Substitution of the antibiotic target: a mechanism of intrinsic resistance to beta-lactam antibiotics in gram-positive bacteria

G. Satta, M. Lleo, E. Tonin, G. M. Rossolini, R. Fontana

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Most beta-lactam antibiotics have multiple penicillin-binding-protein (PBP)targets in gram-positive bacteria. These targets are not protected by any significant impermeable barrier. Therefore, intrinsic (non-beta-lactamase-mediated) resistance can arise from alterations of the targets or under conditions in which the target is 'shifted' from multiple PBPs to a single insensitive target. This can occur in enterococci as a phenotypic adaptation to growth under suboptimal conditions or as a result of a mutation. Methicillin-resistant staphylococci have an additional beta-lactam-resistant PBP, designated PBP2a, that is entirely absent from sensitive strains. This can functionally replace all the sensitive PBPs under conditions in which these have been inhibited by beta-lactam antibiotics. Although methicillin-resistant staphylococci have reduced susceptibility to other beta-lactams besides methicillin, they are not always clinically resistant to these agents.

Original languageEnglish
Title of host publicationCurrent Topics in Infectious Diseases and Clinical Microbiology
Pages31-34
Number of pages4
Volume3
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Medicine(all)

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