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- Title
Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates.
- Authors
Schneider, Muriel C; Prosser, Beverly E; Caesar, Joseph J E; Kugelberg, Elisabeth; Li, Su; Zhang, Qian; Quoraishi, Sadik; Lovett, Janet E; Deane, Janet E; Sim, Robert B; Roversi, Pietro; Johnson, Steven; Tang, Christoph M; Lea, Susan M
- Abstract
The complement system is an essential component of the innate and acquired immune system, and consists of a series of proteolytic cascades that are initiated by the presence of microorganisms. In health, activation of complement is precisely controlled through membrane-bound and soluble plasma-regulatory proteins including complement factor H (fH; ref. 2), a 155 kDa protein composed of 20 domains (termed complement control protein repeats). Many pathogens have evolved the ability to avoid immune-killing by recruiting host complement regulators and several pathogens have adapted to avoid complement-mediated killing by sequestering fH to their surface. Here we present the structure of a complement regulator in complex with its pathogen surface-protein ligand. This reveals how the important human pathogen Neisseria meningitidis subverts immune responses by mimicking the host, using protein instead of charged-carbohydrate chemistry to recruit the host complement regulator, fH. The structure also indicates the molecular basis of the host-specificity of the interaction between fH and the meningococcus, and informs attempts to develop novel therapeutics and vaccines.
- Publication
Nature, 2009, Vol 458, Issue 7240, p890
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature07769