Differences in penicillin-binding protein patterns of penicillin tolerant and non-tolerant group A streptococci

The penicillin-binding proteins (PBPs) of five penicillin tolerant group A streptococci and their isogenic non-tolerantstrains, and seven unrelated non-tolerant group A streptococci were compared. PBPs from late logarithmic cultures were labelled in vitro with 3H-benzylpenicillin and analysed by SDS...

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Bibliographic Details
Published in:Journal of antimicrobial chemotherapy 1995-01, Vol.35 (1), p.67-74
Main Authors: van Asselt, G. J., de Kort, G., van de Klundert, J. A. M.
Format: Article
Language:English
Subjects:
Antibacterial agents
Antibiotics. Antiinfectious agents. Antiparasitic agents
Bacterial Outer Membrane Proteins - metabolism
Bacterial Proteins
Biological and medical sciences
Carrier Proteins - metabolism
Electrophoresis, Polyacrylamide Gel
Hexosyltransferases
Medical sciences
Microbial Sensitivity Tests
Muramoylpentapeptide Carboxypeptidase - metabolism
Penicillin G - metabolism
Penicillin Resistance - physiology
Penicillin-Binding Proteins
Penicillins - metabolism
Peptidyl Transferases
Pharmacology. Drug treatments
Streptococcus
Streptococcus pyogenes - drug effects
Streptococcus pyogenes - metabolism
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Summary:The penicillin-binding proteins (PBPs) of five penicillin tolerant group A streptococci and their isogenic non-tolerantstrains, and seven unrelated non-tolerant group A streptococci were compared. PBPs from late logarithmic cultures were labelled in vitro with 3H-benzylpenicillin and analysed by SDS-PAGE and fluorography. The PBP patterns for all non-tolerant strains were identical. This pattern differed markedly from that for penicillin tolerant strains, both qualitatively and quantitatively. The most striking change in penicillin tolerant strains was decreased binding of 3H-penicillin to PBP 3 and increased binding to PBP 5, while PBP 2a was replaced by a new PBP (PBP 2a') of lower electrophoretic mobility. Tolerance was lost during storage but could be restored by consecutive transfers on to penicillin gradient agar plates.At the same time the PBP profiles of these strains became identical to those found for stable tolerant strains. These results suggest the possibility that PBP 2a' and PBP 5 in combination with other PBP alterations play a role in penicillin tolerance found in group A streptococci.
ISSN:0305-7453
1460-2091
DOI:10.1093/jac/35.1.67