耐青霉素肺炎链球菌青霉素结合蛋白动力学特性的改变。
Alterations in kinetic properties of penicillin-binding proteins of penicillin-resistant Streptococcus pneumoniae.
作者信息
Handwerger S, Tomasz A
出版信息
Antimicrob Agents Chemother. 1986 Jul;30(1):57-63. doi: 10.1128/AAC.30.1.57.
Abstract
Earlier studies have shown that the highly penicillin-resistant South African Strains of pneumococci contain altered penicillin-binding proteins (PBPs) (S. Zighelboim and A. Tomasz, Antimicrob. Agents Chemother. 17:434-442, 1980). We now describe a detailed quantitative characterization of the reaction of radioactively labeled penicillin with the PBPs of the penicillin-susceptible and penicillin-resistant pneumococci and several intermediate-resistance-level genetic transformants as well. The altered binding of the antibiotic by the PBPs of resistant cells appears to be due to a combination of two factors: lower drug affinity and change in the cellular amounts of PBPs. No alteration in the rates of deacylation of the penicilloyl-PBPs of the resistant cells was detected.
摘要
早期研究表明，对青霉素高度耐药的南非肺炎球菌菌株含有改变的青霉素结合蛋白（PBPs）（S. Zighelboim和A. Tomasz，《抗菌药物与化疗》17:434 - 442，1980年）。我们现在描述放射性标记青霉素与青霉素敏感和耐药肺炎球菌以及几个中间耐药水平的基因转化体的PBPs反应的详细定量特征。耐药细胞的PBPs对抗生素结合的改变似乎是由于两个因素的结合：较低的药物亲和力和PBPs细胞含量的变化。未检测到耐药细胞的青霉素酰 - PBPs脱酰化速率有改变。
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