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PMID: 2079445 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Modification of penicillin-binding proteins of penicillin-resistant mutants of different species of enterococci.

The Journal of antimicrobial chemotherapy ·Vol. 26 ·No. 5 ·1990-11-00 ·Pages 613-8

al-Obeid S, Gutmann L, Williamson R

Abstract

Mutants resistant to penicillin G were selected in a stepwise manner from nine different species of enterococci. Mutants with the highest level of resistance showed cross-resistance to all beta-lactams tested. For eight of the nine species, resistance correlated with increased production of a low molecular weight penicillin-binding protein (PBP). Two of these species produced a new PBP of low molecular weight, while two other species produced an additional PBP of high molecular weight. With the exception of Enterococcus faecium, no difference was observed in terms of lysis or bactericidal effect when the sensitive strains and their resistant mutants were tested at ten times their respective MICs of penicillin G. With E. faecium an increased lytic and bactericidal effect was observed for the resistant mutant.

MeSH Terms
Bacterial Proteins Carrier Proteins/metabolism Hexosyltransferases Microbial Sensitivity Tests Muramoylpentapeptide Carboxypeptidase/metabolism Mutation Penicillin Resistance/genetics Penicillin-Binding Proteins Peptidyl Transferases Species Specificity Streptococcus/drug effects,genetics
Chemicals
Bacterial Proteins Carrier Proteins Penicillin-Binding Proteins Peptidyl Transferases Hexosyltransferases Muramoylpentapeptide Carboxypeptidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
al-Obeid S
Laboratoire de Microbiologie Médicale, Université Pierre et Marie Curie, Paris, France.
Gutmann L
Williamson R
Article Info
Journal
The Journal of antimicrobial chemotherapy
Abbr.
J Antimicrob Chemother
ISSN
0305-7453
Published
1990-11-00
Pages
613-8
Language
English
Region
England
NLM ID
7513617
Subset
IM
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