase inhibitors: A therapeutic renaissance in an MDR world","volume":"58","author":"Drawz","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"2849","DOI":"10.1128\/AAC.02286-15","article-title":"Activity of Ceftazidime-Avibactam against Extended-Spectrum- and AmpC \u03b2-Lactamase-Producing Enterobacteriaceae Collected in the INFORM Global Surveillance Study from 2012 to 2014","volume":"60","author":"Karlowsky","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.ijantimicag.2014.12.033","article-title":"In vitro activity of ceftazidime, ceftaroline and aztreonam alone and in combination with avibactam against European Gram-negative and Gram-positive clinical isolates","volume":"45","author":"Testa","year":"2015","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1093\/cid\/ciw378","article-title":"Ceftazidime-avibactam Versus Doripenem for the Treatment of Complicated Urinary Tract Infections, Including Acute Pyelonephritis: RECAPTURE, a Phase 3 Randomized Trial Program","volume":"63","author":"Wagenlehner","year":"2016","journal-title":"Clin. Infect. Dis."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Shields, R.K., Nguyen, M.H., Chen, L., Press, E.G., Potoski, B.A., Marini, R.V., Doi, Y., Kreiswirth, B.N., and Clancy, C.J. (2017). Ceftazidime-Avibactam Is Superior to Other Treatment Regimens against Carbapenem-Resistant Klebsiella pneumoniae Bacteremia. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.00883-17"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1093\/cid\/cix783","article-title":"Colistin Versus Ceftazidime-Avibactam in the Treatment of Infections Due to Carbapenem-Resistant Enterobacteriaceae","volume":"66","author":"Lok","year":"2018","journal-title":"Clin. Infect. Dis."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Shields, R.K., Chen, L., Cheng, S., Chavda, K.D., Press, E.G., Snyder, A., Pandey, R., Doi, Y., Kreiswirth, B.N., and Nguyen, M.H. (2017). Emergence of Ceftazidime-Avibactam Resistance Due to Plasmid-Borne bla(KPC-3) Mutations during Treatment of Carbapenem-Resistant Klebsiella pneumoniae Infections. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.02097-16"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1128\/JCM.02771-15","article-title":"The Problem of Carbapenemase-Producing-Carbapenem-Resistant-Enterobacteriaceae Detection","volume":"54","author":"Lutgring","year":"2016","journal-title":"J. Clin. Microbiol."},{"key":"ref_156","first-page":"1349","article-title":"Role of the Outer Membrane and Porins in Susceptibility of \u03b2-Lactamase-Producing Enterobacteriaceae to Ceftazidime-Avibactam","volume":"60","author":"Peslier","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.2147\/IDR.S180905","article-title":"Ceftolozane\/tazobactam for the treatment of complicated intra-abdominal and urinary tract infections: Current perspectives and place in therapy","volume":"12","author":"Pigrau","year":"2019","journal-title":"Infect. Drug Resist."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"3933","DOI":"10.1128\/AAC.00296-10","article-title":"Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa","volume":"54","author":"Zamorano","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_159","first-page":"2135","article-title":"Ceftolozane-tazobactam: A new-generation cephalosporin","volume":"72","author":"Cluck","year":"2015","journal-title":"Am. J. Health Pharm. AJHP Off. J. Am. Soc. Health Pharm."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1093\/jac\/dkx009","article-title":"Ceftolozane\/tazobactam activity against drug-resistant Enterobacteriaceae and Pseudomonas aeruginosa causing urinary tract and intraabdominal infections in Europe: Report from an antimicrobial surveillance programme (2012-15)","volume":"72","author":"Pfaller","year":"2017","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1218","DOI":"10.1128\/AAC.02253-13","article-title":"Activity of ceftolozane-tazobactam against a broad spectrum of recent clinical anaerobic isolates","volume":"58","author":"Snydman","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1093\/jac\/dkw374","article-title":"Efficacy of ceftolozane\/tazobactam against urinary tract and intra-abdominal infections caused by ESBL-producing Escherichia coli and Klebsiella pneumoniae: A pooled analysis of Phase 3 clinical trials","volume":"72","author":"Popejoy","year":"2017","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1007\/s40265-017-0725-1","article-title":"Novel Beta-Lactamase Inhibitors: Unlocking Their Potential in Therapy","volume":"77","author":"Wong","year":"2017","journal-title":"Drugs"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"4478","DOI":"10.1128\/AAC.00194-12","article-title":"In vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillin-resistant, vancomycin-intermediate, vancomycin-resistant, daptomycin-nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus","volume":"56","author":"Saravolatz","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"5029","DOI":"10.1128\/AAC.00830-15","article-title":"Activity of Imipenem with Relebactam against Gram-Negative Pathogens from New York City","volume":"59","author":"Lapuebla","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_166","doi-asserted-by":"crossref","unstructured":"Lob, S.H., Hackel, M.A., Kazmierczak, K.M., Young, K., Motyl, M.R., Karlowsky, J.A., and Sahm, D.F. (2017). In Vitro Activity of Imipenem-Relebactam against Gram-Negative ESKAPE Pathogens Isolated by Clinical Laboratories in the United States in 2015 (Results from the SMART Global Surveillance Program). Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.02209-16"},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Canver, M.C., Satlin, M.J., Westblade, L.F., Kreiswirth, B.N., Chen, L., Robertson, A., Fauntleroy, K., La Spina, M., Callan, K., and Jenkins, S.G. (2019). Activity of Imipenem-Relebactam and Comparator Agents against Genetically Characterized Isolates of Carbapenem-Resistant Enterobacteriaceae. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.00672-19"},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Haidar, G., Clancy, C.J., Chen, L., Samanta, P., Shields, R.K., Kreiswirth, B.N., and Nguyen, M.H. (2017). Identifying Spectra of Activity and Therapeutic Niches for Ceftazidime-Avibactam and Imipenem-Relebactam against Carbapenem-Resistant Enterobacteriaceae. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.00642-17"},{"key":"ref_169","first-page":"2286","article-title":"Activity of MK-7655 combined with imipenem against Enterobacteriaceae and Pseudomonas aeruginosa","volume":"68","author":"Livermore","year":"2013","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"3753","DOI":"10.1128\/AAC.05927-11","article-title":"In vitro activity of MK-7655, a novel \u03b2-lactamase inhibitor, in combination with imipenem against carbapenem-resistant Gram-negative bacteria","volume":"56","author":"Hirsch","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.1093\/jac\/dky107","article-title":"In vitro activity of imipenem\/relebactam against Gram-negative ESKAPE pathogens isolated in 17 European countries: 2015 SMART surveillance programme","volume":"73","author":"Karlowsky","year":"2018","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Goldstein, E.J.C., Citron, D.M., Tyrrell, K.L., Leoncio, E., and Merriam, C.V. (2018). Comparative In Vitro Activities of Relebactam, Imipenem, the Combination of the Two, and Six Comparator Antimicrobial Agents against 432 Strains of Anaerobic Organisms, Including Imipenem-Resistant Strains. Antimicrob. Agents Chemother., 62.","DOI":"10.1128\/AAC.01992-17"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/s40265-017-0851-9","article-title":"Imipenem-Relebactam and Meropenem-Vaborbactam: Two Novel Carbapenem-\u03b2-Lactamase Inhibitor Combinations","volume":"78","author":"Zhanel","year":"2018","journal-title":"Drugs"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"971","DOI":"10.2217\/fmb-2018-0054","article-title":"Meropenem-vaborbactam: A new weapon in the war against infections due to resistant Gram-negative bacteria","volume":"13","author":"Patel","year":"2018","journal-title":"Future Microbiol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1007\/s40265-014-0267-8","article-title":"Treatment options for carbapenem-resistant and extensively drug-resistant Acinetobacter baumannii infections","volume":"74","author":"Viehman","year":"2014","journal-title":"Drugs"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1128\/AAC.45.2.480-484.2001","article-title":"Carbapenem resistance mechanisms in Pseudomonas aeruginosa clinical isolates","volume":"45","author":"Pai","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1002\/j.1875-9114.1997.tb03742.x","article-title":"Meropenem, a new carbapenem antibiotic","volume":"17","author":"Fish","year":"1997","journal-title":"Pharmacotherapy"},{"key":"ref_178","doi-asserted-by":"crossref","unstructured":"Sader, H.S., Castanheira, M., Huband, M., Jones, R.N., and Flamm, R.K. (2017). WCK 5222 (Cefepime-Zidebactam) Antimicrobial Activity against Clinical Isolates of Gram-Negative Bacteria Collected Worldwide in 2015. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.00072-17"},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Almarzoky Abuhussain, S.S., Avery, L.M., Abdelraouf, K., and Nicolau, D.P. (2019). In Vivo Efficacy of Humanized WCK 5222 (Cefepime-Zidebactam) Exposures against Carbapenem-Resistant Acinetobacter baumannii in the Neutropenic Thigh Model. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.01931-18"},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"Rodvold, K.A., Gotfried, M.H., Chugh, R., Gupta, M., Patel, A., Chavan, R., Yeole, R., Friedland, H.D., and Bhatia, A. (2018). Plasma and Intrapulmonary Concentrations of Cefepime and Zidebactam following Intravenous Administration of WCK 5222 to Healthy Adult Subjects. Antimicrob. Agents Chemother., 62.","DOI":"10.1128\/AAC.00682-18"},{"key":"ref_181","doi-asserted-by":"crossref","unstructured":"Bhagwat, S.S., Periasamy, H., Takalkar, S.S., Palwe, S.R., Khande, H.N., and Patel, M.V. (2019). The Novel \u03b2-Lactam Enhancer Zidebactam Augments the In Vivo Pharmacodynamic Activity of Cefepime in a Neutropenic Mouse Lung Acinetobacter baumannii Infection Model. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.02146-18"},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Lepak, A.J., Zhao, M., and Andes, D.R. (2019). WCK 5222 (Cefepime\/Zidebactam) Pharmacodynamic Target Analysis against Metallo-\u03b2-lactamase producing Enterobacteriaceae in the Neutropenic Mouse Pneumonia Model. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.01648-19"},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"Avery, L.M., Abdelraouf, K., and Nicolau, D.P. (2018). Assessment of the In Vivo Efficacy of WCK 5222 (Cefepime-Zidebactam) against Carbapenem-Resistant Acinetobacter baumannii in the Neutropenic Murine Lung Infection Model. Antimicrob. Agents Chemother., 62.","DOI":"10.1128\/AAC.00948-18"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"1474","DOI":"10.1093\/jac\/dkaa036","article-title":"Effective inhibition of PBPs by cefepime and zidebactam in the presence of VIM-1 drives potent bactericidal activity against MBL-expressing Pseudomonas aeruginosa","volume":"75","author":"Moya","year":"2020","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_185","first-page":"149","article-title":"Efficacy of human-simulated bronchopulmonary exposures of cefepime, zidebactam and the combination (WCK 5222) against MDR Pseudomonas aeruginosa in a neutropenic murine pneumonia model","volume":"75","author":"Kidd","year":"2020","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"2938","DOI":"10.1093\/jac\/dkz294","article-title":"Activity of cefepime\/zidebactam (WCK 5222) against Enterobacteriaceae, Pseudomonas aeruginosa and Acinetobacter baumannii endemic to New York City medical centres","volume":"74","author":"Khan","year":"2019","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_187","first-page":"13","article-title":"An update on \u03b2-lactamase inhibitor discovery and development","volume":"36","author":"Docquier","year":"2018","journal-title":"Drug Resist. Updates Rev. Comment. Antimicrob. Anticancer Chemother."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.tips.2018.03.007","article-title":"The Continuing Challenge of Metallo-\u03b2-Lactamase Inhibition: Mechanism Matters","volume":"39","author":"Ju","year":"2018","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"E3745","DOI":"10.1073\/pnas.1601368113","article-title":"Cross-class metallo-\u03b2-lactamase inhibition by bisthiazolidines reveals multiple binding modes","volume":"113","author":"Hinchliffe","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"1880","DOI":"10.1021\/acs.biochem.7b01299","article-title":"Structural and Kinetic Studies of the Potent Inhibition of Metallo-\u03b2-lactamases by 6-Phosphonomethylpyridine-2-carboxylates","volume":"57","author":"Hinchliffe","year":"2018","journal-title":"Biochemistry"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"3271","DOI":"10.2174\/0929867321666140601200803","article-title":"Boronic acid-based enzyme inhibitors: A review of recent progress","volume":"21","author":"Fu","year":"2014","journal-title":"Curr. Med. Chem."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1128\/AAC.02641-15","article-title":"Boronic Acid Transition State Inhibitors Active against KPC and Other Class A \u03b2-Lactamases: Structure-Activity Relationships as a Guide to Inhibitor Design","volume":"60","author":"Rojas","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Hamrick, J.C., Docquier, J.D., Uehara, T., Myers, C.L., Six, D.A., Chatwin, C.L., John, K.J., Vernacchio, S.F., Cusick, S.M., and Trout, R.E.L. (2020). VNRX-5133 (Taniborbactam), a Broad-Spectrum Inhibitor of Serine- and Metallo-\u03b2-Lactamases, Restores Activity of Cefepime in Enterobacterales and Pseudomonas aeruginosa. Antimicrob. Agents Chemother., 64.","DOI":"10.1128\/AAC.01963-19"},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Abdelraouf, K., Almarzoky Abuhussain, S., and Nicolau, D.P. (2020). In vivo pharmacodynamics of new-generation \u03b2-lactamase inhibitor taniborbactam (formerly VNRX-5133) in combination with cefepime against serine-\u03b2-lactamase-producing Gram-negative bacteria. J. Antimicrob. Chemother.","DOI":"10.1093\/jac\/dkaa373"},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Lang, P.A., Parkova, A., Leissing, T.M., Calvopi\u00f1a, K., Cain, R., Krajnc, A., Panduwawala, T.D., Philippe, J., Fishwick, C.W.G., and Trapencieris, P. (2020). Bicyclic Boronates as Potent Inhibitors of AmpC, the Class C \u03b2-Lactamase from Escherichia coli. Biomolecules, 10.","DOI":"10.3390\/biom10060899"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1850","DOI":"10.1093\/jac\/dkaa053","article-title":"In vitro activity of the novel \u03b2-lactamase inhibitor taniborbactam (VNRX-5133), in combination with cefepime or meropenem, against MDR Gram-negative bacterial isolates from China","volume":"75","author":"Wang","year":"2020","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"3861","DOI":"10.1002\/anie.200500835","article-title":"Irreversible inhibition of metallo-beta-lactamase (IMP-1) by 3-(3-mercaptopropionylsulfanyl)propionic acid pentafluorophenyl ester","volume":"44","author":"Kurosaki","year":"2005","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"9543","DOI":"10.1039\/C5CC02594J","article-title":"Ebselen as a potent covalent inhibitor of New Delhi metallo-\u03b2-lactamase (NDM-1)","volume":"51","author":"Chiou","year":"2015","journal-title":"Chem. Commun."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"4802","DOI":"10.1039\/C8CC01067F","article-title":"A protein structure-guided covalent scaffold selectively targets the B1 and B2 subclass metallo-\u03b2-lactamases","volume":"54","author":"Chen","year":"2018","journal-title":"Chem. Commun."},{"key":"ref_200","doi-asserted-by":"crossref","unstructured":"Vrancianu, C.O., Gheorghe, I., Czobor, I.B., and Chifiriuc, M.C. (2020). Antibiotic Resistance Profiles, Molecular Mechanisms and Innovative Treatment Strategies of Acinetobacter baumannii. Microorganisms, 8.","DOI":"10.3390\/microorganisms8060935"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"25","DOI":"10.4102\/sajs.v108i5\/6.795","article-title":"Antimicrobial properties of the skin secretions of frogs","volume":"108","author":"Govender","year":"2012","journal-title":"S. Afr. J. Sci."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"281","DOI":"10.3389\/fphar.2018.00281","article-title":"Antimicrobial Peptides and Their Therapeutic Potential for Bacterial Skin Infections and Wounds","volume":"9","author":"Pfalzgraff","year":"2018","journal-title":"Front. Pharmacol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.peptides.2016.04.005","article-title":"Anti-infective efficacy of the lactoferrin-derived antimicrobial peptide HLR1r","volume":"81","author":"Mahlapuu","year":"2016","journal-title":"Peptides"},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"S\u00e1nchez-G\u00f3mez, S., Ferrer-Espada, R., Stewart, P.S., Pitts, B., Lohner, K., and Mart\u00ednez de Tejada, G. (2015). Antimicrobial activity of synthetic cationic peptides and lipopeptides derived from human lactoferricin against Pseudomonas aeruginosa planktonic cultures and biofilms. BMC Microbiol., 15.","DOI":"10.1186\/s12866-015-0473-x"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"111369","DOI":"10.18632\/oncotarget.22797","article-title":"Assessment of antimicrobial and wound healing effects of Brevinin-2Ta against the bacterium Klebsiella pneumoniae in dermally-wounded rats","volume":"8","author":"Liu","year":"2017","journal-title":"Oncotarget"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"174","DOI":"10.3389\/fcimb.2019.00174","article-title":"Characterization of the in vitro, ex vivo, and in vivo Efficacy of the Antimicrobial Peptide DPK-060 Used for Topical Treatment","volume":"9","author":"Ringstad","year":"2019","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"41","DOI":"10.3389\/fcimb.2017.00041","article-title":"Human Salivary Protein Histatin 5 Has Potent Bactericidal Activity against ESKAPE Pathogens","volume":"7","author":"Du","year":"2017","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1007\/s00726-018-2625-4","article-title":"Potent effects of amino acid scanned antimicrobial peptide Feleucin-K3 analogs against both multidrug-resistant strains and biofilms of Pseudomonas aeruginosa","volume":"50","author":"Xie","year":"2018","journal-title":"Amino Acids"},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Rishi, P., Vashist, T., Sharma, A., Kaur, A., Kaur, A., Kaur, N., Kaur, I.P., and Tewari, R. (2018). Efficacy of designer K11 antimicrobial peptide (a hybrid of melittin, cecropin A1 and magainin 2) against Acinetobacter baumannii-infected wounds. Pathog. Dis., 76.","DOI":"10.1093\/femspd\/fty072"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.bcp.2017.01.009","article-title":"Novel human bioactive peptides identified in Apolipoprotein B: Evaluation of their therapeutic potential","volume":"130","author":"Gaglione","year":"2017","journal-title":"Biochem. Pharmacol."},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Wu, C.L., Hsueh, J.Y., Yip, B.S., Chih, Y.H., Peng, K.L., and Cheng, J.W. (2020). Antimicrobial Peptides Display Strong Synergy with Vancomycin Against Vancomycin-Resistant E. faecium, S. aureus, and Wild-Type E. coli. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21134578"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1080\/08927014.2017.1332186","article-title":"Titanium surfaces immobilized with the major antimicrobial fragment FK-16 of human cathelicidin LL-37 are potent against multiple antibiotic-resistant bacteria","volume":"33","author":"Mishra","year":"2017","journal-title":"Biofouling"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"488","DOI":"10.24272\/j.issn.2095-8137.2019.062","article-title":"Antimicrobial peptides: New hope in the war against multidrug resistance","volume":"40","author":"Mwangi","year":"2019","journal-title":"Zool. Res."},{"key":"ref_214","doi-asserted-by":"crossref","unstructured":"Wang, Y., Hong, J., Liu, X., Yang, H., Liu, R., Wu, J., Wang, A., Lin, D., and Lai, R. (2008). Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0003217"},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Wang, Y., Zhang, Z., Chen, L., Guang, H., Li, Z., Yang, H., Li, J., You, D., Yu, H., and Lai, R. (2011). Cathelicidin-BF, a snake cathelicidin-derived antimicrobial peptide, could be an excellent therapeutic agent for acne vulgaris. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0022120"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/j.bbamem.2006.07.007","article-title":"The human beta-defensin-3, an antibacterial peptide with multiple biological functions","volume":"1758","author":"Dhople","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1164\/rccm.200307-971OC","article-title":"Cathelicidin peptide sheep myeloid antimicrobial peptide-29 prevents endotoxin-induced mortality in rat models of septic shock","volume":"169","author":"Giacometti","year":"2004","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"e12832","DOI":"10.1097\/MD.0000000000012832","article-title":"A bovine myeloid antimicrobial peptide (BMAP-28) and its analogs kill pan-drug-resistant Acinetobacter baumannii by interacting with outer membrane protein A (OmpA)","volume":"97","author":"Guo","year":"2018","journal-title":"Medicine"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"19298","DOI":"10.1074\/jbc.271.32.19298","article-title":"Mode of action of the antimicrobial peptide indolicidin","volume":"271","author":"Falla","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"5136","DOI":"10.1128\/AAC.02955-14","article-title":"Comparative mechanistic studies of brilacidin, daptomycin, and the antimicrobial peptide LL16","volume":"58","author":"Mensa","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_221","doi-asserted-by":"crossref","unstructured":"Sader, H.S., Dale, G.E., Rhomberg, P.R., and Flamm, R.K. (2018). Antimicrobial Activity of Murepavadin Tested against Clinical Isolates of Pseudomonas aeruginosa from the United States, Europe, and China. Antimicrob. Agents Chemother., 62.","DOI":"10.1128\/AAC.00311-18"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"41331","DOI":"10.1039\/C8RA08065H","article-title":"Design and characterization of chionodracine-derived antimicrobial peptides with enhanced activity against drug-resistant human pathogens","volume":"8","author":"Olivieri","year":"2018","journal-title":"RSC Adv."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1038\/ki.2011.109","article-title":"Ribonuclease 7 is a potent antimicrobial peptide within the human urinary tract","volume":"80","author":"Spencer","year":"2011","journal-title":"Kidney Int."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1046\/j.1432-1033.2003.03419.x","article-title":"Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major","volume":"270","author":"Iijima","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1016\/j.bbrc.2016.12.035","article-title":"Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity","volume":"482","author":"Panteleev","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_226","doi-asserted-by":"crossref","unstructured":"Lee, E., Shin, A., Jeong, K.W., Jin, B., Jnawali, H.N., Shin, S., Shin, S.Y., and Kim, Y. (2014). Role of phenylalanine and valine10 residues in the antimicrobial activity and cytotoxicity of piscidin-1. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0114453"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.molimm.2012.09.006","article-title":"Endotoxin-neutralizing activity of hen egg phosvitin","volume":"53","author":"Ma","year":"2013","journal-title":"Mol. Immunol."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.peptides.2012.09.001","article-title":"A novel cysteine-rich antimicrobial peptide from the mucus of the snail of Achatina fulica","volume":"39","author":"Zhong","year":"2013","journal-title":"Peptides"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.micpath.2018.05.010","article-title":"Alanine rich peptide from Populus trichocarpa inhibit growth of Staphylococcus aureus via targetting its extracellular domain of Sensor Histidine Kinase YycGex protein","volume":"121","author":"Mateen","year":"2018","journal-title":"Microb. Pathog."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.peptides.2013.04.012","article-title":"Application of S-thanatin, an antimicrobial peptide derived from thanatin, in mouse model of Klebsiella pneumoniae infection","volume":"45","author":"Wu","year":"2013","journal-title":"Peptides"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3389\/fcimb.2016.00194","article-title":"Antimicrobial Peptides: An Emerging Category of Therapeutic Agents","volume":"6","author":"Mahlapuu","year":"2016","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"25742","DOI":"10.1074\/jbc.M116.750257","article-title":"Immunomodulatory and Anti-inflammatory Activity in Vitro and in Vivo of a Novel Antimicrobial Candidate","volume":"291","author":"Brunetti","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.jmii.2016.12.005","article-title":"Antimicrobial peptides as potential anti-biofilm agents against multidrug-resistant bacteria","volume":"50","author":"Chung","year":"2017","journal-title":"J. Microbiol. Immunol. Infect."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"eaay6817","DOI":"10.1126\/sciadv.aay6817","article-title":"Enhanced therapeutic index of an antimicrobial peptide in mice by increasing safety and activity against multidrug-resistant bacteria","volume":"6","author":"Di","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1039\/C9MD00031C","article-title":"Tridecaptin-inspired antimicrobial peptides with activity against multidrug-resistant Gram-negative bacteria","volume":"10","author":"Ballantine","year":"2019","journal-title":"Medchemcomm"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/s11274-020-02907-1","article-title":"Antimicrobial peptide polymers: No escape to ESKAPE pathogens\u2014A review","volume":"36","author":"Mukhopadhyay","year":"2020","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_237","unstructured":"Grumezescu, A.M. (2019). Chapter 8\u2014Nanodrug delivery. Nanomaterials for Drug Delivery and Therapy, William Andrew Publishing."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1021\/acs.biomac.8b00208","article-title":"Synthesis, Self-Assembly, and Biomedical Applications of Antimicrobial Peptide-Polymer Conjugates","volume":"19","author":"Sun","year":"2018","journal-title":"Biomacromolecules"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.3389\/fphar.2019.01153","article-title":"Nanoparticles in the Treatment of Infections Caused by Multidrug-Resistant Organisms","volume":"10","author":"Lee","year":"2019","journal-title":"Front. Pharmacol."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"8211","DOI":"10.2147\/IJN.S132163","article-title":"Nanomaterials for alternative antibacterial therapy","volume":"12","author":"Hemeg","year":"2017","journal-title":"Int. J. Nanomed."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"3322","DOI":"10.1021\/acs.jproteome.6b00489","article-title":"Qualitative Alterations of Bacterial Metabolome after Exposure to Metal Nanoparticles with Bactericidal Properties: A Comprehensive Workflow Based on (1)H NMR, UHPLC-HRMS, and Metabolic Databases","volume":"15","author":"Chatzimitakos","year":"2016","journal-title":"J. Proteome Res."},{"key":"ref_242","first-page":"506","article-title":"Influence of Silver-hydroxyapatite Nanocomposite Coating on Biofilm Formation of Joint Prosthesis and Its Mechanism","volume":"64","author":"Zhao","year":"2015","journal-title":"West Indian Med. J."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1186\/s12951-016-0184-y","article-title":"Exposure to TiO2 nanoparticles increases Staphylococcus aureus infection of HeLa cells","volume":"14","author":"Xu","year":"2016","journal-title":"J. Nanobiotechnol."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"7281","DOI":"10.1038\/s41598-020-64127-9","article-title":"Antimicrobial activity of a silver-microfibrillated cellulose biocomposite against susceptible and resistant bacteria","volume":"10","author":"Dugmore","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1007\/s10876-016-1016-9","article-title":"Biosynthesis, Characterization and Antibacterial Effect of Phenolics-Coated Silver Nanoparticles Using Cassia javanica L.","volume":"27","author":"Bankalgi","year":"2016","journal-title":"J. Clust. Sci."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1007\/s00284-016-1034-8","article-title":"Silver Nanoforms as a Therapeutic Agent for Killing Escherichia coli and Certain ESKAPE Pathogens","volume":"73","author":"Kedziora","year":"2016","journal-title":"Curr. Microbiol."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.3389\/fmicb.2018.01441","article-title":"Nano-Strategies to Fight Multidrug Resistant Bacteria-\u201cA Battle of the Titans\u201d","volume":"9","author":"Baptista","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_248","doi-asserted-by":"crossref","unstructured":"Su, H.L., Lin, S.H., Wei, J.C., Pao, I.C., Chiao, S.H., Huang, C.C., Lin, S.Z., and Lin, J.J. (2011). Novel nanohybrids of silver particles on clay platelets for inhibiting silver-resistant bacteria. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0021125"},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1186\/s12951-014-0040-x","article-title":"Green silver nanoparticles of Phyllanthus amarus: As an antibacterial agent against multi drug resistant clinical isolates of Pseudomonas aeruginosa","volume":"12","author":"Singh","year":"2014","journal-title":"J. Nanobiotechnol."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1002\/jemt.23390","article-title":"Fungal mediated synthesis of silver nanoparticles and evaluation of antibacterial activity","volume":"83","author":"Feroze","year":"2020","journal-title":"Microsc. Res. Tech."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1080\/17435390.2019.1665727","article-title":"Antibacterial properties of silver nanoparticles grown in situ and anchored to titanium dioxide nanotubes on titanium implant against Staphylococcus aureus","volume":"14","author":"Gunputh","year":"2020","journal-title":"Nanotoxicology"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1016\/j.sjbs.2019.12.014","article-title":"Biogenic synthesis of silver nanoparticles: Antibacterial and cytotoxic potential","volume":"27","author":"Algebaly","year":"2020","journal-title":"Saudi J. Biol. Sci."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"206","DOI":"10.2174\/1389201020666191001123219","article-title":"Synergistic Antibacterial Efficacy of Biogenic Synthesized Silver Nanoparticles using Ajuga bractosa with Standard Antibiotics: A Study Against Bacterial Pathogens","volume":"21","author":"Nazer","year":"2020","journal-title":"Curr. Pharm. Biotechnol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.ijpharm.2016.06.121","article-title":"Bactericidal effect of graphene oxide\/Cu\/Ag nanoderivatives against Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae, Staphylococcus aureus and Methicillin-resistant Staphylococcus aureus","volume":"511","author":"Lazauskas","year":"2016","journal-title":"Int. J. Pharm."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"2768","DOI":"10.1128\/AEM.06513-11","article-title":"Nanoparticles functionalized with ampicillin destroy multiple-antibiotic-resistant isolates of Pseudomonas aeruginosa and Enterobacter aerogenes and methicillin-resistant Staphylococcus aureus","volume":"78","author":"Brown","year":"2012","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"12940","DOI":"10.1021\/ja4058635","article-title":"Synergy of non-antibiotic drugs and pyrimidinethiol on gold nanoparticles against superbugs","volume":"135","author":"Zhao","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.colsurfb.2017.10.018","article-title":"Direct one-pot synthesis of cinnamaldehyde immobilized on gold nanoparticles and their antibiofilm properties","volume":"160","author":"Ramasamy","year":"2017","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"5737","DOI":"10.1021\/acsnano.7b01240","article-title":"Pharmaceutical Intermediate-Modified Gold Nanoparticles: Against Multidrug-Resistant Bacteria and Wound-Healing Application via an Electrospun Scaffold","volume":"11","author":"Yang","year":"2017","journal-title":"ACS Nano"},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"e1800854","DOI":"10.1002\/adhm.201800854","article-title":"Gold Nanoparticles with Antibiotic-Metallopolymers toward Broad-Spectrum Antibacterial Effects","volume":"8","author":"Yang","year":"2019","journal-title":"Adv. Healthc. Mater."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"e00698","DOI":"10.1002\/mbo3.698","article-title":"Antibacterial effects and resistance induction of silver and gold nanoparticles against Staphylococcus aureus-induced mastitis and the potential toxicity in rats","volume":"8","author":"Elbehiry","year":"2019","journal-title":"Microbiologyopen"},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"148","DOI":"10.2174\/2211738505666170424121944","article-title":"Antimicrobial, Biofilm Inhibitory and Anti-infective Activity of Metallic Nanoparticles Against Pathogens MRSA and Pseudomonas aeruginosa PA01","volume":"5","author":"Aswathanarayan","year":"2017","journal-title":"Pharm. Nanotechnol."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1111\/lam.12456","article-title":"Inhibition of quorum-sensing-dependent virulence factors and biofilm formation of clinical and environmental Pseudomonas aeruginosa strains by ZnO nanoparticles","volume":"61","author":"Ramasamy","year":"2015","journal-title":"Lett. Appl. Microbiol."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"217","DOI":"10.4161\/viru.2.3.16161","article-title":"Susceptibility of Gram-positive and -negative bacteria to novel nitric oxide-releasing nanoparticle technology","volume":"2","author":"Friedman","year":"2011","journal-title":"Virulence"},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1021\/nn700191f","article-title":"Bactericidal efficacy of nitric oxide-releasing silica nanoparticles","volume":"2","author":"Hetrick","year":"2008","journal-title":"ACS Nano"},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.arabjc.2017.07.004","article-title":"Physical properties, biological applications and biocompatibility studies on biosynthesized single phase cobalt oxide (Co3O4) nanoparticles via Sageretia thea (Osbeck.)","volume":"13","author":"Khalil","year":"2020","journal-title":"Arab. J. Chem."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.scitotenv.2019.05.078","article-title":"Bactericidal effects of metallosurfactants based cobalt oxide\/hydroxide nanoparticles against Staphylococcus aureus","volume":"681","author":"Dogra","year":"2019","journal-title":"Sci. Total Environ."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"43","DOI":"10.15171\/ijb.1138","article-title":"Antimicrobial Effect of Imipenem-Functionalized Fe(2)O(3) Nanoparticles on Pseudomonas aeruginosa Producing Metallo \u03b2-lactamases","volume":"13","author":"Khataminejad","year":"2015","journal-title":"Iran. J. Biotechnol."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1016\/S0140-6736(01)20383-3","article-title":"An investigation on the nature of ultra-microscopic viruses","volume":"186","author":"Twort","year":"1915","journal-title":"Lancet"},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.resmic.2007.07.005","article-title":"On an invisible microbe antagonistic toward dysenteric bacilli: Brief note by Mr. F. D\u2019Herelle, presented by Mr. Roux. 1917","volume":"158","year":"2007","journal-title":"Res. Microbiol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1002\/jobm.201600108","article-title":"Preliminary survey of local bacteriophages with lytic activity against multi-drug resistant bacteria","volume":"56","author":"Latz","year":"2016","journal-title":"J. Basic Microbiol."},{"key":"ref_271","doi-asserted-by":"crossref","unstructured":"Domingo-Calap, P., and Delgado-Mart\u00ednez, J. (2018). Bacteriophages: Protagonists of a Post-Antibiotic Era. Antibiotics, 7.","DOI":"10.3390\/antibiotics7030066"},{"key":"ref_272","doi-asserted-by":"crossref","unstructured":"Pirnay, J.P., Verbeken, G., Ceyssens, P.J., Huys, I., De Vos, D., Ameloot, C., and Fauconnier, A. (2018). The Magistral Phage. Viruses, 10.","DOI":"10.3390\/v10020064"},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"167","DOI":"10.2174\/1874364101509010167","article-title":"Corneal Infection Therapy with Topical Bacteriophage Administration","volume":"9","author":"Fadlallah","year":"2015","journal-title":"Open Ophthalmol. J."},{"key":"ref_274","doi-asserted-by":"crossref","unstructured":"Schooley, R.T., Biswas, B., Gill, J.J., Hernandez-Morales, A., Lancaster, J., Lessor, L., Barr, J.J., Reed, S.L., Rohwer, F., and Benler, S. (2017). Development and Use of Personalized Bacteriophage-Based Therapeutic Cocktails To Treat a Patient with a Disseminated Resistant Acinetobacter baumannii Infection. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.00954-17"},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"S27","DOI":"10.12968\/jowc.2016.25.7.S27","article-title":"Bacteriophage treatment of intransigent diabetic toe ulcers: A case series","volume":"25","author":"Fish","year":"2016","journal-title":"J. Wound Care"},{"key":"ref_276","doi-asserted-by":"crossref","unstructured":"Leitner, L., Sybesma, W., Chanishvili, N., Goderdzishvili, M., Chkhotua, A., Ujmajuridze, A., Schneider, M.P., Sartori, A., Mehnert, U., and Bachmann, L.M. (2017). Bacteriophages for treating urinary tract infections in patients undergoing transurethral resection of the prostate: A randomized, placebo-controlled, double-blind clinical trial. BMC Urol., 17.","DOI":"10.1186\/s12894-017-0283-6"},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.3389\/fmicb.2018.01832","article-title":"Adapted Bacteriophages for Treating Urinary Tract Infections","volume":"9","author":"Ujmajuridze","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1046\/j.1365-4362.2002.01451.x","article-title":"A novel sustained-release matrix based on biodegradable poly(ester amide)s and impregnated with bacteriophages and an antibiotic shows promise in management of infected venous stasis ulcers and other poorly healing wounds","volume":"41","author":"Markoishvili","year":"2002","journal-title":"Int. J. Dermatol."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"769","DOI":"10.2217\/fmb.13.47","article-title":"Phage cocktails and the future of phage therapy","volume":"8","author":"Chan","year":"2013","journal-title":"Future Microbiol."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1089\/sur.2018.184","article-title":"Bacteriophages: A Therapy Concept against Multi-Drug-Resistant Bacteria","volume":"19","author":"Rohde","year":"2018","journal-title":"Surg. Infect."},{"key":"ref_281","doi-asserted-by":"crossref","unstructured":"Casey, E., van Sinderen, D., and Mahony, J. (2018). In Vitro Characteristics of Phages to Guide \u201cReal Life\u201d Phage Therapy Suitability. Viruses, 10.","DOI":"10.3390\/v10040163"},{"key":"ref_282","first-page":"934","article-title":"SLPW: A Virulent Bacteriophage Targeting Methicillin-Resistant Staphylococcus aureus In vitro and In vivo","volume":"7","author":"Wang","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"850","DOI":"10.3389\/fmicb.2018.00850","article-title":"Two New Lytic Bacteriophages of the Myoviridae Family Against Carbapenem-Resistant Acinetobacter baumannii","volume":"9","author":"Zhou","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_284","doi-asserted-by":"crossref","unstructured":"Cooper, C.J., Koonjan, S., and Nilsson, A.S. (2018). Enhancing Whole Phage Therapy and Their Derived Antimicrobial Enzymes through Complex Formulation. Pharmaceuticals, 11.","DOI":"10.3390\/ph11020034"},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"3302","DOI":"10.3389\/fmicb.2018.03302","article-title":"A Novel Phage PD-6A3, and Its Endolysin Ply6A3, With Extended Lytic Activity Against Acinetobacter baumannii","volume":"9","author":"Wu","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.cis.2017.05.014","article-title":"Formulation, stabilisation and encapsulation of bacteriophage for phage therapy","volume":"249","author":"Malik","year":"2017","journal-title":"Adv. Colloid Interface Sci."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1128\/IAI.70.1.204-210.2002","article-title":"Bacteriophage therapy rescues mice bacteremic from a clinical isolate of vancomycin-resistant Enterococcus faecium","volume":"70","author":"Biswas","year":"2002","journal-title":"Infect. Immun."},{"key":"ref_288","doi-asserted-by":"crossref","unstructured":"Manohar, P., Nachimuthu, R., and Lopes, B.S. (2018). The therapeutic potential of bacteriophages targeting gram-negative bacteria using Galleria mellonella infection model. BMC Microbiol., 18.","DOI":"10.1186\/s12866-018-1234-4"},{"key":"ref_289","doi-asserted-by":"crossref","unstructured":"Uchiyama, J., Matsui, H., Murakami, H., Kato, S.I., Watanabe, N., Nasukawa, T., Mizukami, K., Ogata, M., Sakaguchi, M., and Matsuzaki, S. (2018). Potential Application of Bacteriophages in Enrichment Culture for Improved Prenatal Streptococcus agalactiae Screening. Viruses, 10.","DOI":"10.1101\/384222"},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.archoralbio.2016.07.001","article-title":"Effect of a genetically engineered bacteriophage on Enterococcus faecalis biofilms","volume":"71","author":"Tinoco","year":"2016","journal-title":"Arch. Oral Biol."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"2696","DOI":"10.1128\/AEM.00096-15","article-title":"Targeting Enterococcus faecalis biofilms with phage therapy","volume":"81","author":"Khalifa","year":"2015","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.ijantimicag.2019.06.007","article-title":"Lytic bacteriophages against multidrug-resistant Staphylococcus aureus, Enterococcus faecalis and Escherichia coli isolates from orthopaedic implant-associated infections","volume":"54","author":"Barros","year":"2019","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1164\/rccm.201812-2372OC","article-title":"Bacteriophages Improve Outcomes in Experimental Staphylococcus aureus Ventilator-associated Pneumonia","volume":"200","author":"Prazak","year":"2019","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"ref_294","doi-asserted-by":"crossref","unstructured":"Kaur, S., Harjai, K., and Chhibber, S. (2016). In Vivo Assessment of Phage and Linezolid Based Implant Coatings for Treatment of Methicillin Resistant S. aureus (MRSA) Mediated Orthopaedic Device Related Infections. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0157626"},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/s41564-019-0634-z","article-title":"Safety of bacteriophage therapy in severe Staphylococcus aureus infection","volume":"5","author":"Lin","year":"2020","journal-title":"Nat. Microbiol."},{"key":"ref_296","doi-asserted-by":"crossref","unstructured":"Thiry, D., Passet, V., Danis-Wlodarczyk, K., Lood, C., Wagemans, J., De Sordi, L., van Noort, V., Dufour, N., Debarbieux, L., and Mainil, J.G. (2019). New Bacteriophages against Emerging Lineages ST23 and ST258 of Klebsiella pneumoniae and Efficacy Assessment in Galleria mellonella Larvae. Viruses, 11.","DOI":"10.3390\/v11050411"},{"key":"ref_297","doi-asserted-by":"crossref","unstructured":"Patel, D.R., Bhartiya, S.K., Kumar, R., Shukla, V.K., and Nath, G. (2019). Use of Customized Bacteriophages in the Treatment of Chronic Nonhealing Wounds: A Prospective Study. Int. J. Low. Extrem. Wounds.","DOI":"10.1177\/1534734619881076"},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"574","DOI":"10.3389\/fmicb.2019.00574","article-title":"Therapeutic Characterization and Efficacy of Bacteriophage Cocktails Infecting Escherichia coli, Klebsiella pneumoniae, and Enterobacter Species","volume":"10","author":"Manohar","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"293","DOI":"10.4103\/ijmm.IJMM_18_154","article-title":"Oral administration of Klebsiella pneumoniae-specific bacteriophage eradicates the bacteria in albino mice","volume":"36","author":"Chaturvedi","year":"2018","journal-title":"Indian J. Med. Microbiol."},{"key":"ref_300","doi-asserted-by":"crossref","unstructured":"Cano, E.J., Caflisch, K.M., Bollyky, P.L., Van Belleghem, J.D., Patel, R., Fackler, J., Brownstein, M.J., Horne, B., Biswas, B., and Henry, M. (2020). Phage Therapy for Limb-threatening Prosthetic Knee Klebsiella pneumoniae Infection: Case Report and In Vitro Characterization of Anti-biofilm Activity. Clin. Infect. Dis.","DOI":"10.1093\/cid\/ciaa705"},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"1998","DOI":"10.1093\/cid\/ciz782","article-title":"Eradication of a Multidrug-Resistant, Carbapenemase-Producing Klebsiella pneumoniae Isolate Following Oral and Intra-rectal Therapy With a Custom Made, Lytic Bacteriophage Preparation","volume":"70","author":"Corbellino","year":"2020","journal-title":"Clin. Infect. Dis."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1093\/jpids\/pix056","article-title":"Refractory Pseudomonas Bacteremia in a 2-Year-Old Sterilized by Bacteriophage Therapy","volume":"7","author":"Duplessis","year":"2018","journal-title":"J. Pediatr. Infect. Dis. Soc."},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S1473-3099(18)30482-1","article-title":"Efficacy and tolerability of a cocktail of bacteriophages to treat burn wounds infected by Pseudomonas aeruginosa (PhagoBurn): A randomised, controlled, double-blind phase 1\/2 trial","volume":"19","author":"Jault","year":"2019","journal-title":"Lancet Infect. Dis."},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"696","DOI":"10.3389\/fmicb.2018.00696","article-title":"Characterization of Two Novel Bacteriophages Infecting Multidrug-Resistant (MDR) Acinetobacter baumannii and Evaluation of Their Therapeutic Efficacy in Vivo","volume":"9","author":"Cha","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_305","doi-asserted-by":"crossref","unstructured":"Jeon, J., Park, J.H., and Yong, D. (2019). Efficacy of bacteriophage treatment against carbapenem-resistant Acinetobacter baumannii in Galleria mellonella larvae and a mouse model of acute pneumonia. BMC Microbiol., 19.","DOI":"10.1186\/s12866-019-1443-5"},{"key":"ref_306","first-page":"1100","article-title":"Formation of therapeutic phage cocktail and endolysin to highly multi-drug resistant Acinetobacter baumannii: In vitro and in vivo study","volume":"21","author":"Jasim","year":"2018","journal-title":"Iran. J. Basic Med. Sci."},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1164\/rccm.201904-0839LE","article-title":"Bacteriophage Therapy of Ventilator-associated Pneumonia and Empyema Caused by Pseudomonas aeruginosa","volume":"200","author":"Maddocks","year":"2019","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1038\/nbt.3043","article-title":"Exploiting CRISPR-Cas nucleases to produce sequence-specific antimicrobials","volume":"32","author":"Bikard","year":"2014","journal-title":"Nat. Biotechnol."},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"11544","DOI":"10.1038\/s41598-018-29746-3","article-title":"Characterizing the activity of abundant, diverse and active CRISPR-Cas systems in lactobacilli","volume":"8","author":"Crawley","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_310","doi-asserted-by":"crossref","unstructured":"Walker, F.C., and Hatoum-Aslan, A. (2017). Conjugation Assay for Testing CRISPR-Cas Anti-plasmid Immunity in Staphylococci. Bio-Protocol, 7.","DOI":"10.21769\/BioProtoc.2293"},{"key":"ref_311","doi-asserted-by":"crossref","unstructured":"Mangas, E.L., Rubio, A., \u00c1lvarez-Mar\u00edn, R., Labrador-Herrera, G., Pach\u00f3n, J., Pach\u00f3n-Ib\u00e1\u00f1ez, M.E., Divina, F., and P\u00e9rez-Pulido, A.J. (2019). Pangenome of Acinetobacter baumannii uncovers two groups of genomes, one of them with genes involved in CRISPR\/Cas defence systems associated with the absence of plasmids and exclusive genes for biofilm formation. Microb. Genom., 5.","DOI":"10.1099\/mgen.0.000309"},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"1732","DOI":"10.1016\/j.chembiol.2019.09.003","article-title":"A Highly Efficient CRISPR-Cas9-Based Genome Engineering Platform in Acinetobacter baumannii to Understand the H(2)O(2)-Sensing Mechanism of OxyR","volume":"26","author":"Wang","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"578","DOI":"10.3389\/fmicb.2020.00578","article-title":"Exploring the Potential of CRISPR-Cas9 Under Challenging Conditions: Facing High-Copy Plasmids and Counteracting Beta-Lactam Resistance in Clinical Strains of Enterobacteriaceae","volume":"11","author":"Tagliaferri","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_314","doi-asserted-by":"crossref","unstructured":"Sun, Q., Wang, Y., Dong, N., Shen, L., Zhou, H., Hu, Y., Gu, D., Chen, S., Zhang, R., and Ji, Q. (2019). Application of CRISPR\/Cas9-Based Genome Editing in Studying the Mechanism of Pandrug Resistance in Klebsiella pneumoniae. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.00113-19"},{"key":"ref_315","doi-asserted-by":"crossref","unstructured":"Wang, Y., Wang, S., Chen, W., Song, L., Zhang, Y., Shen, Z., Yu, F., Li, M., and Ji, Q. (2018). CRISPR-Cas9 and CRISPR-Assisted Cytidine Deaminase Enable Precise and Efficient Genome Editing in Klebsiella pneumoniae. Appl. Environ. Microbiol., 84.","DOI":"10.1128\/AEM.01834-18"},{"key":"ref_316","doi-asserted-by":"crossref","unstructured":"Hao, M., He, Y., Zhang, H., Liao, X.P., Liu, Y.H., Sun, J., Du, H., Kreiswirth, B.N., and Chen, L. (2020). CRISPR-Cas9-Mediated Carbapenemase Gene and Plasmid Curing in Carbapenem-Resistant Enterobacteriaceae. Antimicrob. Agents Chemother., 64.","DOI":"10.1128\/AAC.00843-20"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1093\/abbs\/gmx074","article-title":"CRISPR\/Cas9-based efficient genome editing in Staphylococcus aureus","volume":"49","author":"Liu","year":"2017","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.isci.2018.07.024","article-title":"CRISPR\/Cas9-based Genome Editing in Pseudomonas aeruginosa and Cytidine Deaminase-Mediated Base Editing in Pseudomonas Species","volume":"6","author":"Chen","year":"2018","journal-title":"iScience"},{"key":"ref_319","doi-asserted-by":"crossref","first-page":"109","DOI":"10.33314\/jnhrc.v17i01.1877","article-title":"Prevalence of Pseudomonas Aeruginosa and its Antibiotic Sensitivity Pattern","volume":"17","author":"Pokharel","year":"2019","journal-title":"J. Nepal Health Res. Counc."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1016\/j.celrep.2019.10.006","article-title":"Native CRISPR-Cas-Mediated Genome Editing Enables Dissecting and Sensitizing Clinical Multidrug-Resistant P. aeruginosa","volume":"29","author":"Xu","year":"2019","journal-title":"Cell Rep."},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.3389\/fimmu.2020.01048","article-title":"Vaccines Against Antimicrobial Resistance","volume":"11","author":"Rosini","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"22332","DOI":"10.1038\/srep22332","article-title":"An Inactivated Antibiotic-Exposed Whole-Cell Vaccine Enhances Bactericidal Activities Against Multidrug-Resistant Acinetobacter baumannii","volume":"6","author":"Shu","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.molimm.2015.07.031","article-title":"Immunological evaluation of OMV(PagL)+Bap(1-487aa) and AbOmpA(8-346aa)+Bap(1-487aa) as vaccine candidates against Acinetobacter baumannii sepsis infection","volume":"67","author":"Badmasti","year":"2015","journal-title":"Mol. Immunol."},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"4153","DOI":"10.1016\/j.vaccine.2018.05.113","article-title":"Immunization with lipopolysaccharide-free outer membrane complexes protects against Acinetobacter baumannii infection","volume":"36","author":"Pulido","year":"2018","journal-title":"Vaccine"},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.micpath.2016.04.019","article-title":"Mucosal immunization with purified OmpA elicited protective immunity against infections caused by multidrug-resistant Acinetobacter baumannii","volume":"96","author":"Zhang","year":"2016","journal-title":"Microb. Pathog."},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"6978","DOI":"10.1016\/j.vaccine.2019.01.076","article-title":"Spontaneously released Neisseria meningitidis outer membrane vesicles as vaccine platform: Production and purification","volume":"37","author":"Gerritzen","year":"2019","journal-title":"Vaccine"},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.micres.2014.09.006","article-title":"Methods of isolation and purification of outer membrane vesicles from gram-negative bacteria","volume":"170","year":"2015","journal-title":"Microbiol. Res."},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1186\/s12934-018-1007-7","article-title":"High dissolved oxygen tension triggers outer membrane vesicle formation by Neisseria meningitidis","volume":"17","author":"Gerritzen","year":"2018","journal-title":"Microb. Cell Fact."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"7131","DOI":"10.7150\/thno.44564","article-title":"Bacterial extracellular vesicle-coated multi-antigenic nanovaccines protect against drug-resistant Staphylococcus aureus infection by modulating antigen processing and presentation pathways","volume":"10","author":"Chen","year":"2020","journal-title":"Theranostics"},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"151415","DOI":"10.1016\/j.ijmm.2020.151415","article-title":"Recombinant N-terminal outer membrane porin (OprF) of Pseudomonas aeruginosa is a promising vaccine candidate against both P. aeruginosa and some strains of Acinetobacter baumannii","volume":"310","author":"Mohamed","year":"2020","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_331","doi-asserted-by":"crossref","unstructured":"Hernandez, D.N., Tam, K., Shopsin, B., Radke, E.E., Law, K., Cardozo, T., Torres, V.J., and Silverman, G.J. (2020). Convergent Evolution of Neutralizing Antibodies to Staphylococcus aureus \u03b3-Hemolysin C That Recognize an Immunodominant Primary Sequence-Dependent B-Cell Epitope. MBio, 11.","DOI":"10.1128\/mBio.00460-20"},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1089\/omi.2019.0183","article-title":"Design of Staphylococcus aureus New Vaccine Candidates with B and T Cell Epitope Mapping, Reverse Vaccinology, and Immunoinformatics","volume":"24","author":"Soltan","year":"2020","journal-title":"OMICS"},{"key":"ref_333","doi-asserted-by":"crossref","unstructured":"Rostamian, M., Farasat, A., Chegene Lorestani, R., Nemati Zargaran, F., Ghadiri, K., and Akya, A. (2020). Immunoinformatics and molecular dynamics studies to predict T-cell-specific epitopes of four Klebsiella pneumoniae fimbriae antigens. J. Biomol. Struct. Dyn.","DOI":"10.1080\/07391102.2020.1810126"},{"key":"ref_334","doi-asserted-by":"crossref","first-page":"4640","DOI":"10.1016\/j.vaccine.2020.03.057","article-title":"Development and evaluation of a new recombinant protein vaccine (YidR) against Klebsiella pneumoniae infection","volume":"38","author":"Rodrigues","year":"2020","journal-title":"Vaccine"},{"key":"ref_335","doi-asserted-by":"crossref","unstructured":"Malachowa, N., Kobayashi, S.D., Porter, A.R., Freedman, B., Hanley, P.W., Lovaglio, J., Saturday, G.A., Gardner, D.J., Scott, D.P., and Griffin, A. (2019). Vaccine Protection against Multidrug-Resistant Klebsiella pneumoniae in a Nonhuman Primate Model of Severe Lower Respiratory Tract Infection. MBio, 10.","DOI":"10.1128\/mBio.02994-19"},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.vaccine.2016.11.032","article-title":"Safety, tolerability, and immunogenicity of a single dose 4-antigen or 3-antigen Staphylococcus aureus vaccine in healthy older adults: Results of a randomised trial","volume":"35","author":"Creech","year":"2017","journal-title":"Vaccine"},{"key":"ref_337","doi-asserted-by":"crossref","unstructured":"Creech, C.B., Frenck, R.W., Fiquet, A., Feldman, R., Kankam, M.K., Pathirana, S., Baber, J., Radley, D., Cooper, D., and Eiden, J. (2019). Persistence of Immune Responses Through 36 Months in Healthy Adults After Vaccination with a Novel Staphylococcus aureus 4-Antigen Vaccine (SA4Ag). Open Forum Infect. Dis., 7.","DOI":"10.1093\/ofid\/ofz532"},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"13973","DOI":"10.1002\/anie.201700964","article-title":"A Semi-Synthetic Glycoconjugate Vaccine Candidate for Carbapenem-Resistant Klebsiella pneumoniae","volume":"56","author":"Seeberger","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"909","DOI":"10.2147\/DDDT.S189847","article-title":"Mechanistic research holds promise for bacterial vaccines and phage therapies for Pseudomonas aeruginosa","volume":"13","author":"Hoggarth","year":"2019","journal-title":"Drug Des. Devel. Ther."},{"key":"ref_340","doi-asserted-by":"crossref","first-page":"3387","DOI":"10.1016\/j.vaccine.2017.05.017","article-title":"Vaccination with a live attenuated Acinetobacter baumannii deficient in thioredoxin provides protection against systemic Acinetobacter infection","volume":"35","author":"Ainsworth","year":"2017","journal-title":"Vaccine"},{"key":"ref_341","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.3389\/fimmu.2018.02315","article-title":"Bacterial Vaccine Antigen Discovery in the Reverse Vaccinology 2.0 Era: Progress and Challenges","volume":"9","author":"Bidmos","year":"2018","journal-title":"Front. Immunol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/22\/8527\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:32:37Z","timestamp":1760178757000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/22\/8527"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11,12]]},"references-count":341,"journal-issue":{"issue":"22","published-online":{"date-parts":[[2020,11]]}},"alternative-id":["ijms21228527"],"URL":"https:\/\/doi.org\/10.3390\/ijms21228527","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,11,12]]}}}