Details

Autor(en) / Beteiligte

• Tang, Christoph M
• Johnson, Steven
• Lovett, Janet E
• Deane, Janet E
• Kugelberg, Elisabeth
• Lea, Susan M
• Prosser, Beverly E
• Quoraishi, Sadik
• Caesar, Joseph J. E
• Roversi, Pietro
• Sim, Robert B
• Zhang, Qian
• Li, Su
• Schneider, Muriel C

Titel

Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates

Ist Teil von

• Nature, 2009-04, Vol.458 (7240), p.890-893

Ort / Verlag

London: Nature Publishing Group

Erscheinungsjahr

2009

Link zum Volltext

Quelle

EBSCOhost Psychology and Behavioral Sciences Collection

Beschreibungen/Notizen

• 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.