麻疹病毒
血凝素(流感)
外域
病毒学
病毒
受体
生物
糖蛋白
细胞生物学
化学
麻疹
接种疫苗
分子生物学
生物化学
作者
Takao Hanabusa,Toyoyuki Ose,Mitsuru Kubota,Nobuo Maita,Jun Kamishikiryo,Katsumi Maenaka,Yusuke Yanagi
摘要
Measles virus, a major cause of childhood morbidity and mortality worldwide, predominantly infects immune cells using signaling lymphocyte activation molecule (SLAM) as a cellular receptor. Here we present crystal structures of measles virus hemagglutinin (MV-H), the receptor-binding glycoprotein, in complex with SLAM. The MV-H head domain binds to a β-sheet of the membrane-distal ectodomain of SLAM using the side of its β-propeller fold. This is distinct from attachment proteins of other paramyxoviruses that bind receptors using the top of their β-propeller. The structure provides templates for antiviral drug design, an explanation for the effectiveness of the measles virus vaccine, and a model of the homophilic SLAM-SLAM interaction involved in immune modulations. Notably, the crystal structures obtained show two forms of the MV-H-SLAM tetrameric assembly (dimer of dimers), which may have implications for the mechanism of fusion triggering.
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