Department of Infection, Immunity and Inflammation, University of Leicester, UK.
Immunobiology. 2010;215(1):1-11. doi: 10.1016/j.imbio.2009.08.006. Epub 2009 Sep 27.
Understanding the structural organisation and mode of action of the initiating complex of the classical pathway of complement activation (C1) has been a central goal in complement biology since its isolation almost 50 years ago. Nevertheless, knowledge is still incomplete, especially with regard to the interactions between its subcomponents C1q, C1r and C1s that trigger activation upon binding to a microbial target. Recent studies have provided new insights into these interactions, and have revealed unexpected parallels with initiating complexes of the lectin pathway of complement: MBL-MASP and ficolin-MASP. Here, we develop and expand these concepts and delineate their implications towards the key aspects of complement activation via the classical and lectin pathways.
自 50 年前分离出经典补体激活途径起始复合物(C1)以来,了解其结构组织和作用模式一直是补体生物学的核心目标。然而,相关知识仍然不完整,特别是在其亚基 C1q、C1r 和 C1s 之间的相互作用方面,这些亚基在与微生物靶标结合时会引发激活。最近的研究为这些相互作用提供了新的见解,并揭示了与补体凝集素途径起始复合物(MBL-MASP 和 ficolin-MASP)之间出人意料的相似之处。在这里,我们发展和扩展了这些概念,并阐述了它们对经典和凝集素途径补体激活关键方面的影响。