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dc.contributor.authorDavis, K.-
dc.contributor.authorAkinbi, H.-
dc.contributor.authorStandish, A.-
dc.contributor.authorWeiser, J.-
dc.identifier.citationPLoS Pathogens, 2008; 4(12):1-11-
dc.description.abstractThe abundance of lysozyme on mucosal surfaces suggests that successful colonizers must be able to evade its antimicrobial effects. Lysozyme has a muramidase activity that hydrolyzes bacterial peptidoglycan and a non-muramidase activity attributable to its function as a cationic antimicrobial peptide. Two enzymes (PgdA, a N-acetylglucosamine deacetylase, and Adr, an O-acetyl transferase) that modify different sites on the peptidoglycan of Streptococcus pneumoniae have been implicated in its resistance to lysozyme in vitro. Here we show that the antimicrobial effect of human lysozyme is due to its muramidase activity and that both peptidoglycan modifications are required for full resistance by pneumococci. To examine the contribution of lysozyme and peptidoglycan modifications during colonization of the upper respiratory tract, competition experiments were performed with wild-type and pgdAadr mutant pneumococci in lysozyme M-sufficient (LysM+/+) and -deficient (LysM2/2) mice. The wild-type strain out-competed the double mutant in LysM+/+, but not LysM2/2 mice, indicating the importance of resistance to the muramidase activity of lysozyme during mucosal colonization. In contrast, strains containing single mutations in either pgdA or adr prevailed over the wild-type strain in both LysM+/+ and LysM2/2 mice. Our findings demonstrate that individual peptidoglycan modifications diminish fitness during colonization. The competitive advantage of wild-type pneumococci in LysM+/+ but not LysM2/2 mice suggests that the combination of peptidoglycan modifications reduces overall fitness, but that this is outweighed by the benefits of resistance to the peptidoglycan degrading activity of lysozyme.-
dc.description.statementofresponsibilityKimberly M. Davis, Henry T. Akinbi, Alistair J. Standish, Jeffrey N. Weiser-
dc.publisherPublic Library of Science-
dc.rightsCopyright: © 2008 Davis et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.-
dc.subjectRespiratory Mucosa-
dc.subjectCell Wall-
dc.subjectStreptococcus pneumoniae-
dc.subjectPneumococcal Infections-
dc.subjectRespiratory Tract Infections-
dc.subjectBacterial Capsules-
dc.subjectBacterial Proteins-
dc.titleResistance to mucosal lysozyme compensates for the fitness deficit of peptidoglycan modifications by Streptococcus pneumoniae-
dc.typeJournal article-
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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