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青霉素结合蛋白活性的调节:金黄色葡萄球菌中一种甲氧西林诱导型青霉素结合蛋白的描述。

Regulation of penicillin-binding protein activity: description of a methicillin-inducible penicillin-binding protein in Staphylococcus aureus.

作者信息

Rossi L, Tonin E, Cheng Y R, Fontana R

出版信息

Antimicrob Agents Chemother. 1985 May;27(5):828-31. doi: 10.1128/AAC.27.5.828.

Abstract

The penicillin-binding proteins (PBPs) of two methicillin-resistant strains of Staphylococcus aureus (R2 and R1) were analyzed in cells grown in the absence and in the presence of methicillin. Under the former condition, strain R2 showed the typical PBP pattern of beta-lactam-susceptible strains, while strain R1 showed a markedly increased amount of PBP-3. Under the latter condition, on the other hand, a novel PBP (PBP-2a) located between PBP-2 and -3 was detected in strain R2, while strain R1 appeared to synthesize an even greater amount of PBP-3, in respect to untreated cells. Both R2 PBP-2a and R1 PBP-3 showed a very low affinity for methicillin, which was consistent with the MICs for the respective strains.

摘要

对两株耐甲氧西林金黄色葡萄球菌(R2和R1)的青霉素结合蛋白(PBPs)进行了分析,分析对象为在不存在和存在甲氧西林的情况下生长的细胞。在前一种条件下,R2菌株呈现出β-内酰胺敏感菌株典型的PBP模式,而R1菌株的PBP-3含量显著增加。另一方面,在后一种条件下,在R2菌株中检测到一种位于PBP-2和-3之间的新型PBP(PBP-2a),而R1菌株相对于未处理的细胞似乎合成了更多的PBP-3。R2的PBP-2a和R1的PBP-3对甲氧西林的亲和力都非常低,这与各菌株的最低抑菌浓度(MIC)一致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7542/180160/eeaf12e4d3d9/aac00183-0181-a.jpg

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