Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection

被引：40

作者：

Brissette, Catherine A. ^{[1
]}

Cooley, Anne E. ^{[1
]}

Burns, Logan H. ^{[1
]}

Riley, Sean P. ^{[1
]}

Verma, Ashutosh ^{[1
]}

Woodman, Michael E. ^{[1
]}

Bykowski, Tomasz ^{[1
]}

Stevenson, Brian ^{[1
]}

机构：

[1] Univ Kentucky, Coll Med, Dept Microbiol Mol Genet & Immunol, MS Chandler Med Ctr 421, Lexington, KY 40536 USA

来源：

INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY | 2008年 / 298卷

关键词：

Borrelia burgdorferi; outer surface protein; adhesin; complement; factor H; laminin;

D O I：

10.1016/j.ijmm.2007.09.004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Lyme borreliae naturally maintain numerous distinct DNA elements of the cp32 family, each of which carries a mono- or bicistronic erp locus. The encoded Erp proteins are surface-exposed outer membrane lipoproteins that are produced at high levels during mammalian infection but largely repressed during colonization of vector ticks. Recent studies have revealed that some Erp proteins can serve as bacterial adhesins, binding host proteins such as the complement regulator factor H and the extracellular matrix component laminin. These results suggest that Erp proteins play roles in multiple aspects of mammalian infection. (C) 2008 Elsevier GmbH. All rights reserved.

引用

页码：257 / 267

页数：11

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