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PMID: 3850810 Published · ppublish English Journal Article

Penicillin-binding proteins of beta-lactam-resistant strains of Staphylococcus aureus. Effect of growth conditions.

FEBS letters ·Vol. 192 ·No. 1 ·1985-11-11 ·Pages 28-32

Reynolds PE, Brown DF

Abstract

Methicillin-resistant clinical isolates of Staphylococcus aureus are intrinsically resistant to beta-lactam antibiotics in that the resistance mechanism is unrelated to the possession of beta-lactamases. We have demonstrated that a new, high-molecular-mass penicillin-binding protein (PBP) is present in these strains with a low affinity for beta-lactams and that its amount is regulated by the growth conditions. The new PBP from all strains that have been examined has an identical mobility on SDS gel electrophoresis and is the only PBP still present in an uncomplexed state with beta-lactams (and therefore the only functional PBP when these strains are grown in media containing concentrations of beta-lactam antibiotics sufficient to kill sensitive strains.

MeSH Terms
Anti-Bacterial Agents/pharmacology Bacterial Proteins Carboxypeptidases/metabolism Carrier Proteins/metabolism Cephalothin/metabolism Culture Media Electrophoresis, Polyacrylamide Gel Hexosyltransferases Methicillin/pharmacology Molecular Weight Muramoylpentapeptide Carboxypeptidase/metabolism Penicillin G/metabolism Penicillin Resistance Penicillin-Binding Proteins Peptidyl Transferases Staphylococcus aureus/drug effects,metabolism
Chemicals
Anti-Bacterial Agents Bacterial Proteins Carrier Proteins Culture Media Penicillin-Binding Proteins Peptidyl Transferases Hexosyltransferases Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Penicillin G Methicillin Cephalothin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Reynolds P E
Brown D F
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1985-11-11
Pages
28-32
Language
English
Region
England
NLM ID
0155157
Subset
IM
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