Gene Symbol: cspA
Description: complement regulator-acquiring surface protein 1 (CRASP-1)
Species: Borrelia burgdorferi B31
- Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteinsPeter Kraiczy
Institute of Medical Microbiology, University Hospital of Frankfurt, Paul Ehrlich Strasse 40, D 60596 Frankfurt, Germany
J Biol Chem 279:2421-9. 2004..is the key molecule of the complement resistance of spirochetes, and (iii). is distinct from the Erp protein family. Thus, BbCRASP-1 most likely contributes to persistence of B. burgdorferi and to pathogenesis of Lyme disease...
- A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferiFrank S Cordes
Laboratory of Molecular Biophysics, Department of Biochemistry, South Parks Road, Oxford, UK
Nat Struct Mol Biol 12:276-7. 2005..Here we report the atomic structure for the key FHL-1- and FH-binding protein BbCRASP-1 and reveal a homodimer that presents a novel target for drug design...
- Artificial-infection protocols allow immunodetection of novel Borrelia burgdorferi antigens suitable as vaccine candidates against Lyme diseaseReinhard Wallich
Institut fur Immunologie, Universitatsklinikum Heidelberg, Heidelberg, Germany
Eur J Immunol 33:708-19. 2003..These findings suggest that all three recombinant antigens represent potential candidates for a "second generation" vaccine to prevent and/or cure Lyme disease...
- Crystallization and preliminary crystallographic analysis of BbCRASP-1, a complement regulator-acquiring surface protein of Borrelia burgdorferiFrank S Cordes
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England
Acta Crystallogr D Biol Crystallogr 60:929-32. 2004..2 A resolution have been collected. The selenium substructure has been solved and initial phases have been refined to 3.0 A by density-modification methods. Model building and refinement are under way...
- Putative coiled-coil structural elements of the BBA68 protein of Lyme disease spirochetes are required for formation of its factor H binding siteJohn V McDowell
Department of Microbiology and Immunology, Medical College of Virginia Commonwealth University, Richmond, VA 23298, USA
J Bacteriol 187:1317-23. 2005..These analyses revealed that the factor H binding site is discontinuous and provide strong evidence that coiled-coil structural elements are involved in the formation of the binding site...