1887

Abstract

The Lyme disease spirochaete, , can invade and persistently infect its hosts' connective tissues. We now demonstrate that 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.

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2009-03-01
2019-10-22
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vol. , part 3, pp. 863 - 872

Alignment of predicted amino acid sequences of strain B31 ErpX and the two known borrelial Erp proteins most similar to ErpX: the ErpX protein of strain N40 and the ErpQ protein of strain B31. Immature (non-processed, non-lipidated) forms are shown to illustrate overall similarities between the two proteins. Identical amino acids are boxed and shaded. The 84 amino acid central region of ErpX that by itself is sufficient for laminin binding, as identified by recombinant protein rErpX15, is indicated by a line over the ErpX sequence. [ PDF] (605 kb)



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