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

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11 Citations (Scopus)


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
Issue number6
Publication statusPublished - 2013
Externally publishedYes


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

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