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

B. burgdorferi binds complement factor H using a dimeric surface protein, CspA (BbCRASP-1). Presented here is a new structure of CspA that suggests that there is a degree of flexibility between subunits which may have implications for complement regulator binding., - Borrelia burgdorferi has evolve...

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Main Authors: Caesar, Joseph J. E. (Author) , Wallich, Reinhard (Author) , Kraiczy, Peter (Author) , Zipfel, Peter F. (Author) , Lea, Susan M. (Author)
Format: Article (Journal)
Language:English
Published: 9 May 2013
In: Acta crystallographica. Section F, Structural biology communications
Year: 2013, Volume: 69, Issue: 6, Pages: 629-633
ISSN:2053-230X
DOI:10.1107/S1744309113012748
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1107/S1744309113012748
Verlag, lizenzpflichtig, Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668580/
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Author Notes:Joseph J.E. Caesar, Reinhard Wallich, Peter Kraiczy, Peter F. Zipfel and Susan M. Lea
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Summary:B. burgdorferi binds complement factor H using a dimeric surface protein, CspA (BbCRASP-1). Presented here is a new structure of CspA that suggests that there is a degree of flexibility between subunits which may have implications for complement regulator binding., - 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.
Item Description:Gesehen am 28.01.2021
Physical Description:Online Resource
ISSN:2053-230X
DOI:10.1107/S1744309113012748

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