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Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates

Author

Listed:
  • Muriel C. Schneider

    (Centre for Molecular Microbiology and Infection, Imperial College
    Present address: Harvard Medical School, Boston, Massachusetts 02115, USA.)

  • Beverly E. Prosser

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Joseph J. E. Caesar

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Elisabeth Kugelberg

    (Centre for Molecular Microbiology and Infection, Imperial College)

  • Su Li

    (Centre for Molecular Microbiology and Infection, Imperial College)

  • Qian Zhang

    (Centre for Molecular Microbiology and Infection, Imperial College)

  • Sadik Quoraishi

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Janet E. Lovett

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Janet E. Deane

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Robert B. Sim

    (MRC Immunochemistry Unit, University of Oxford, South Parks Road, Oxford OX1 3QU, UK)

  • Pietro Roversi

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Steven Johnson

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

  • Christoph M. Tang

    (Centre for Molecular Microbiology and Infection, Imperial College)

  • Susan M. Lea

    (Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK)

Abstract

A mimic in meningitis The human pathogen Neisseria meningitidis, a leading cause of bacterial meningitis and septic shock, possesses a surface protein, factor H binding protein or fHbp, that binds to host complement regulator factor H, thereby interfering with the immune response. Now the structure of the complex between human complement regulator factor H and fHbp has been determined. It reveals that the bacterial protein binds factor H by mimicking the glycosaminoglycans that occur naturally on host endothelial cells where they recruit factor H to prevent complement-mediated damage of the vascular tree. This work has important implications for the development of vaccines and therapeutics to counter meningococcal disease.

Suggested Citation

  • Muriel C. Schneider & Beverly E. Prosser & Joseph J. E. Caesar & Elisabeth Kugelberg & Su Li & Qian Zhang & Sadik Quoraishi & Janet E. Lovett & Janet E. Deane & Robert B. Sim & Pietro Roversi & Steven, 2009. "Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates," Nature, Nature, vol. 458(7240), pages 890-893, April.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7240:d:10.1038_nature07769
    DOI: 10.1038/nature07769
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