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- Title
Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus.
- Authors
Bingrun Liu; Fuguang Chen; Chongwei Bi; Lin Wang; Xiaobo Zhong; Hongjun Cai; Xuming Deng; Xiaodi Niu; Dacheng Wang
- Abstract
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.
- Subjects
SORTASES; STAPHYLOCOCCAL diseases; BACTERIAL enzymes; CYSTEINE proteinases; ENZYME inhibitors; FIBRINOGEN; BLOOD coagulation factors
- Publication
Molecules, 2015, Vol 20, Issue 4, p6533
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules20046533