The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin

Catherine A. Brissette, Ashutosh Verma, Amy Bowman, Anne E. Cooley, Brian Stevenson

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


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.

Original languageEnglish
Pages (from-to)863-872
Number of pages10
Issue number3
StatePublished - 2009

ASJC Scopus subject areas

  • Microbiology


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