Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus
作者： Bingrun Liu , Fuguang Chen , Chongwei Bi , Lin Wang , Xiaobo Zhong
DOI: 10.3390/MOLECULES20046533
关键词:
摘要: Sortase A (SrtA) is a cysteine transpeptidase of most Gram-positive bacteria that responsible for the anchorage many surface protein virulence factors to cell wall layer. SrtA mutants are unable display proteins and defective in establishment infections without affecting microbial viability. In this study, we report quercitrin (QEN), natural compound does not affect Staphylococcus aureus growth, can inhibit catalytic activity fibrinogen (Fg) cell-clumping immobilized fibronectin (Fn) adhesion assays. Molecular dynamics simulations mutagenesis assays suggest QEN binds binding sites G167A V193A mutants. These findings indicate potential lead development new anti-virulence agents against S. infections.
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