{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T19:44:56Z","timestamp":1789760696177,"version":"4.0.1"},"reference-count":26,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2020,3,23]],"date-time":"2020-03-23T00:00:00Z","timestamp":1584921600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100004325","name":"AstraZeneca","doi-asserted-by":"publisher","award":["Service contract"],"award-info":[{"award-number":["Service contract"]}],"id":[{"id":"10.13039\/100004325","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Class D \u03b2-lactamases exhibit very heterogeneous hydrolysis activity spectra against the various types of clinically useful \u03b2-lactams. Similarly, and according to the available data, their sensitivities to inactivation by avibactam can vary by a factor of more than 100. In this paper, we performed a detailed kinetic study of the interactions between two ceftazidime-hydrolyzing OXA enzymes and showed that they were significantly more susceptible to avibactam than several other class D enzymes that do not hydrolyze ceftazidime. From a clinical point of view, this result is rather interesting if one considers that avibactam is often administered in combination with ceftazidime.<\/jats:p>","DOI":"10.3390\/biom10030483","type":"journal-article","created":{"date-parts":[[2020,3,24]],"date-time":"2020-03-24T13:04:04Z","timestamp":1585055044000},"page":"483","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Interactions between Avibactam and Ceftazidime-Hydrolyzing Class D \u03b2-Lactamases"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8280-9783","authenticated-orcid":false,"given":"Jean-Marie","family":"Fr\u00e8re","sequence":"first","affiliation":[{"name":"Centre for Protein Engineering, University of Li\u00e8ge, B 4000 Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre","family":"Bogaerts","sequence":"additional","affiliation":[{"name":"National Reference Laboratory for Monitoring of Antimicrobial Resistance in Gram-Negative Bacteria, CHU Dinant-Godinne, UCL Namur, B 5530 Yvoir, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Te-Din","family":"Huang","sequence":"additional","affiliation":[{"name":"National Reference Laboratory for Monitoring of Antimicrobial Resistance in Gram-Negative Bacteria, CHU Dinant-Godinne, UCL Namur, B 5530 Yvoir, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"Stefanic","sequence":"additional","affiliation":[{"name":"Centre for Protein Engineering, University of Li\u00e8ge, B 4000 Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00ebl","family":"Moray","sequence":"additional","affiliation":[{"name":"Centre for Protein Engineering, University of Li\u00e8ge, B 4000 Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabrice","family":"Bouillenne","sequence":"additional","affiliation":[{"name":"Centre for Protein Engineering, University of Li\u00e8ge, B 4000 Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alain","family":"Brans","sequence":"additional","affiliation":[{"name":"Centre for Protein Engineering, University of Li\u00e8ge, B 4000 Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,3,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Bush, K. (2018). Past and present perspectives on \u03b2-lactamases. Antimicrob. Agents Chemother., 62.","DOI":"10.1128\/AAC.01076-18"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/s41579-019-0159-8","article-title":"Interplay between \u03b2-lactamases and \u03b2-lactamase inhibitors","volume":"17","author":"Bush","year":"2019","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_3","unstructured":"Fr\u00e8re, J.M. (2012). \u0392-Lactamases, Nova Science Publishers."},{"key":"ref_4","unstructured":"Fr\u00e8re, J.M. (2012). \u03b2-Lactams as Unhibitors of \u03b2-Lactamases in \u0392-Lactamases, Nova Science Publishers."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/S0014-5793(98)01689-5","article-title":"Interaction between class B \u03b2-lactamases and suicide substrates of active-site serine \u03b2-lactamases","volume":"443","author":"Llabres","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3823","DOI":"10.1128\/AAC.05058-14","article-title":"Genetic and biochemical characterization of OXA-405, an OXA-48-type extended-spectrum \u03b2-lactamase without significant carbapenemase activity","volume":"59","author":"Dortet","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1093\/jac\/dku524","article-title":"Heterogeneous hydrolytic features for OXA- 48-like \u03b2-lactamases","volume":"70","author":"Oueslati","year":"2015","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2546","DOI":"10.1128\/AAC.00022-11","article-title":"OXA-163, an OXA-48-related class D \u03b2-lactamase with extended activity toward expanded-spectrum cephalosporins","volume":"55","author":"Poirel","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1128\/JCM.02086-16","article-title":"Noncarbapenemase OXA-48 Variants (OXA-163 and OXA-405) Falsely Detected as Carbapenemases by the \u03b2 Carba Test","volume":"55","author":"Dortet","year":"2017","journal-title":"J. Clin. Microbiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1128\/JCM.02114-16","article-title":"Reply to \u201cNoncarbapenemase OXA-48 Variants (OXA-163 and OXA-405) Falsely Detected as Carbapenemases by the \u03b2 Carba Test\u201d","volume":"55","author":"Arlet","year":"2017","journal-title":"J. Clin. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2832","DOI":"10.1128\/JCM.01175-16","article-title":"Rapid Identification of OXA-48 and OXA-163 Subfamilies in Carbapenem-Resistant Gram-Negative Bacilli with a Novel Immunochromatographic Lateral Flow Assay","volume":"54","author":"Pasteran","year":"2016","journal-title":"J. Clin. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2489","DOI":"10.1128\/JCM.06710-11","article-title":"OXA-163-producing Klebsiella pneumoniae in Cairo, Egypt, in 2009 and 2010","volume":"50","author":"Abdelaziz","year":"2012","journal-title":"J. Clin. Microbiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2469","DOI":"10.1093\/jac\/dkx184","article-title":"OXA-427, a new plasmid-borne carbapenem-hydrolysing class D \u03b2-lactamase in Enterobacteriaceae","volume":"72","author":"Bogaerts","year":"2017","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"e01448","DOI":"10.1128\/AAC.01448-17","article-title":"Antibiotic Resistance Plasmids Cointegrated into a Megaplasmid Harboring the blaOXA-427 Carbapenemase Gene","volume":"62","author":"Desmet","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1007\/s10096-016-2782-x","article-title":"multicenter study group. Increasing incidence of carbapenemase-producing Escherichia coli and Klebsiella pneumoniae in Belgian hospitals","volume":"36","author":"Huang","year":"2017","journal-title":"Eur. J. Clin. Microbiol. Infect. Dis."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"27960","DOI":"10.1074\/jbc.M113.485979","article-title":"Kinetics of avibactam inhibition against Class A, C, and D \u03b2-lactamases","volume":"288","author":"Ehmann","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1021\/cb500703p","article-title":"Molecular basis of selective inhibition and slow reversibility of avibactam against class D carbapenemases: A structure-guided study of OXA-24 and OXA-48","volume":"10","author":"Lahiri","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1556","DOI":"10.1128\/AAC.44.6.1556-1561.2000","article-title":"OXA-24, a novel class D \u03b2-lactamase with carbapenemase activity in an Acinetobacter baumannii clinical strain","volume":"44","author":"Bou","year":"2000","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.1016\/0006-2952(87)90609-5","article-title":"Automated analysis of enzyme inactivation phenomena. Application to -lactamases and D-peptidases","volume":"36","author":"Joris","year":"1987","journal-title":"Biochem. Pharmacol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"e02371","DOI":"10.1128\/AAC.02371-17","article-title":"Probing the Mechanism of Inactivation of the FOX-4 Cephamycinase by Avibactam","volume":"62","author":"Nukaga","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Ruggiero, M., Papp-Wallace, K.M., Taracila, M.A., Mojica, M.F., Bethel, C.R., Rudin, S.D., Zeiser, E.T., Gutkind, G., Bonomo, R.A., and Power, P. (2017). Exploring the Landscape of Diazabicyclooctane (DBO) Inhibition: Avibactam Inactivation of PER-2 \u03b2-Lactamase. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.02476-16"},{"key":"ref_22","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_23","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.jiac.2014.08.028","article-title":"In vitro susceptibility of characterized \u03b2-lactamase-producing Gram-negative bacteria isolated in Japan to ceftazidime-, ceftaroline-, and aztreonam-avibactam combinations","volume":"21","author":"Yoshizumi","year":"2015","journal-title":"J. Infect. Chemother."},{"key":"ref_24","first-page":"e01172","article-title":"Activity of the \u03b2-Lactamase Inhibitor LN-1-255 against Carbapenem-Hydrolyzing Class D \u03b2-Lactamases from Acinetobacter baumannii","volume":"61","author":"Maneiro","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1128\/AAC.37.8.1637","article-title":"OXA-11, an extended- spectrum variant of OXA-10 (PSE-2) \u03b2-lactamase from Pseudomonas aeruginosa","volume":"37","author":"Hall","year":"1993","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"4848","DOI":"10.1128\/AAC.00762-13","article-title":"Structures of the class D Carbapenemases OXA-23 and OXA-146: Mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam","volume":"57","author":"Kaitany","year":"2013","journal-title":"Antimicrob. Agents Chemother."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/10\/3\/483\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:10:39Z","timestamp":1760173839000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/10\/3\/483"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3,23]]},"references-count":26,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2020,3]]}},"alternative-id":["biom10030483"],"URL":"https:\/\/doi.org\/10.3390\/biom10030483","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,3,23]]}}}