Streptococcal collagen-like surface protein 1 promotes adhesion to the respiratory epithelial cell

BMC Microbiology

Research Article

Chin-Ming Wu¹  Ling-Chia Wu²  Pei-Jane Tsai³  Shuen-Kuei Liao⁴  Shih-Ming Chen⁴  Ya-Hui Liu⁵  Cherng-Shyang Chang⁵  Yau-Sheng Tsai⁶ 

[1] Department of Cell Biology and Anatomy, College of Medicine, National Cheng Kung University, Tainan, Taiwan ROC;Department of Medical Laboratory Science and Biotechnology, College of Medicine, National Cheng Kung University, Tainan, Taiwan ROC;Department of Medical Laboratory Science and Biotechnology, College of Medicine, National Cheng Kung University, Tainan, Taiwan ROC;Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan ROC;Graduate Institute of Clinical Medical Sciences, Chang Gung University, Taoyuan, Taiwan, ROC;Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan ROC;Institute of Clinical Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan ROC;

关键词: Necrotizing Fasciitis;    Human Epithelial Cell;    M29588 Strain;    Human Umbilical Vein Endothelial Cell Cell;    Outer Membrane Fraction;   

DOI  :  10.1186/1471-2180-10-320

 received in 2010-04-16, accepted in 2010-12-15,  发布年份 2010

来源: Springer

【 摘 要 】

BackgroundCollagen-like surface proteins Scl1 and Scl2 on Streptococcus pyogenes contain contiguous Gly-X-X triplet amino acid motifs, the characteristic structure of human collagen. Although the potential role of Scl1 in adhesion has been studied, the conclusions may be affected by the use of different S. pyogenes strains and their carriages of various adhesins. To explore the bona fide nature of Scl1 in adherence to human epithelial cells without the potential interference of other streptococcal surface factors, we constructed a scl1 isogenic mutant from the Scl2-defective S. pyogenes strain and a Scl1-expressed Escherichia coli.ResultsLoss of Scl1 in a Scl2-defective S. pyogenes strain dramatically decreased the adhesion of bacteria to HEp-2 human epithelial cells. Expression of Scl1 on the surface of the heterologous bacteria E. coli significantly increased adhesion to HEp-2. The increase in adhesion was nullified when Scl1-expressed E. coli was pre-incubated with proteases or antibodies against recombinant Scl1 (rScl1) protein. Treatment of HEp-2 cells with rScl protein or pronase drastically reduced the binding capability of Scl1-expressed E. coli. These findings suggest that the adhesion is mediated through Scl1 on bacterial surface and protein receptor(s) on epithelial cells. Further blocking of potential integrins revealed significant contributions of α2 and β1 integrins in Scl1-mediated binding to epithelial cells.ConclusionsTogether, these results underscore the importance of Scl1 in the virulence of S. pyogenes and implicate Scl1 as an adhesin during pathogenesis of streptococcal infection.

【 授权许可】

Unknown   
© Chen et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.