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口腔链球菌的菌毛能够与纤连蛋白结合,从而促进细胞黏附。

Pili of oral Streptococcus sanguinis bind to fibronectin and contribute to cell adhesion.

机构信息

Department of Oral Frontier Biology, Graduate School of Dentistry, Osaka University, 1-8 Yamadaoka, Suita-Osaka 565-0871, Japan.

出版信息

Biochem Biophys Res Commun. 2010 Jan 8;391(2):1192-6. doi: 10.1016/j.bbrc.2009.12.029. Epub 2009 Dec 14.

Abstract

Streptococcus sanguinis is a predominant bacterium in the human oral cavity and occasionally causes infective endocarditis. We identified a unique cell surface polymeric structure named pili in this species and investigated its functions in regard to its potential virulence. Pili of S. sanguinis strain SK36 were shown to be composed of three distinctive pilus proteins (PilA, PilB, and PilC), and a pili-deficient mutant demonstrated reduced bacterial adherence to HeLa and human oral epithelial cells. PilC showed a binding ability to fibronectin, suggesting that pili are involved in colonization by this species. In addition, ATCC10556, a standard S. sanguinis strain, was unable to produce pili due to defective pilus genes, which indicates a diversity of pilus expression among various S. sanguinis strains.

摘要

血链球菌是人类口腔中的主要细菌,偶尔会引起感染性心内膜炎。我们在该物种中鉴定出一种独特的细胞表面聚合结构,称为菌毛,并研究了其在潜在毒力方面的功能。结果表明,血链球菌 SK36 菌株的菌毛由三种不同的菌毛蛋白(PilA、PilB 和 PilC)组成,菌毛缺陷突变体显示出对 HeLa 和人口腔上皮细胞的粘附能力降低。PilC 显示出与纤维连接蛋白的结合能力,表明菌毛参与了该物种的定植。此外,由于缺陷的菌毛基因,标准的血链球菌菌株 ATCC10556 无法产生菌毛,这表明不同血链球菌菌株之间菌毛表达存在多样性。

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