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The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin.

ABSTRACT: 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.

SUBMITTER: Brissette CA

PROVIDER: S-EPMC10010501 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin.

Brissette Catherine A CA Verma Ashutosh A Bowman Amy A Cooley Anne E AE Stevenson Brian B

Microbiology (Reading, England) 20090301 Pt 3

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 a ...[more]

PMID: 19246757

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