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

• Verfasst von: Caesar, Joseph J. E. [VerfasserIn]
• Verfasst von: Wallich, Reinhard [VerfasserIn]
• Verfasst von: Kraiczy, Peter [VerfasserIn]
• Verfasst von: Zipfel, Peter F. [VerfasserIn]
• Verfasst von: Lea, Susan M. [VerfasserIn]
• Titel: Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi
• Verf.angabe: Joseph J.E. Caesar, Reinhard Wallich, Peter Kraiczy, Peter F. Zipfel and Susan M. Lea
• E-Jahr: 2013
• Jahr: 9 May 2013
• Umfang: 5 S.
• Fussnoten: Gesehen am 28.01.2021
• Titel Quelle: Enthalten in: Acta crystallographica / F
• Ort Quelle: Oxford [u.a.] : Blackwell, 2005
• Jahr Quelle: 2013
• Band/Heft Quelle: 69(2013), 6, Seite 629-633
• ISSN Quelle: 2053-230X
• ISSN Quelle: 1744-3091
• DOI: doi:10.1107/S1744309113012748
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1745938672

Abstract

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.