cspA

Summary

Gene Symbol: cspA
Description: complement regulator-acquiring surface protein 1 (CRASP-1)
Species: Borrelia burgdorferi B31

Top Publications

  1. ncbi 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 proteins
    Peter Kraiczy
    Institute of Medical Microbiology, University Hospital of Frankfurt, Paul Ehrlich Strasse 40, D 60596 Frankfurt, Germany
    J Biol Chem 279:2421-9. 2004
  2. ncbi A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi
    Frank S Cordes
    Laboratory of Molecular Biophysics, Department of Biochemistry, South Parks Road, Oxford, UK
    Nat Struct Mol Biol 12:276-7. 2005
  3. ncbi Artificial-infection protocols allow immunodetection of novel Borrelia burgdorferi antigens suitable as vaccine candidates against Lyme disease
    Reinhard Wallich
    Institut fur Immunologie, Universitatsklinikum Heidelberg, Heidelberg, Germany
    Eur J Immunol 33:708-19. 2003
  4. ncbi Crystallization and preliminary crystallographic analysis of BbCRASP-1, a complement regulator-acquiring surface protein of Borrelia burgdorferi
    Frank S Cordes
    Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England
    Acta Crystallogr D Biol Crystallogr 60:929-32. 2004
  5. pmc Putative coiled-coil structural elements of the BBA68 protein of Lyme disease spirochetes are required for formation of its factor H binding site
    John V McDowell
    Department of Microbiology and Immunology, Medical College of Virginia Commonwealth University, Richmond, VA 23298, USA
    J Bacteriol 187:1317-23. 2005

Scientific Experts

  • P Kraiczy
  • Frank S Cordes
  • Reinhard Wallich
  • Markus M Simon
  • John V McDowell
  • Susan M Lea
  • Christine Skerka
  • Volker Brade
  • Pietro Roversi
  • Oliver Jahraus
  • Matthew E Harlin
  • Elizabeth A Rogers
  • Richard T Marconi
  • Russell Wallis
  • Peter F Zipfel
  • Edward D Lowe
  • Michael Kirschfink
  • Peter Zipfel
  • Thi Thanh Thao Tran
  • Thomas Stehle
  • Heidelore Hofmann
  • Christiane Brenner
  • Lise Gern

Detail Information

Publications5

  1. ncbi 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 proteins
    Peter 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...
  2. ncbi A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi
    Frank 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...
  3. ncbi Artificial-infection protocols allow immunodetection of novel Borrelia burgdorferi antigens suitable as vaccine candidates against Lyme disease
    Reinhard 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...
  4. ncbi Crystallization and preliminary crystallographic analysis of BbCRASP-1, a complement regulator-acquiring surface protein of Borrelia burgdorferi
    Frank 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...
  5. pmc Putative coiled-coil structural elements of the BBA68 protein of Lyme disease spirochetes are required for formation of its factor H binding site
    John 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...