Next Article in Journal
Longevity Extension by Phytochemicals
Previous Article in Journal
A Facile Synthesis and Antimicrobial Activity Evaluation of Sydnonyl-Substituted Thiazolidine Derivatives
Article Menu

Export Article

Open AccessArticle
Molecules 2015, 20(4), 6533-6543; doi:10.3390/molecules20046533

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

1
College of Animal Science, Jilin University, Changchun 130062, China
2
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Science, Harbin 150001, China
3
Key Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Changchun 130062, China
4
Department of Food Quality and Safety, Jilin University, Changchun130062, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 13 January 2015 / Revised: 5 April 2015 / Accepted: 8 April 2015 / Published: 13 April 2015
(This article belongs to the Section Medicinal Chemistry)
View Full-Text   |   Download PDF [2445 KB, uploaded 13 April 2015]   |  

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. View Full-Text
Keywords: sortase A; quercitrin; Staphylococcus aureus; molecular modeling sortase A; quercitrin; Staphylococcus aureus; molecular modeling
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Liu, B.; Chen, F.; Bi, C.; Wang, L.; Zhong, X.; Cai, H.; Deng, X.; Niu, X.; Wang, D. Quercitrin, an Inhibitor of Sortase A, Interferes with the Adhesion of Staphylococcal aureus. Molecules 2015, 20, 6533-6543.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top