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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):624-8. doi: 10.1107/S1744309113013249. Epub 2013 May 23.

ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family.

Author information

1
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, England.

Abstract

Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts.

KEYWORDS:

BbCRASP-4; Borrelia burgdorferi; ErpC; complement; factor H

PMID:
23722838
PMCID:
PMC3668579
DOI:
10.1107/S1744309113013249
[Indexed for MEDLINE]
Free PMC Article

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