{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T11:17:26Z","timestamp":1790680646751,"version":"4.1.0"},"reference-count":238,"publisher":"MDPI AG","issue":"20","license":[{"start":{"date-parts":[[2021,10,19]],"date-time":"2021-10-19T00:00:00Z","timestamp":1634601600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004329","name":"Javna Agencija za Raziskovalno Dejavnost RS","doi-asserted-by":"publisher","award":["P4-0121"],"award-info":[{"award-number":["P4-0121"]}],"id":[{"id":"10.13039\/501100004329","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005989","name":"Ministrstvo za Izobra\u017eevanje, Znanost in \u0160port","doi-asserted-by":"publisher","award":["OP20.03521"],"award-info":[{"award-number":["OP20.03521"]}],"id":[{"id":"10.13039\/501100005989","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Lactoferrins are an iron-binding glycoprotein that have important protective roles in the mammalian body through their numerous functions, which include antimicrobial, antitumor, anti-inflammatory, immunomodulatory, and antioxidant activities. Among these, their antimicrobial activity has been the most studied, although the mechanism behind antimicrobial activities remains to be elucidated. Thirty years ago, the first lactoferrin-derived peptide was isolated and showed higher antimicrobial activity than the native lactoferrin lactoferricin. Since then, numerous studies have investigated the antimicrobial potencies of lactoferrins, lactoferricins, and other lactoferrin-derived peptides to better understand their antimicrobial activities at the molecular level. This review defines the current antibacterial, antiviral, antifungal, and antiparasitic activities of lactoferrins, lactoferricins, and lactoferrin-derived peptides. The primary focus is on their different mechanisms of activity against bacteria, viruses, fungi, and parasites. The role of their structure, amino-acid composition, conformation, charge, hydrophobicity, and other factors that affect their mechanisms of antimicrobial activity are also reviewed.<\/jats:p>","DOI":"10.3390\/ijms222011264","type":"journal-article","created":{"date-parts":[[2021,10,20]],"date-time":"2021-10-20T03:01:13Z","timestamp":1634698873000},"page":"11264","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":177,"title":["Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides"],"prefix":"10.3390","volume":"22","author":[{"given":"\u0160pela","family":"Gruden","sequence":"first","affiliation":[{"name":"Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, 1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2731-9973","authenticated-orcid":false,"given":"Nata\u0161a","family":"Poklar Ulrih","sequence":"additional","affiliation":[{"name":"Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, 1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,10,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3345","DOI":"10.1021\/ja01498a029","article-title":"The isolation of a red protein from milk","volume":"82","author":"Groves","year":"1960","journal-title":"J. Am. Chem. Soc."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"510","DOI":"10.3891\/acta.chem.scand.14-0510","article-title":"Isolation of an iron-containing red protein from human milk","volume":"14","author":"Johansson","year":"1960","journal-title":"Acta Chem. Scand."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/0006-3002(60)91478-5","article-title":"Preparation and properties of lactosiderophilin (lactotransferrin) of human milk","volume":"45","author":"Montreuil","year":"1960","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/0305-0491(71)90258-6","article-title":"Lactoferrin in milk from different species","volume":"39B","author":"Masson","year":"1971","journal-title":"Comp. Biochem. Physiol. B"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/0009-8981(66)90004-0","article-title":"An iron-binding protein common to many external secretions","volume":"14","author":"Masson","year":"1966","journal-title":"Clin. Chim. Acta"},{"key":"ref_6","first-page":"445","article-title":"Lactoferrin from canine neutrophils: Isolation and physicochemical and antimicrobial properties","volume":"72","author":"Berlov","year":"2007","journal-title":"Biochemistry"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1002\/ar.1092210202","article-title":"Neutrophil lactoferrin content: Variation among mammals","volume":"221","author":"Barton","year":"1988","journal-title":"Anat. Rec."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1042\/bj2290353","article-title":"Comparison of human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass; isoelectric point; iron-binding properties and uptake by the liver","volume":"229","author":"Moguilevsky","year":"1985","journal-title":"Biochem. J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.cbpb.2008.02.005","article-title":"Isolation of lactoferrin from milk of different species: Calorimetric and antimicrobial studies","volume":"150","author":"Conesa","year":"2008","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1203\/00006450-198602000-00021","article-title":"Isolation and characterization of Rhesus monkey milk actoferrin","volume":"20","author":"Davidson","year":"1986","journal-title":"Pediatr. Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1084\/jem.131.3.559","article-title":"Association of lactoferrin with specific granules in rabbit heterophil leukocytes","volume":"131","author":"Baggiolini","year":"1970","journal-title":"J. Exp. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/0958-6946(94)00055-7","article-title":"Purification and Characterization of lactoferrin; lactoperoxidase; lysozyme and immunoglobulins from Camel\u2019s Milk","volume":"6","author":"Elagamy","year":"1996","journal-title":"Int. Dairy J."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0304-4165(94)00126-I","article-title":"Isolation and characterization of sheep lactoferrin; an inhibitor of platelet aggregation and comparison with human lactoferrin","volume":"1243","author":"Qian","year":"1995","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/s00435-004-0098-3","article-title":"Secretory and defensive functions of the duct system of the lactating mammary gland of the African elephant (Loxodonta africana; Proboscidea)","volume":"123","author":"Stumpf","year":"2004","journal-title":"Zoomorphology"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"5288","DOI":"10.1093\/nar\/18.17.5288","article-title":"Complete nucleotide sequence of human mammary gland lactoferrin","volume":"18","author":"Rey","year":"1990","journal-title":"Nucleic Acids Res."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1107\/S0907444994013521","article-title":"Structure of human diferric lactoferrin refined at 2.2 A resolution","volume":"51","author":"Haridas","year":"1995","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/jmbi.1997.1386","article-title":"Three-dimensional Structure of Diferric Bovine Lactoferrin at 2.8 A Resolution","volume":"274","author":"Moore","year":"1997","journal-title":"J. Mol. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"7167","DOI":"10.1093\/nar\/18.23.7167","article-title":"cDNA and protein sequence of bovine lactoferrin","volume":"18","author":"Mead","year":"1990","journal-title":"Nucleic Acids Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1111\/j.1432-1033.1991.tb15801.x","article-title":"Molecular cloning and sequence analysis of bovine lactotransferrin","volume":"196","author":"Pierce","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1006\/bbrc.1994.2327","article-title":"Characterization of the goat lactoferrin cDNA: Assignment of the relevant locus to bovine U12 synteny group","volume":"203","author":"Nocart","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1111\/j.1365-2052.1997.00154.x","article-title":"Polymorphic sequence of Korean Native goat lactoferrin exhibiting greater antibacterialactivity","volume":"28","author":"Lee","year":"1997","journal-title":"Anim. Genet."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1006\/jmbi.2001.4692","article-title":"Camel lactoferrin; a transferrin-cum-lactoferrin: Crystal structure of camel apolactoferrin at 2.6 A resolution and structural basis of its dual role","volume":"309","author":"Khan","year":"2001","journal-title":"J. Mol. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1107\/S0907444999010951","article-title":"Structure of buffalo lactoferrin at 2.5 \u00c5 resolution using crystals grown at 303 K shows different orientations of the N and C lobes","volume":"55","author":"Karthikeyan","year":"1999","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_24","first-page":"303","article-title":"Three-dimensional structure of mare diferric lactoferrin at 2.6 \u00c5 resolution","volume":"289","author":"Ashwani","year":"1998","journal-title":"J. Mol. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1111\/j.1365-2052.1992.tb00137.x","article-title":"Cloning and sequencing of the porcine lactoferrin cDNA","volume":"23","author":"Alexander","year":"1992","journal-title":"Anim. Genet."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"10134","DOI":"10.1016\/S0021-9258(18)61088-9","article-title":"Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions","volume":"262","author":"Pentecost","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1073\/pnas.84.7.1769","article-title":"Structure of human lactoferrin at 3.2-A resolution","volume":"84","author":"Anderson","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1016\/0022-2836(89)90602-5","article-title":"Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 A resolution","volume":"209","author":"Anderson","year":"1989","journal-title":"J. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1107\/S0907444900005151","article-title":"Structure of buffalo lactoferrin at 3.3 \u00c5 resolution at 277 K","volume":"56","author":"Karthikeyan","year":"2000","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1007\/s00018-005-5368-9","article-title":"Molecular structure; Binding properties and dynamics of lactoferrin","volume":"62","author":"Baker","year":"2005","journal-title":"Cell Mol. Life Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.biochi.2008.05.006","article-title":"A structural framework for understanding the multifunctionalcharacter of lactoferrin","volume":"91","author":"Baker","year":"2009","journal-title":"Biochimie"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1023\/B:BIOM.0000027694.40260.70","article-title":"Lactoferrin and Iron: Structural and dynamic aspects of binding and release","volume":"17","author":"Baker","year":"2004","journal-title":"Biometals"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4615-2548-6_1","article-title":"Three-dimensional structure of lactoferrin in various functional states","volume":"357","author":"Baker","year":"1994","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1111\/j.1432-1033.1968.tb00484.x","article-title":"Metal-combining properties of human lactoferrin (red milk protein). 1. The involvement of bicarbonate in the reaction","volume":"6","author":"Masson","year":"1968","journal-title":"Eur. J. Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/glycob\/cww086","article-title":"Biological roles of glycans","volume":"27","author":"Varki","year":"2017","journal-title":"Glycobiology"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Karav, S., German, J., Rouqui\u00e9, C., Le Parc, A., and Barile, D. (2017). Studying Lactoferrin N-Glycosylation. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18040870"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1139\/bcb-2020-0106","article-title":"The N-glycans of lactoferrin: More than just a sweet decoration","volume":"99","author":"Zlatina","year":"2021","journal-title":"Biochem. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Bruni, N., Capucchio, M., Biasibetti, E., Pessione, E., Cirrincione, S., Giraudo, L., Corona, A., and Dosio, F. (2016). Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine. Molecules, 21.","DOI":"10.3390\/molecules21060752"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.biochi.2008.05.015","article-title":"Antimicrobial properties of lactoferrin","volume":"91","author":"Jenssen","year":"2009","journal-title":"Biochimie"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Zarzosa Moreno, D., Avalos G\u00f3mez, C., Ram\u00edrez Texcalco, L., Torres L\u00f3pez, E., Ram\u00edrez Mondrag\u00f3n, R., Hern\u00e1ndez Ram\u00edrez, J., Serrano Luna, J., and de la Garza, M. (2020). Lactoferrin and Its Derived Peptides: An Alternative for Combating Virulence Mechanisms Developed by Pathogens. Molecules, 25.","DOI":"10.3390\/molecules25245763"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"6992","DOI":"10.3390\/molecules16086992","article-title":"Antiviral Properties of Lactoferrin\u2014A Natural Immunity Molecule","volume":"16","author":"Berlutti","year":"2011","journal-title":"Molecules"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1016\/j.crvi.2014.08.003","article-title":"Potential lactoferrin activity against pathogenic viruses","volume":"337","author":"Redwan","year":"2014","journal-title":"CR Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1023\/B:BIOM.0000027708.27142.bc","article-title":"Antiviral activity of lactoferrin towards naked viruses","volume":"17","author":"Seganti","year":"2004","journal-title":"Biometals"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2","DOI":"10.3389\/fmicb.2017.00002","article-title":"The Antifungal Activity of Lactoferrin and Its Derived Peptides: Mechanisms of Action and Synergy with Drugs against Fungal Pathogens","volume":"8","author":"Fernandes","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"114","DOI":"10.2174\/187152109787846105","article-title":"Antifungal and Antiparasitic Activities of Lactoferrin","volume":"8","author":"Leboffe","year":"2009","journal-title":"Anti Infect. Agents Med. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Campione, E., Cosio, T., Rosa, L., Lanna, C., Di Girolamo, S., Gaziano, R., Valenti, P., and Bianchi, L. (2020). Lactoferrin as Protective Natural Barrier of Respiratory and Intestinal Mucosa against Coronavirus Infection and Inflammation. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21144903"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"106118","DOI":"10.1016\/j.ijantimicag.2020.106118","article-title":"Lactoferrin as potential preventative and adjunct treatment for COVID-19","volume":"56","author":"Chang","year":"2020","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1021\/acsptsci.0c00059","article-title":"The Potential of Antimicrobial Peptides as an Antiviral Therapy against COVID-19","volume":"3","author":"Elnagdy","year":"2020","journal-title":"ACS Pharmacol. Transl. Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"272","DOI":"10.3892\/etm.2020.9402","article-title":"Lactoferrin for the treatment of COVID-19 (Review)","volume":"20","author":"Wang","year":"2020","journal-title":"Exp. Ther. Med."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"107571","DOI":"10.1016\/j.intimp.2021.107571","article-title":"The potential for Lactoferrin to reduce SARS-CoV-2 induced cytokine storm","volume":"95","author":"Zimecki","year":"2021","journal-title":"Int. Immunopharmacol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1956","DOI":"10.2174\/138161209788453202","article-title":"Lactoferrin as a natural immune modulator","volume":"15","author":"Actor","year":"2009","journal-title":"Curr. Pharm. Des."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Lepanto, M., Rosa, L., Paesano, R., Valenti, P., and Cutone, A. (2019). Lactoferrin in Aseptic and Septic Inflammation. Molecules, 24.","DOI":"10.3390\/molecules24071323"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Rosa, L., Cutone, A., Lepanto, M., Paesano, R., and Valenti, P. (2017). Lactoferrin: A Natural Glycoprotein Involved in Iron and Inflammatory Homeostasis. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18091985"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/aps.2013.200","article-title":"Immunomodulatory effects of lactoferrin","volume":"35","year":"2014","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Cutone, A., Rosa, L., Ianiro, G., Lepanto, M., Bonaccorsi di Patti, M., Valenti, P., and Musci, G. (2020). Lactoferrin\u2019s Anti-Cancer Properties: Safety; Selectivity, and Wide Range of Action. Biomolecules, 10.","DOI":"10.3390\/biom10030456"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1111\/nure.12155","article-title":"Anticancer effects of lactoferrin: Underlying mechanisms and future trends in cancer therapy","volume":"72","author":"Zhang","year":"2014","journal-title":"Nutr. Rev."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0167-4838(92)90346-F","article-title":"Identification of the bactericidal domain of lactoferrin","volume":"1121","author":"Bellamy","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.3168\/jds.S0022-0302(91)78608-6","article-title":"Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin","volume":"74","author":"Tomita","year":"1991","journal-title":"J. Dairy. Sci."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1128\/iai.35.3.792-799.1982","article-title":"Bactericidal activity of human lactoferrin: Differentiation from the stasis of iron deprivation","volume":"35","author":"Arnold","year":"1982","journal-title":"Infect. Immun."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1126\/science.327545","article-title":"A bactericidal effect for human lactoferrin","volume":"197","author":"Arnold","year":"1977","journal-title":"Science"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1128\/iai.61.2.719-728.1993","article-title":"Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment","volume":"61","author":"Yamauchi","year":"1993","journal-title":"Infect. Immun."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2774","DOI":"10.1128\/iai.56.11.2774-2781.1988","article-title":"Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin","volume":"56","author":"Ellison","year":"1988","journal-title":"Infect. Immun."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1099\/00221287-136-7-1437","article-title":"Lactoferrin and transferrin damage of the gram-negative outer membrane is modulated by Ca2+ and Mg2+","volume":"136","author":"Ellison","year":"1990","journal-title":"J. Gen. Microbiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.1172\/JCI115407","article-title":"Killing of gram-negative bacteria by lactoferrin and lysozyme","volume":"88","author":"Ellison","year":"1991","journal-title":"J. Clin. Investig."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1042\/bj3120839","article-title":"Lactoferrin-lipopolysaccharide interaction: Involvement of the 28\u201334 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide","volume":"312","author":"Roseanu","year":"1995","journal-title":"Biochem. J."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1128\/MMBR.67.4.593-656.2003","article-title":"Molecular basis of bacterial outer membrane permeability revisited","volume":"67","author":"Nikaido","year":"2003","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_67","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_68","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1128\/iai.62.6.2628-2632.1994","article-title":"Lactoferrin is a lipid A-binding protein","volume":"62","author":"Appelmelk","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1042\/bj3280145","article-title":"N-terminal stretch Arg2; Arg3; Arg4 and Arg5 of human lactoferrin is essential for binding to heparin; bacterial lipopolysaccharide; human lysozyme and DNA","volume":"328","author":"Geerts","year":"1997","journal-title":"Biochem. J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3387","DOI":"10.1128\/AAC.49.8.3387-3395.2005","article-title":"Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent","volume":"49","author":"Hunter","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1128\/iai.28.3.893-898.1980","article-title":"Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms","volume":"28","author":"Arnold","year":"1980","journal-title":"Infect. Immun."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1128\/iai.32.2.655-660.1981","article-title":"Bactericidal activity of human lactoferrin: Influence of physical conditions and metabolic state of the target microorganism","volume":"32","author":"Arnold","year":"1981","journal-title":"Infect. Immun."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1128\/iai.51.2.373-377.1986","article-title":"Bactericidal effect of lactoferrin on Legionella pneumophila","volume":"51","author":"Bortner","year":"1986","journal-title":"Infect. Immun."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1128\/iai.56.10.2552-2557.1988","article-title":"Killing of Actinobacillus actinomycetemcomitans by human lactoferrin","volume":"56","author":"Kalmar","year":"1988","journal-title":"Infect. Immun."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1134\/S0003683816040116","article-title":"Bovine lactoferrin and its tryptic peptides: Antibacterial activity against different species","volume":"52","author":"Lizzi","year":"2016","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/S0006-291X(81)80014-9","article-title":"Calcium-dependent polymerization of lactoferrin","volume":"101","author":"Bennett","year":"1981","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1128\/mr.56.3.395-411.1992","article-title":"Agents that increase the permeability of the outer membrane","volume":"56","author":"Vaara","year":"1992","journal-title":"Microbiol. Rev."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"9147","DOI":"10.1073\/pnas.0913737107","article-title":"Quantitative determination of ion distributions in bacterial lipopolysaccharide membranes by grazing-incidence X-ray fluorescence","volume":"107","author":"Schnecka","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1021\/la504407v","article-title":"Effect of divalent cation removal on the structure of gram-negative bacterial outer membrane models","volume":"31","author":"Clifton","year":"2015","journal-title":"Langmuir"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/mr.49.1.1-32.1985","article-title":"Molecular basis of bacterial outer membrane permeability","volume":"49","author":"Nikaido","year":"1985","journal-title":"Microbiol. Rev."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1139\/o01-209","article-title":"Ca2+ binding to bovine lactoferrin enhances protein stability and influences the release of bacterial lipopolysaccharide","volume":"80","author":"Rossi","year":"2002","journal-title":"Biochem. Cell. Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1128\/iai.62.4.1236-1240.1994","article-title":"Lactoferrin Binds to Porins OmpF and OmpC in Escherichia coli","volume":"62","author":"Erdei","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1128\/AAC.37.2.240","article-title":"Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium","volume":"37","author":"Naidu","year":"1993","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1007\/s10534-014-9775-y","article-title":"Bactericidal effect of bovine lactoferrin and synthetic peptide lactoferrin chimera in Streptococcus pneumoniae and the decrease in luxS gene expression by lactoferrin","volume":"27","author":"Vidal","year":"2014","journal-title":"Biometals"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Al Mogbel, M., Menezes, G., Elabbasy, M., Alkhulaifi, M., Hossain, A., and Khan, M. (2021). Effect of Synergistic Action of Bovine Lactoferrin with Antibiotics on Drug Resistant Bacterial Pathogens. Medicina, 57.","DOI":"10.3390\/medicina57040343"},{"key":"ref_86","first-page":"42","article-title":"The concerted action of lactoferrin and bacteriophages in the clearance of bacteria in sublethally infected mice","volume":"62","author":"Zimecki","year":"2008","journal-title":"Postepy. High Med. Dosw."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1271\/bbb.64.348","article-title":"Inhibitory effects of bovine lactoferrin on the adherence of enterotoxigenic Escherichia coli to host cells","volume":"64","author":"Kawasaki","year":"2000","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"12641","DOI":"10.1073\/pnas.95.21.12641","article-title":"Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae","volume":"95","author":"Qiu","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_89","unstructured":"De Ara\u00fajo, A., and Giugliano, L. (2001). Lactoferrin and free secretory component of human milk inhibit the adhesion of enteropathogenic Escherichia coli to HeLa cells. BMC Microbiol., 1."},{"key":"ref_90","first-page":"M111.015248","article-title":"Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactation enhancing its role in pathogenic bacteria-host interactions","volume":"11","author":"Barboza","year":"2012","journal-title":"MCP"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.exer.2016.01.013","article-title":"Glycan involvement in the adhesion of Pseudomonas aeruginosa to tears","volume":"145","author":"Kautto","year":"2016","journal-title":"Exp. Eye Res."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"52","DOI":"10.14715\/cmb\/2018.64.9.8","article-title":"Selective deglycosylation of lactoferrin to understand glycans\u2019 contribution to antimicrobial activity of lactoferrin","volume":"64","author":"Karav","year":"2018","journal-title":"Cell. Mol. Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1093\/jn\/131.8.2121","article-title":"Functional fragments of ingested lactoferrin are resistant to proteolytic degradation in the gastrointestinal tract of adult rats","volume":"131","author":"Yamauchi","year":"2001","journal-title":"J. Nutr."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0167-4838(98)00224-6","article-title":"Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin","volume":"1429","author":"Kuwata","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"75","DOI":"10.3168\/jds.2012-5946","article-title":"Identification of lactoferrin peptides generated by digestion with human gastrointestinal enzymes","volume":"96","author":"Furlund","year":"2013","journal-title":"J. Dairy Sci."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"65","DOI":"10.3168\/jds.S0022-0302(91)78144-7","article-title":"Heat stability of bovine lactoferrin at acidic pH","volume":"74","author":"Abe","year":"1990","journal-title":"J. Dairy Sci."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.3168\/jds.S0022-0302(91)78563-9","article-title":"Potent bactericidal activity of bovine lactoferrin hydrolysate produced by heat treatment at acidic pH","volume":"74","author":"Saito","year":"1991","journal-title":"J. Dairy Sci."},{"key":"ref_98","first-page":"513","article-title":"Lactoferricin of bovine origin is more active than lactoferricins of human; murine and caprine origin. Scand","volume":"30","author":"Vorland","year":"1998","journal-title":"J. Infect. Dis."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1021\/jf053031s","article-title":"Synthetic porcine lactoferricin with a 20-residue peptide exhibits antimicrobial activity against Escherichia coli; Staphylococcus aureus; and Candida albicans","volume":"54","author":"Chen","year":"2006","journal-title":"J. Agric. Food. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1111\/j.1365-2672.1992.tb05007.x","article-title":"Antibacterial spectrum of lactoferricin B; A potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin","volume":"73","author":"Bellamy","year":"1992","journal-title":"J. Appl. Bacteriol."},{"key":"ref_101","first-page":"377","article-title":"Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis","volume":"237","author":"Ulvatne","year":"2004","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"2197","DOI":"10.1016\/j.bbamem.2011.05.001","article-title":"Structural basis for the enhanced activity of cyclic antimicrobial peptides: The case of BPC194","volume":"1808","author":"Mika","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"4288","DOI":"10.1021\/bi972323m","article-title":"Three-dimensional solution structure of lactoferricin B; an antimicrobial peptide derived from bovine lactoferrin","volume":"37","author":"Hwang","year":"1998","journal-title":"Biochemistry"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2190","DOI":"10.1128\/AAC.48.6.2190-2198.2004","article-title":"Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide","volume":"48","author":"Chapple","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/j.1574-6968.2004.tb09759.x","article-title":"Variation in antimicrobial activity of lactoferricin-derived peptides explained by structure modelling","volume":"238","author":"Farnaud","year":"2004","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1007\/s12602-020-09726-8","article-title":"Secondary structural transformation of bovine lactoferricin affects its antibacterial activity","volume":"13","author":"Pei","year":"2021","journal-title":"Probiotics Antimicrob. Proteins"},{"key":"ref_107","first-page":"179","article-title":"Antibacterial effects of lactoferricin B. Scand","volume":"31","author":"Vorland","year":"1999","journal-title":"J. Infect. Dis."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1002\/psc.318","article-title":"The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide","volume":"7","author":"Haug","year":"2001","journal-title":"J. Pept. Sci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1111\/j.1574-6968.2004.tb09482.x","article-title":"Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity","volume":"233","author":"Farnaud","year":"2004","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1007\/s10534-011-9465-y","article-title":"Comparative antimicrobial activity and mechanism of action of bovine lactoferricin-derived synthetic peptides","volume":"24","author":"Liu","year":"2011","journal-title":"Biometals"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1080\/00365540110026692","article-title":"Bactericidal kinetics of 3 lactoferricins against Staphylococcus aureus and Escherichia coli","volume":"33","author":"Ulvatne","year":"2001","journal-title":"Scand. J. Infect. Dis."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1111\/j.1399-3011.1996.tb00852.x","article-title":"Structure-biological activity relationships of 1 1-residue highly basic peptide segment of bovine lactoferrin","volume":"48","author":"Kang","year":"1996","journal-title":"Int. J. Pept. Protein Res."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1002\/psc.629","article-title":"Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin","volume":"11","author":"Nguyen","year":"2005","journal-title":"J. Pept. Sci."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1111\/j.1365-2672.2006.03089.x","article-title":"Activity and mode of action against fungal phytopathogens of bovine lactoferricin-derived peptides","volume":"101","author":"Munoz","year":"2006","journal-title":"J. Appl. Microbiol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.peptides.2003.08.023","article-title":"The relationship between peptide structure and antibacterial activity","volume":"24","author":"Powers","year":"2003","journal-title":"Peptides"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"691532","DOI":"10.3389\/fchem.2021.691532","article-title":"Antimicrobial Peptides and Proteins: From Nature\u2019s Reservoir to the Laboratory and Beyond","volume":"9","author":"Sarkar","year":"2021","journal-title":"Front. Chem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1034\/j.1399-3011.2000.00770.x","article-title":"Antibacterial activity of 15-residue lactoferricin derivatives","volume":"56","author":"Rekdal","year":"2000","journal-title":"J. Pept. Res."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"44278","DOI":"10.1038\/srep44278","article-title":"Killing of Staphylococcus aureus and Salmonella enteritidis and neutralization of lipopolysaccharide by 17-residue bovine lactoferricins: Improved activity of Trp\/Ala-containing molecules","volume":"7","author":"Hao","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Huertas M\u00e9ndez, N.J., Vargas Casanova, Y., G\u00f3mez Chimbi, A.K., Hern\u00e1ndez, E., Leal Castro, A.L., Melo Diaz, J.M., Rivera Monroy, Z.J., and Garc\u00eda Casta\u00f1eda, J.E. (2017). Synthetic peptides derived from bovine lactoferricin exhibit antimicrobial activity against E. coli ATCC 11775, S. maltophilia ATCC 13636 and S. enteritidis ATCC 13076. Molecules, 22.","DOI":"10.3390\/molecules22030452"},{"key":"ref_120","first-page":"453826","article-title":"Antibacterial activity of synthetic peptides derived from lactoferricin against Escherichia coli ATCC 25922 and Enterococcus faecalis ATCC 29212","volume":"2015","year":"2015","journal-title":"Biomed. Res. Int."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1523","DOI":"10.1016\/j.bbamem.2006.06.014","article-title":"Interactions of bovine lactoferricin with acidic phospholipid bilayers and its antimicrobial activity as studied by solid-state NMR","volume":"1758","author":"Umeyama","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1093\/jmicro\/52.2.207","article-title":"Ultrastructural and cytochemical study of cell wall modification by lactoferrin; lactoferricin and penicillin G against Staphylococcus aureus","volume":"52","author":"Diarra","year":"2003","journal-title":"J. Electron. Microsc."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/S0014-5793(01)02233-5","article-title":"Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes","volume":"492","author":"Ulvatne","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1080\/00365549950163987","article-title":"Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli","volume":"31","author":"Vorland","year":"1999","journal-title":"Scand. J. Infect. Dis."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/S0014-5793(01)03100-3","article-title":"The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm","volume":"508","author":"Hauklanda","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"M111.014720","DOI":"10.1074\/mcp.M111.014720","article-title":"Lactoferricin B inhibits the phosphorylation of the two-component system response regulators BasR and CreB","volume":"11","author":"Ho","year":"2012","journal-title":"Mol. Cell. Proteom."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1007\/BF02490180","article-title":"Antibacterial effects of lactoferrin and a pepsin-generated lactoferrin peptide against Helicobacter pylori in vitro","volume":"3","author":"Yamazaki","year":"1997","journal-title":"J. Infect. Chemother."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.1128\/iai.58.11.3724-3730.1990","article-title":"Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins","volume":"58","author":"Skerlavaj","year":"1990","journal-title":"Infect. Immun."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1128\/AAC.7.5.596","article-title":"Effect of calcium and magnesium ions on the susceptibility of Pseudomonas species to tetracycline; gentamicin polymyxin B, and carbenicillin","volume":"7","author":"Thornsberry","year":"1975","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Zhang, R., Fan, X., Jiang, X., Zou, M., Xiao, H., and Wu, G. (2020). Multiple mechanisms of the synthesized antimicrobial peptide TS against Gram-negative bacteria for high efficacy antibacterial action in vivo. Molecules, 26.","DOI":"10.3390\/molecules26010060"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1177\/00220345870660021601","article-title":"Characterization of lactoferrin interaction with Streptococcus mutans","volume":"66","author":"Lassiter","year":"1987","journal-title":"J. Dent. Res."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"667","DOI":"10.3168\/jds.S0022-0302(97)75985-X","article-title":"Antibacterial peptides of bovine lactoferrin: Purification and characterization","volume":"80","author":"Dionysius","year":"1997","journal-title":"J. Dairy Sci."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0021-9673(98)00950-9","article-title":"Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin In situ enzymatic hydrolysis on an ion-exchange membrane","volume":"831","author":"Recio","year":"1999","journal-title":"J. Chromatogr. A"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"487","DOI":"10.5851\/kosfa.2016.36.4.487","article-title":"Sensitivity of Pseudomonas syringae to bovine lactoferrin hydrolysates and identification of a novel inhibitory peptide","volume":"36","author":"Kim","year":"2016","journal-title":"Korean J. Food. Sci. Anim. Resour."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Rastogi, N., Nagpal, N., Alam, H., Pandey, S., Gautam, L., Sinha, M., Shin, K., Manzoor, N., Virdi, J.S., and Kaur, P. (2014). Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0090011"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1128\/AAC.41.1.54","article-title":"Antibacterial activity in bovine lactoferrin-derived peptides","volume":"41","author":"Hoek","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.biochi.2008.05.019","article-title":"Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides","volume":"91","author":"Bolscher","year":"2009","journal-title":"Biochimie"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1038\/nbt1267","article-title":"Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies","volume":"24","author":"Hancock","year":"2006","journal-title":"Nat. Biotechnol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.peptides.2003.12.006","article-title":"Lactoferrampin: A novel antimicrobial peptide in the N1-domain of bovine lactoferrin","volume":"25","author":"Groenink","year":"2004","journal-title":"Peptides"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.peptides.2005.06.012","article-title":"A one-enzyme strategy to release an antimicrobial peptide from the LFampin-domain of bovine lactoferrin","volume":"27","author":"Bolscher","year":"2006","journal-title":"Peptides"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.biochi.2008.04.013","article-title":"Novel lactoferrampin antimicrobial peptides derived from human lactoferrin","volume":"91","author":"Haney","year":"2009","journal-title":"Biochimie"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.biochi.2008.06.009","article-title":"Bactericidal effect of lactoferrin and lactoferrin chimera against halophilic Vibrio parahaemolyticus","volume":"91","author":"ReyesLopez","year":"2009","journal-title":"Biochimie"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1007\/s10534-018-0136-0","article-title":"LFchimera protects HeLa cells from invasion by Yersinia spp. in vitro","volume":"31","author":"Sijbrandij","year":"2018","journal-title":"Biometals"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1007\/s11274-013-1284-6","article-title":"A heterodimer comprised of two bovine lactoferrin antimicrobial peptides exhibits powerful bactericidal activity against Burkholderia pseudomallei","volume":"29","author":"Puknun","year":"2013","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1016\/j.bbamem.2011.11.023","article-title":"Structural and biophysical characterization of an antimicrobial peptide chimera comprised of lactoferricin and lactoferrampin","volume":"1818","author":"Haney","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0166-3542(02)00214-0","article-title":"Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir","volume":"58","author":"Andersen","year":"2003","journal-title":"Antiviral. Res."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1007\/s10534-010-9323-3","article-title":"Bovine lactoferrin inhibits Influenza A virus induced programmed cell death in vitro","volume":"23","author":"Pietrantoni","year":"2010","journal-title":"Biometals"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.ijantimicag.2005.02.011","article-title":"Inhibitory activity of bovine lactoferrin against echovirus induced programmed cell death in vitro","volume":"25","author":"Tinari","year":"2005","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1179\/2047773212Y.0000000004","article-title":"Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus","volume":"106","author":"Ammendolia","year":"2012","journal-title":"Pathog. Glob. Health"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1006\/bbrc.1998.8481","article-title":"Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes","volume":"245","author":"Ikeda","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/S1386-6346(02)00088-8","article-title":"Lactoferrin inhibits hepatitis B virus infection in cultured human hepatocytes","volume":"24","author":"Hara","year":"2002","journal-title":"Hepatol. Res."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1002\/jmv.20171","article-title":"Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface","volume":"74","author":"Andersen","year":"2004","journal-title":"J. Med. Virol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1007\/BF01322673","article-title":"Lactoferrin inhibits herpes simplex virus type-1 (HSV-1) infection to mouse cornea","volume":"140","author":"Fujihara","year":"1995","journal-title":"Arch. Virol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"73","DOI":"10.7883\/yoken1952.47.73","article-title":"Inhibition with lactoferrin of in vitro infection with human herpes virus","volume":"47","author":"Hasegawa","year":"1994","journal-title":"Jpn. J. Med. Sci. Biol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/0166-3542(95)00840-3","article-title":"Lactoferrin inhibits herpes simplex virus type 1 adsorption to Vero cells","volume":"29","author":"Marchetti","year":"1996","journal-title":"Antiviral. Res."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.virol.2003.09.029","article-title":"Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans","volume":"318","author":"Marchetti","year":"2004","journal-title":"Virology"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Superti, F., Agamennone, M., Pietrantoni, A., and Ammendolia, M.G. (2019). Bovine lactoferrin prevents influenza A virus infection by interfering with the fusogenic function of viral hemagglutinin. Viruses, 11.","DOI":"10.3390\/v11010051"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0166-3542(01)00146-2","article-title":"Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fi broblasts","volume":"51","author":"Andersen","year":"2001","journal-title":"Antiviral. Res."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1093\/infdis\/172.2.380","article-title":"Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro","volume":"172","author":"Harmsen","year":"1995","journal-title":"J. Infect. Dis."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/S0166-3542(02)00069-4","article-title":"Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and proteinderived peptides","volume":"55","author":"Berkhout","year":"2002","journal-title":"Antiviral. Res."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/S1357-2725(98)00066-1","article-title":"Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection","volume":"30","author":"Puddu","year":"1998","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1089\/aid.1996.12.769","article-title":"Antiviral effects of milk proteins: Acylation results in polyanionic compounds with potent activity against human immunodeficiency virus types 1 and 2 in vitro","volume":"12","author":"Swart","year":"1996","journal-title":"AIDS Res. Hum. Retrovir."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0166-3542(01)00197-8","article-title":"Antiadenovirus activity of milk proteins: Lactoferrin prevents viral infection","volume":"53","author":"Arnold","year":"2002","journal-title":"Antiviral. Res."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1002\/jmv.10337","article-title":"Heparin-interacting sites of bovine lactoferrin are involved in anti-adenovirus activity","volume":"69","author":"Pietrantoni","year":"2003","journal-title":"J. Med. Virol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1128\/AAC.47.8.2688-2691.2003","article-title":"Bovine lactoferrin inhibits adenovirus infection by interacting with viral structural polypeptides","volume":"47","author":"Pietrantoni","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.antiviral.2004.05.005","article-title":"Lactoferrin inhibits human papillomavirus binding and uptake in vitro","volume":"64","author":"Drobni","year":"2004","journal-title":"Antiviral. Res."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.antiviral.2007.03.012","article-title":"The anti-papillomavirus activity of human and bovine lactoferricin","volume":"75","author":"Mistry","year":"2007","journal-title":"Antiviral. Res."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s004300050093","article-title":"Inhibition of poliovirus type 1 infection by iron-manganeseand zinc-saturated lactoferrin","volume":"187","author":"Marchetti","year":"1999","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.antiviral.2005.10.006","article-title":"Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection","volume":"69","author":"Pietrantoni","year":"2006","journal-title":"Antiviral. Res."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/s004300050049","article-title":"Antirotaviral activity of milk proteins: Lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29","volume":"186","author":"Superti","year":"1997","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1046\/j.1365-2672.2003.02071.x","article-title":"The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures","volume":"95","author":"McCann","year":"2003","journal-title":"J. Appl. Microbiol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.biochi.2008.05.016","article-title":"Bovine lactoferrin and lactoferricin interfere with intracellular trafficking of Herpes simplex virus-1","volume":"91","author":"Marr","year":"2009","journal-title":"Biochimie"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.antiviral.2007.07.005","article-title":"Bovine lactoferrin prevents the entry and intercellular spread of herpes simplex virus type 1 in Green Monkey Kidney cells","volume":"76","author":"Ammendolia","year":"2007","journal-title":"Antiviral. Res."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1186\/1743-422X-7-330","article-title":"Effectiveness of esterified whey proteins fractions against Egyptian Lethal Avian Influenza A (H5N1)","volume":"7","author":"Taha","year":"2010","journal-title":"Virol. J."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"2717","DOI":"10.1093\/emboj\/cdg279","article-title":"Caspase 3 activation is essential for efficient influenza virus propagation","volume":"22","author":"Wurzer","year":"2003","journal-title":"EMBO J."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/289366a0","article-title":"Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 \u00c5 resolution","volume":"289","author":"Wilson","year":"1981","journal-title":"Nature"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.3389\/fimmu.2018.01581","article-title":"Influenza A virus cell entry; replication; virion assembly and movement","volume":"9","author":"Dou","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"10593","DOI":"10.1038\/s41598-017-10492-x","article-title":"Lactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors","volume":"7","author":"Scala","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_179","first-page":"17006","article-title":"Hepatitis C virus infection","volume":"3","author":"Manns","year":"2017","journal-title":"Nat. Rev."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"10162","DOI":"10.1074\/jbc.M207879200","article-title":"Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein","volume":"278","author":"Nozaki","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"5997","DOI":"10.1128\/jvi.71.8.5997-6002.1997","article-title":"Hepatitis C Virus Envelope Proteins Bind Lactoferrin","volume":"71","author":"Yi","year":"1994","journal-title":"J. Virol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1006\/bbrc.1999.1318","article-title":"Bovine lactoferrin peptidic fragments involved in inhibition of herpes simplex virus type 1 infection","volume":"264","author":"Siciliano","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"617578","DOI":"10.3389\/fcimb.2020.617578","article-title":"Herpes simplex virus cell entry mechanisms: An update","volume":"10","author":"Madavaraju","year":"2021","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1161\/01.ATV.14.12.2025","article-title":"Lactoferrin binding to heparan sulfate proteoglycans and the LDL receptor-related protein. Further evidence supporting the importance of direct binding of remnant lipoproteins to HSPG","volume":"14","author":"Ji","year":"1994","journal-title":"Arterioscler. Thromb."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.peptides.2014.07.006","article-title":"A study of effects of peptide fragments of bovine and human lactoferrins on activities of three key HIV-1 enzymes","volume":"62","author":"Wong","year":"2014","journal-title":"Peptides"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.3390\/v4061011","article-title":"Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike","volume":"4","author":"Belouzard","year":"2012","journal-title":"Protein Viruses"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"14451","DOI":"10.1128\/JVI.79.22.14451-14456.2005","article-title":"Murine Coronavirus with an Extended Host Range Uses Heparan Sulfate as an Entry Receptor","volume":"79","author":"Li","year":"2005","journal-title":"J. Virol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"13221","DOI":"10.1128\/JVI.02078-14","article-title":"Human Coronavirus NL63 Utilizes Heparan Sulfate Proteoglycans for Attachment to Target Cells","volume":"88","author":"Milewskaa","year":"2014","journal-title":"J. Virol."},{"key":"ref_189","doi-asserted-by":"crossref","unstructured":"Lang, J., Yang, N., Deng, J., Liu, K., Yang, P., Zhang, G., and Jiang, C. (2011). Inhibition of SARS Pseudovirus Cell Entry by Lactoferrin Binding to Heparan Sulfate Proteoglycans. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0023710"},{"key":"ref_190","first-page":"8","article-title":"Liposomal Lactoferrin as Potential Preventative and Cure for COVID-19","volume":"8","author":"Serrano","year":"2020","journal-title":"Int. J. Res. Health Sci."},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Salaris, C., Scarpa, M., Elli, M., Bertolini, A., Guglielmetti, S., Pregliasco, F., Blandizzi, C., Brun, P., and Castagliuolo, I. (2021). Protective Effects of Lactoferrin against SARS-CoV-2 Infection In Vitro. Nutrients, 13.","DOI":"10.3390\/nu13020328"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"666600","DOI":"10.3389\/fphar.2021.666600","article-title":"Lactoferrin Against SARS-CoV-2: In Vitro and In Silico Evidences","volume":"12","author":"Campione","year":"2021","journal-title":"Front. Pharmacol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1080\/22221751.2021.1888660","article-title":"The in vitro antiviral activity of lactoferrin against common human coronaviruses and SARS-CoV-2 is mediated by targeting the heparan sulfate co-receptor","volume":"10","author":"Hu","year":"2021","journal-title":"Emerg. Microbes Infect."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"e2105815118","DOI":"10.1073\/pnas.2105815118","article-title":"Morphological cell profiling of SARS-CoV-2 infection identifies drug repurposing candidates for COVID-19","volume":"118","author":"Mirabellia","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1128\/JVI.01995-06","article-title":"Adenoviruses use lactoferrin as a bridge for CAR-independent binding to and infection of epithelial cells","volume":"81","author":"Johansson","year":"2007","journal-title":"J. Virol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1099\/vir.0.008342-0","article-title":"Adenovirus serotype 5 infects human dendritic cells via a coxsackievirus\u2013adenovirus receptorindependent receptor pathway mediated by lactoferrin and DC-SIGN","volume":"90","author":"Adams","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_197","doi-asserted-by":"crossref","unstructured":"Ch\u00e9neau, C., Eichholz, K., Tran, T.H., Tran, T.T., Paris, O., Henriquet, C., Pugni\u00e8re, M., and Kremer, E. (2020). Lactoferrin retargets adenoviruses to TLR4 to induce an abortive NLRP3-associated pyroptotic response in human dendritic cells. bioRxiv.","DOI":"10.1101\/2020.06.03.131664"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S0304-4165(01)00178-7","article-title":"Involvement of bovine lactoferrin metal saturation; sialic acid and protein fragments in the inhibition of rotavirus infection","volume":"1528","author":"Superti","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1093\/infdis\/124.6.539","article-title":"Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: Relation to host-defense mechanisms in chronic mucocutaneous candidiasis","volume":"124","author":"Kirkpatrick","year":"1971","journal-title":"J. Infect. Dis."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1016\/0003-9969(93)90167-K","article-title":"The fungicidal effect of human lactoferrin on Candida albicans and Candida krusei","volume":"38","author":"Nikawa","year":"1993","journal-title":"Arch. Oral Biol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1111\/j.1574-6968.1992.tb05156.x","article-title":"Fungicidal effect of human lactoferrin against Candida albicans","volume":"90","author":"Soukka","year":"1992","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/BF00189377","article-title":"Killing of Candida albicans by lactoferricin B; a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin","volume":"182","author":"Bellamy","year":"1993","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1007\/BF02350646","article-title":"Antifungal spectrum and fungicidal mechanism of an N-terminal peptide of bovine lactoferrin","volume":"1","author":"Wakabayash","year":"1996","journal-title":"J. Infect. Chemother."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1111\/j.1472-765X.1994.tb00854.x","article-title":"Antifungal properties of lactoferricin B; a peptide derived from the N-terminal region of bovine lactoferrin","volume":"18","author":"Bellamy","year":"1994","journal-title":"Lett. Appl. Microbiol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1111\/j.1399-3011.2001.00821.x","article-title":"A novel bovine lactoferrin peptide; FKCRRWQWRM; suppresses Candida cell growth and activates neutrophils","volume":"57","author":"Ueta","year":"2001","journal-title":"J. Pept. Res."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Morici, P., Fais, R., Rizzato, C., Tavanti, A., and Lupetti, A. (2016). Inhibition of Candida albicans biofilm formation by the synthetic lactoferricin derived peptide hLF1-11. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0167470"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1515\/BC.2005.017","article-title":"Lactoferrampin, an antimicrobial peptide of bovine lactoferrin; exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part","volume":"386","author":"Nazmi","year":"2005","journal-title":"Biol. Chem."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"710","DOI":"10.4269\/ajtmh.2005.73.710","article-title":"Inhibitory effect of lactoferrin on in vitro growth of Babesia caballi","volume":"73","author":"Ikadai","year":"2005","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/S0169-4758(98)01294-0","article-title":"Iron acquisition by parasitic protozoa","volume":"14","author":"Wilson","year":"1998","journal-title":"Parasitol. Today"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"4550","DOI":"10.1128\/iai.63.11.4550-4552.1995","article-title":"Giardicidal activity of lactoferrin and N-terminal peptides","volume":"63","author":"Turchany","year":"1995","journal-title":"Infect. Immun."},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Frontera, L., Moyano, S., Quassollo, G., Lanfredi Rangel, A., R\u00f3polo, A., and Touz, M. (2018). Lactoferrin and lactoferricin endocytosis halt Giardia cell growth and prevent infective cyst production. Sci. Rep., 1\u201315.","DOI":"10.1038\/s41598-018-36563-1"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1139\/bcb-2016-0079","article-title":"Parasiticidal effect of synthetic bovine lactoferrin peptides on the enteric parasite Giardia intestinalis","volume":"95","author":"Nazmi","year":"2017","journal-title":"Biochem. Cell Biol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1111\/j.1550-7408.1997.tb05694.x","article-title":"Ultrastructural effects of lactoferrin binding on Giardia lamblia trophozoites","volume":"44","author":"Turchany","year":"1997","journal-title":"J. Eukaryot. Microbiol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"774","DOI":"10.4269\/ajtmh.16-0804","article-title":"Killing of Cryptosporidium sporozoites by Lactoferrin","volume":"97","author":"Paredes","year":"2017","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1126\/science.184.4140.952","article-title":"Iron and Susceptibility to Infectious Disease","volume":"184","author":"Weinberg","year":"1974","journal-title":"Science"},{"key":"ref_216","doi-asserted-by":"crossref","unstructured":"Sehgal, R., Goyal, K., and Sehgal, A. (2012). Trichomoniasis and lactoferrin: Future prospects. Infect. Dis. Obstet. Gynecol., 1\u20138.","DOI":"10.1155\/2012\/536037"},{"key":"ref_217","doi-asserted-by":"crossref","unstructured":"Kariuki, C., Stijlemans, B., and Magez, S. (2019). The Trypanosomal Transferrin Receptor of Trypanosoma Brucei\u2014A Review. Trop. Med. Infect. Dis., 4.","DOI":"10.3390\/tropicalmed4040126"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1006\/expr.1996.0068","article-title":"Tritrichomonas foetus: Iron acquisition from lactoferrin and transferrin","volume":"83","author":"Tachezy","year":"1996","journal-title":"Exp. Parasitol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"3262","DOI":"10.1128\/iai.62.8.3262-3269.1994","article-title":"Acquisition of iron from transferrin and lactoferrin by the protozoan Leishmania chagasi","volume":"62","author":"Wilson","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/S0014-4894(02)00018-8","article-title":"Leishmania chagasi: Uptake of iron bound to lactoferrin or transferrin requires an iron reductase","volume":"100","author":"Wilson","year":"2002","journal-title":"Exp. Parasitol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1292\/jvms.66.619","article-title":"The detection of bovine lactoferrin binding protein on Trypanosoma brucei","volume":"66","author":"Tanaka","year":"2004","journal-title":"J. Vet. Med. Sci."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1292\/jvms.65.1377","article-title":"The detection of bovine lactoferrin binding protein on Toxoplasma gondii","volume":"65","author":"Tanaka","year":"2003","journal-title":"J. Vet. Med. Sci."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.exppara.2006.09.012","article-title":"Identification of Toxoplasma gondii proteins binding human lactoferrin: A new aspect of rhoptry proteins function","volume":"115","author":"Dziadek","year":"2007","journal-title":"Exp. Parasitol."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.exppara.2005.03.019","article-title":"Toxoplasma gondii binds human lactoferrin but not transferrin","volume":"110","author":"Dziadek","year":"2005","journal-title":"Exp. Parasitol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1006\/expr.1995.1157","article-title":"Toxoplasma gondii: Parasiticidal effects of bovine lactoferricin against parasites","volume":"81","author":"Tanaka","year":"1995","journal-title":"Exp. Parasitol."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1292\/jvms.58.61","article-title":"Growth Inhibitory Effects of Bovine Lactoferrin to Toxoplasma gondii Parasites in Murine Somatic Cells","volume":"58","author":"Tanak","year":"1996","journal-title":"J. Vet. Med. Sci."},{"key":"ref_227","first-page":"25","article-title":"Toxoplasma gondii: Inhibition of the Intracellular Growth by Human Lactoferrin","volume":"56","author":"Dzitko","year":"2007","journal-title":"Pol. J. Microbiol."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1292\/jvms.60.241","article-title":"Protective effect of lactoferricin against Toxoplasma gondii infection in mice","volume":"60","author":"Isamida","year":"1998","journal-title":"J. Vet. Med. Sci."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1292\/jvms.63.187","article-title":"Reduction of the infectivity of Toxoplasma gondii and Eimeria stiedai sporozoites by treatment with bovine lactoferricin","volume":"63","author":"Omata","year":"2001","journal-title":"J. Vet. Med. Sci."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"238","DOI":"10.4315\/0362-028X-55.4.238","article-title":"Inactivation of Listeria monocytogenes by lactoferricin; a potent antimicrobial peptide derived from cow's milk","volume":"55","author":"Wakabayashi","year":"1992","journal-title":"J. Food. Prot."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0958-6946(00)00089-3","article-title":"Antibacterial and binding characteristics of bovine; ovine and caprine lactoferrins: A comparative study","volume":"10","author":"Recio","year":"2000","journal-title":"Int. Dairy J."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"2633","DOI":"10.3389\/fmicb.2017.02633","article-title":"Bovine lactoferrin and lactoferrin-derived peptides inhibit the growth of Vibrio cholerae and other Vibrio species","volume":"8","author":"Bolscher","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1007\/s007050070077","article-title":"In vitro antiviral activity of lactoferrin and ribavirin upon hantavirus","volume":"145","author":"Murphy","year":"2000","journal-title":"Arch. Virol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0168-1702(99)00121-5","article-title":"Characterization of antiviral activity of lactoferrin against hepatitis C virus infection in human cultured cells","volume":"66","author":"Ikeda","year":"2000","journal-title":"Virus. Res."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0168-1702(98)00063-X","article-title":"Human hepatocyte clonal cell lines that support persistent replication of hepatitis C virus","volume":"56","author":"Ikeda","year":"1998","journal-title":"Virus. Res."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1023\/A:1009217709851","article-title":"Metal complexes of bovine lactoferrin inhibit in vitro replication of herpes simplex virus type 1 and 2","volume":"11","author":"Marchetti","year":"1998","journal-title":"Biometals"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"2894","DOI":"10.1002\/eji.200324218","article-title":"Lactoferrin and surfactant protein A exhibit distinct binding specificity to F protein and differently modulate respiratory syncytial virus infection","volume":"33","author":"Sano","year":"2002","journal-title":"Eur. J. Immunol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1086\/343809","article-title":"Lactoferrin inhibits enterovirus 71 infection of human embryonal rhabdomyosarcoma cells in vitro","volume":"186","author":"Lin","year":"2002","journal-title":"J. Infect. Dis."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/20\/11264\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:17:48Z","timestamp":1760167068000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/20\/11264"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,10,19]]},"references-count":238,"journal-issue":{"issue":"20","published-online":{"date-parts":[[2021,10]]}},"alternative-id":["ijms222011264"],"URL":"https:\/\/doi.org\/10.3390\/ijms222011264","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,10,19]]}}}