溶葡萄球菌素免疫因子Lif在葡萄球菌肽聚糖肽间桥形成过程中补充FemB的功能。

Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation.

作者信息

Tschierske M, Ehlert K, Strandén A M, Berger-Bächi B

机构信息

Institute of Medical Microbiology, University of Zürich, Switzerland.

出版信息

FEMS Microbiol Lett. 1997 Aug 15;153(2):261-4. doi: 10.1016/s0378-1097(97)00234-6.

DOI:10.1016/s0378-1097(97)00234-6

PMID:9271851

Abstract

The formation of the Staphylococcus aureus peptidoglycan pentaglycine interpeptide chain needs FemA and FemB for the incorporation of glycines Gly2-Gly3, and Gly4-Gly5, respectively. The lysostaphin immunity factor Lif was able to complement FemB, as could be shown by serine incorporation and by an increase in lysostaphin resistance in the wild-type as well as in a femB mutant. However, Lif could not substitute for FemA in femA or in femAB-null mutants. Methicillin resistance, which is dependent on functional FemA and FemB, was not complemented by Lif, suggesting that serine-substituted side chains are a lesser substrate for penicillin-binding protein PBP2' in methicillin resistance.

摘要

金黄色葡萄球菌肽聚糖五甘氨酸间肽链的形成分别需要FemA和FemB来掺入甘氨酸Gly2 - Gly3以及Gly4 - Gly5。溶葡萄球菌素免疫因子Lif能够互补FemB，这可通过丝氨酸掺入以及野生型和femB突变体中溶葡萄球菌素抗性的增加得以证明。然而，Lif不能在femA或femAB缺失突变体中替代FemA。依赖于功能性FemA和FemB的耐甲氧西林特性不能被Lif互补，这表明在耐甲氧西林过程中，丝氨酸取代的侧链是青霉素结合蛋白PBP2'的较差底物。