Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi

Joseph J.E. Caesar, Reinhard Wallich, Peter Kraiczy, Peter F. Zipfel, Susan M. Lea

Research output: Contribution to journalArticleResearchpeer-review

10 Citations (Scopus)

Abstract

Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators.

Original languageEnglish
Pages (from-to)629-633
Number of pages5
JournalActa Crystallographica Section F: Structural Biology Communications
Volume69
Issue number6
DOIs
Publication statusPublished - 2013
Externally publishedYes

Keywords

  • BbCRASP-1
  • Borrelia burgdorferi
  • complement
  • CspA
  • factor H

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