ErpC, a Member of the Complement Regulator-acquiring Family of Surface Proteins from Borrelia Burgdorferi, Possesses an Architecture Previously Unseen in This Protein Family

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2013 Jun 1

PMID 23722838

Citations 9

Authors

Joseph J E Caesar

Steven Johnson

Peter Kraiczy

Susan M Lea

Affiliations

Soon will be listed here.

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.

Citing Articles

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Borrelia burgdorferi outer surface protein C (OspC) binds complement component C4b and confers bloodstream survival.

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Hijacking Complement Regulatory Proteins for Bacterial Immune Evasion.

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