Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus
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 affect...
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MDPI AG
2015-04-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/20/4/6533 |
| _version_ | 1818110473421193216 |
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| author | Bingrun Liu Fuguang Chen Chongwei Bi Lin Wang Xiaobo Zhong Hongjun Cai Xuming Deng Xiaodi Niu Dacheng Wang |
| author_facet | Bingrun Liu Fuguang Chen Chongwei Bi Lin Wang Xiaobo Zhong Hongjun Cai Xuming Deng Xiaodi Niu Dacheng Wang |
| author_sort | Bingrun Liu |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-11T02:47:42Z |
| format | Article |
| id | doaj.art-ce3cc745c4594e40a8b84050a754fa8c |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-11T02:47:42Z |
| publishDate | 2015-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-ce3cc745c4594e40a8b84050a754fa8c2022-12-22T01:23:24ZengMDPI AGMolecules1420-30492015-04-012046533654310.3390/molecules20046533molecules20046533Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureusBingrun Liu0Fuguang Chen1Chongwei Bi2Lin Wang3Xiaobo Zhong4Hongjun Cai5Xuming Deng6Xiaodi Niu7Dacheng Wang8College of Animal Science, Jilin University, Changchun 130062, ChinaCollege of Animal Science, Jilin University, Changchun 130062, ChinaCollege of Animal Science, Jilin University, Changchun 130062, ChinaKey Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Changchun 130062, ChinaCollege of Animal Science, Jilin University, Changchun 130062, ChinaCollege of Animal Science, Jilin University, Changchun 130062, ChinaKey Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Changchun 130062, ChinaDepartment of Food Quality and Safety, Jilin University, Changchun130062, ChinaCollege of Animal Science, Jilin University, Changchun 130062, ChinaSortase 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.http://www.mdpi.com/1420-3049/20/4/6533sortase AquercitrinStaphylococcus aureusmolecular modeling |
| spellingShingle | Bingrun Liu Fuguang Chen Chongwei Bi Lin Wang Xiaobo Zhong Hongjun Cai Xuming Deng Xiaodi Niu Dacheng Wang Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus Molecules sortase A quercitrin Staphylococcus aureus molecular modeling |
| title | Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus |
| title_full | Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus |
| title_fullStr | Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus |
| title_full_unstemmed | Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus |
| title_short | Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus |
| title_sort | quercitrin an inhibitor of sortase a interferes with the adhesion of staphylococcal aureus |
| topic | sortase A quercitrin Staphylococcus aureus molecular modeling |
| url | http://www.mdpi.com/1420-3049/20/4/6533 |
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