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ErpC, a member of the complement regulator-acquiring family of surface proteins from

DOI: 10.1107/S1744309113013249 DOI Help
PMID: 23722838 PMID Help

Authors: Joseph Caesar (University of Oxford) , Steven Johnson (University of Oxford) , Peter Kraiczy (University of Oxford) , Susan Lea (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology and Crystallization Communications , VOL 69 , PAGES 624 - 628

State: Published (Approved)
Published: June 2013

Open Access Open Access

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/Frelated paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts.

Journal Keywords: Base; Binding; Borrelia; Complement; Crystallization ; Membrane; Protein; Secondary ; Protein; Tertiary ; Receptors ; Cell Surface

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

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