The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin

被引：57

作者：

Brissette, Catherine A. ^{[1
]}

Verma, Ashutosh ^{[1
]}

Bowman, Amy ^{[1
]}

Cooley, Anne E. ^{[1
]}

Stevenson, Brian ^{[1
]}

机构：

[1] Univ Kentucky, Coll Med, Dept Microbiol Mol Genet & Immunol, Lexington, KY 40536 USA

来源：

MICROBIOLOGY-SGM | 2009年 / 155卷

基金：

美国国家卫生研究院;

关键词：

LYME-DISEASE SPIROCHETE; INHIBITOR FACTOR-H; 32-KILOBASE CIRCULAR PLASMIDS; SENSU-STRICTO; CLINICAL-MANIFESTATIONS; MEMBRANE-PROTEINS; TEMPORAL ANALYSIS; ERYTHEMA MIGRANS; GENE-EXPRESSION; NORTH-AMERICA;

D O I：

10.1099/mic.0.024604-0

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The Lyme disease spirochaete, Borrelia burgdorferi, can invade and persistently infect its hosts' connective tissues. We now demonstrate that B. burgdorferi adheres to the extracellular matrix component laminin. The surface-exposed outer-membrane protein ErpX was identified as having affinity for laminin, and is the first laminin-binding protein to be identified in a Lyme disease spirochaete. The adhesive domain of ErpX was shown to be contained within a small, unstructured hydrophilic segment at the protein's centre. The sequence of that domain is distinct from any previously identified bacterial laminin adhesin, suggesting a unique mode of laminin binding.

引用

页码：863 / 872

页数：10

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