Involvement of a challenge in penicillin target and peptidoglycan structure in low-level resistance to beta -lactam antibiotics in Neisseria gonorrhoeae

A penicillin-susceptible gonococcus and its low-level resistant penA transformant were examined with regard to their penicillin-binding proteins (PBPs) and their peptidoglycan structures. Treatment of the susceptible strain with its MIC of penicillin (0.01 mu g/ml) led to significant binding to PBPs...

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Bibliographic Details
Published inAntimicrobial agents and chemotherapy Vol. 28; no. 1; pp. 90 - 95
Main Author Dougherty, T J
Format Journal Article
LanguageEnglish
Published 01.01.1985
Subjects
Neisseria gonorrhoeae
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Summary:A penicillin-susceptible gonococcus and its low-level resistant penA transformant were examined with regard to their penicillin-binding proteins (PBPs) and their peptidoglycan structures. Treatment of the susceptible strain with its MIC of penicillin (0.01 mu g/ml) led to significant binding to PBPs 2 and 3 and a substantial decrease in the O-acetyl modification on the peptidoglycan. Peptidoglycan synthesis gradually ceased over an extended time. In both strains the rate of peptidoglycan synthesis and the cross-linkage of the peptidoglycan made declined sharply, suggesting that significant inhibition of PBP 1 interfered with transpeptidation. A model for low-level resistance is proposed in which a decreased PBP 2 affinity leads to assumption of the role of primary target in the resistant transformant by PBP 1. The differences observed in peptidoglycan metabolism are a direct consequence of this change.
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ISSN:0066-4804