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PMID: 6563036 Published · ppublish English Journal Article

Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus.

Journal of bacteriology ·Vol. 158 ·No. 2 ·1984-05-00 ·Pages 513-6

Hartman BJ, Tomasz A

Abstract

Methicillin resistance in Staphylococcus aureus has been associated with alterations in the penicillin-binding proteins (PBPs). An intriguing property of all methicillin-resistant staphylococci is the dependence of resistance on the pH value of the growth medium. Growth of such bacteria at pH 5.2 completely suppressed the expression of methicillin resistance. We have examined the PBP patterns of methicillin-resistant staphylococci grown at pH 7.0. We detected a high-molecular-weight PBP (PBP-2a; approximate size, 78,000 daltons) that was only present in the resistant bacteria but not in the isogenic sensitive strain. In cultures grown at pH 5.2, the extra PBP was not detectable.

MeSH Terms
Bacterial Proteins Carboxypeptidases/metabolism Carrier Proteins/analysis,metabolism Hexosyltransferases Hydrogen-Ion Concentration Methicillin/metabolism,pharmacology Molecular Weight Muramoylpentapeptide Carboxypeptidase/analysis,metabolism Penicillin Resistance Penicillin-Binding Proteins Peptidyl Transferases Staphylococcus aureus/drug effects,metabolism
Chemicals
Bacterial Proteins Carrier Proteins Penicillin-Binding Proteins Peptidyl Transferases Hexosyltransferases Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Methicillin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hartman B J
Tomasz A
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17 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1984-05-00
Pages
513-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC215458
Subset
IM
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