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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.

Original publication

DOI

10.1107/S1744309113013249

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

06/2013

Volume

69

Pages

624 - 628

Keywords

BbCRASP-4, Borrelia burgdorferi, ErpC, complement, factor H, Bacterial Outer Membrane Proteins, Base Sequence, Binding Sites, Borrelia burgdorferi, Complement System Proteins, Crystallization, Membrane Proteins, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, Receptors, Cell Surface