Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates

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 Johnson, Christoph M. Tang () and Susan M. Lea ()
Additional contact information
Muriel C. Schneider: Centre for Molecular Microbiology and Infection, Imperial College
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

Nature, 2009, vol. 458, issue 7240, 890-893

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.

Date: 2009
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DOI: 10.1038/nature07769

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