專題：Nature報道
人類病原體腦膜炎奈瑟球菌是細菌性腦膜炎和敗血病性休克的一個主要病因,，它擁有一種表面蛋白，即“H-因子結合蛋白”（fHbp），后者與“宿主互補調控因子H”結合,，從而干涉免疫反應,。
現(xiàn)在，“人互補調控因子H”與fHbp之間所形成的復合物的結構已被確定,。它顯示,，細菌蛋白通過模仿糖胺聚糖來結合H-因子，這種聚糖自然出現(xiàn)在宿主內皮細胞上,，在那里它們與H-因子結合來防止血管樹（vascular tree）的互補調控損傷,。這項工作對于抵抗腦膜炎球菌疾病的疫苗及療法的開發(fā)具有重要意義。（生物谷Bioon.com）
生物谷推薦原始出處：
Nature 458, 890-893 (16 April 2009) | doi:10.1038/nature07769
Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates
Muriel C. Schneider1,4,5, Beverly E. Prosser2,4, Joseph J. E. Caesar2, Elisabeth Kugelberg1, Su Li1, Qian Zhang1, Sadik Quoraishi2, Janet E. Lovett2, Janet E. Deane2, Robert B. Sim3, Pietro Roversi2, Steven Johnson2, Christoph M. Tang1 & Susan M. Lea2
1 Centre for Molecular Microbiology and Infection, Imperial College, London SW7 2AZ, UK
2 Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
3 MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
4 These authors contributed equally to this work.
5 Present address: Harvard Medical School, Boston, Massachusetts 02115, USA.
The complement system is an essential component of the innate and acquired immune system1, 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 regulators3 and several pathogens have adapted to avoid complement-mediated killing by sequestering fH to their surface4. 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.
