Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus

文献类型： 外文期刊

第一作者： Liu, Bingrun

作者： Liu, Bingrun;Chen, Fuguang;Bi, Chongwei;Zhong, Xiaobo;Cai, Hongjun;Wang, Dacheng;Chen, Fuguang;Wang, Lin;Deng, Xuming;Niu, Xiaodi

作者机构：

关键词： sortase A;quercitrin;Staphylococcus aureus;molecular modeling

期刊名称：MOLECULES （ 影响因子：4.411； 五年影响因子：4.587 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： Sortase A (SrtA) is a cysteine transpeptidase of most Gram-positive bacteria that is responsible for the anchorage of many surface protein virulence factors to the cell wall layer. SrtA mutants are unable to display surface proteins and are defective in the establishment of infections without affecting microbial viability. In this study, we report that quercitrin (QEN), a natural compound that does not affect Staphylococcus aureus growth, can inhibit the catalytic activity of SrtA in fibrinogen (Fg) cell-clumping and immobilized fibronectin (Fn) adhesion assays. Molecular dynamics simulations and mutagenesis assays suggest that QEN binds to the binding sites of the SrtA G167A and V193A mutants. These findings indicate that QEN is a potential lead compound for the development of new anti-virulence agents against S. aureus infections.

分类号： O62

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