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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| Hauptverfasser: | , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
9 May 2013
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| In: |
Acta crystallographica. Section F, Structural biology communications
Year: 2013, Jahrgang: 69, Heft: 6, Pages: 629-633 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/S1744309113012748 |
| Online-Zugang: | 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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| Verfasserangaben: | Joseph J.E. Caesar, Reinhard Wallich, Peter Kraiczy, Peter F. Zipfel and Susan M. Lea |
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| 245 | 1 | 0 | |a Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi |c Joseph J.E. Caesar, Reinhard Wallich, Peter Kraiczy, Peter F. Zipfel and Susan M. Lea |
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| 520 | |a 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. | ||
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