Bibliographic Details
| 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 |
| Source: |
Molecules, Vol 20, Iss 4, Pp 6533-6543 (2015) |
| Publisher Information: |
MDPI AG, 2015. |
| Publication Year: |
2015 |
| Collection: |
LCC:Organic chemistry |
| Subject Terms: |
sortase A, quercitrin, Staphylococcus aureus, molecular modeling, Organic chemistry, QD241-441 |
| More Details: |
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. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
1420-3049 |
| Relation: |
http://www.mdpi.com/1420-3049/20/4/6533; https://doaj.org/toc/1420-3049 |
| DOI: |
10.3390/molecules20046533 |
| Access URL: |
https://doaj.org/article/ce3cc745c4594e40a8b84050a754fa8c |
| Accession Number: |
edsdoj.3cc745c4594e40a8b84050a754fa8c |
| Database: |
Directory of Open Access Journals |
