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PMID: 7425601 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Multiple changes of penicillin-binding proteins in penicillin-resistant clinical isolates of Streptococcus pneumoniae.

Antimicrobial agents and chemotherapy ·Vol. 17 ·No. 3 ·1980-03-00 ·Pages 364-71

Hakenbeck R, Tarpay M, Tomasz A

Abstract

Penicillin-binding properties and characteristics of penicillin-binding proteins (PBPs) were investigated in several clinical isolates of Streptococcus pneumoniae differing in their susceptibilities to penicillin (minimal inhibitory concentration [MIC], 0.03 to 0.5 microgram/ml) and compared with the penicillin-susceptible strain R36A (MIC, 0.07 microgram/ml). Several changes accompanied the development of resistance: the relative affinity to penicillin of whole cells, isolated membranes, and two major PBPs after in vivo or in vitro labeling decreased (with increasing resistance). Furthermore, one additional PBP (2') appeared in four of five relatively resistant strains with an MIC of 0.25 microgram/ml and higher. PBP 3 maintained the same high affinity toward penicillin in all strains under all labeling conditions.

MeSH Terms
Bacterial Proteins/metabolism Carrier Proteins/metabolism Cell Fractionation Humans Membrane Proteins/metabolism Penicillin Resistance Penicillins/metabolism Protein Binding Species Specificity Streptococcus pneumoniae/drug effects,metabolism
Chemicals
Bacterial Proteins Carrier Proteins Membrane Proteins Penicillins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hakenbeck R
Tarpay M
Tomasz A
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26 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
DOI
10.1128/AAC.17.3.364
Published
1980-03-00
Pages
364-71
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC283792
Subset
IM
Grants
NIAID NIH HHS · AI 16170 · United States
External Links
PubMed source DOI: 10.1128/AAC.17.3.364 PMC Full Text View journal details
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