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一株对特定β-内酰胺类抗生素耐药的金黄色葡萄球菌中的青霉素结合蛋白

Penicillin-binding proteins in a Staphylococcus aureus strain resistant to specific beta-lactam antibiotics.

作者信息

Georgopapadakou N H, Smith S A, Bonner D P

出版信息

Antimicrob Agents Chemother. 1982 Jul;22(1):172-5. doi: 10.1128/AAC.22.1.172.

Abstract

The penicillin-binding proteins (PBPs) of a clinical isolate of Staphylococcus aureus specifically resistant to oral cephalosporins were compared with those of a susceptible strain. In the resistant strain, PBP3 (75,000 molecular weight) was missing or had substantially (greater than 100-fold) reduced affinity for penicillin; PBP2 (80,000 molecular weight) was increased in amount and contained a satellite band, PBP2'; PBPs 1 and 4 were unchanged. Oral cephalosporins bound poorly to PBP2 in both susceptible and resistant strains, but only in the latter did binding correlate with antibiotic activity. The results are consistent with the suggestion that PBP2 is essential in S. aureus. PBP2 might in addition compensate for PBP3 when the latter is missing. In the susceptible strain the lack of correlation between binding to PBP2 and beta-lactam antibiotic activity is due to the very high affinity of the also essential PBP3 for beta-lactam antibiotics.

摘要

将一株对口服头孢菌素具有特异性耐药性的金黄色葡萄球菌临床分离株的青霉素结合蛋白(PBPs)与一株敏感菌株的进行比较。在耐药菌株中,PBP3(分子量75,000)缺失或对青霉素的亲和力大幅降低(超过100倍);PBP2(分子量80,000)数量增加并含有一条卫星带,即PBP2';PBP1和PBP4未发生变化。在敏感和耐药菌株中,口服头孢菌素与PBP2的结合都很差,但只有在耐药菌株中,结合才与抗生素活性相关。这些结果与PBP2在金黄色葡萄球菌中至关重要的观点一致。当PBP3缺失时,PBP2可能还会补偿PBP3的功能。在敏感菌株中,与PBP2的结合和β-内酰胺抗生素活性之间缺乏相关性是由于同样至关重要的PBP3对β-内酰胺抗生素具有非常高的亲和力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fe5/183698/8298df100fbd/aac00208-0183-a.jpg

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