Isolation of a putative laminin binding protein from Streptococcus anginosus

被引：15

作者：

Allen, BL ^{[1
]}

Höök, M

机构：

[1] Indianapolis VA Med Ctr, Indianapolis, IN 46202 USA

[2] Indiana Univ, Sch Med, Dept Internal Med, Div Infect Dis, Indianapolis, IN USA

[3] Texas A&M Univ, Albert A Alkek Inst Biosci & Technol, Ctr Extracellular Matrix Biol, Houston, TX USA

来源：

MICROBIAL PATHOGENESIS | 2002年 / 33卷 / 01期

关键词：

endocarditis; Streptococcus; bacterial adherence; basement membrane; laminin; extracellular matrix;

D O I：

10.1006/mpat.2002.0510

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Viridans streptococci, including Streptococcus anginosus, are a common cause of infective endocarditis in humans. Adherence mechanisms involved in colonization of non-diseased native valves (present in 40% of native valve endocarditis) are unknown. We have previously shown that an endocarditis isolate of S. anginosus adheres to exposed basement membrane of human and porcine valve tissue in a laminin dependent manner. We now describe the partial purification of an 80 kDa putative laminin binding protein (PLBP) by biochemical methods. Amino acid sequence of PLBP peptides is similar to substrate binding proteins of ABC transporters in other Gram-positive cocci. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：23 / 31

页数：9

共 37 条

[1] Streptococcus anginosus adheres to vascular endothelium basement membrane and purified extracellular matrix proteins [J].