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Functional characterization of BbCRASP-2, a distinct outer membrane protein of Borrelia burgdorferi that binds host complement regulators factor H and FHL-1

Borrelia burgdorferi, the aetiological agent of Lyme disease, employs sophisticated means to survive in diverse mammalian hosts. Recent studies demonstrated that acquisition of complement regulators factor H and factor H-like protein-1 (FHL-1) allows spirochetes to resist complement-mediated killing...

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Hauptverfasser: Hartmann, Kristina (VerfasserIn) , Corvey, Carsten (VerfasserIn) , Skerka, Christine (VerfasserIn) , Kirschfink, Michael (VerfasserIn) , Karas, Michael (VerfasserIn) , Brade, Volker (VerfasserIn) , Miller, Jennifer C. (VerfasserIn) , Stevenson, Brian (VerfasserIn) , Wallich, Reinhard (VerfasserIn) , Zipfel, Peter F. (VerfasserIn) , Kraiczy, Peter (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 01 August 2006
In: Molecular microbiology
Year: 2006, Jahrgang: 61, Heft: 5, Pages: 1220-1236
ISSN:1365-2958
DOI:10.1111/j.1365-2958.2006.05318.x
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1111/j.1365-2958.2006.05318.x
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2006.05318.x
Volltext
Verfasserangaben:Kristina Hartmann, Carsten Corvey, Christine Skerka, Michael Kirschfink, Michael Karas, Volker Brade, Jennifer C. Miller, Brian Stevenson, Reinhard Wallich, Peter F. Zipfel and Peter Kraiczy
Beschreibung
Zusammenfassung:Borrelia burgdorferi, the aetiological agent of Lyme disease, employs sophisticated means to survive in diverse mammalian hosts. Recent studies demonstrated that acquisition of complement regulators factor H and factor H-like protein-1 (FHL-1) allows spirochetes to resist complement-mediated killing. Serum-resistant B. burgdorferi express up to five distinct complement regulator-acquiring surface proteins (CRASPs) that bind factor H and/or FHL-1. In this study we have identified and characterized one of those B. burgdorferi proteins, named BbCRASP-2. BbCRASP-2 is distinct from the four previously identified factor H/FHL-1-binding CRASPs of B. burgdorferi strains. The single copy of the gene encoding BbCRASP-2, cspZ, is located on the linear plasmid lp28-3. BbCRASP-2 is highly divergent from the factor H/FHL-1-binding protein BbCRASP-1 and from members of the factor H-binding Erp (OspE/F-related) protein family. Peptide mapping analysis revealed that the factor H/FHL-1 binding site is discontinuous and it was found that C-terminal truncations abrogate factor H and FHL-1 binding. The predominant BbCRASP-2 binding site of both host complement regulators was mapped to the short consensus repeat 7 (SCR 7). Factor H and FHL-1 bound to BbCRASP-2 maintain cofactor activity for factor I-mediated C3b inactivation and accelerate the decay of the C3 convertase. Expression of BbCRASP-2 in serum-sensitive B. burgdorferi mutant B313 increased resistance to complement-mediated lysis. The characterization of BbCRASP-2 now provides a complete picture of the three diverse complement regulator-binding protein families of B. burgdorferi yielding new insights into the pathogenesis of Lyme disease.
Beschreibung:Gesehen am 15.02.2021
Beschreibung:Online Resource
ISSN:1365-2958
DOI:10.1111/j.1365-2958.2006.05318.x

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