日本研究人员在10日的《自然·结构和分子生物学》网络版上发表论文说，他们从原子层面探明麻疹病毒入侵细胞时起重要作用的蛋白质及其受体结合部位的立体结构，这项成果有望帮助人们开发抗麻疹病毒新药。
麻疹病毒表面的“H－蛋白质”在病毒感染细胞时发挥着重要作用，这种蛋白质和人体细胞表面的受体“SLAM”蛋白质相结合，相当于钥匙插入锁孔。这一结合开启了麻疹病毒入侵细胞的进程。
日本九州大学教授柳雄介的研究小组大量合成上述两种蛋白质结合形成的复合体，并使之结晶化。随后，他们通过X射线分析这种结晶，从原子层面探明了其立体结构。研究人员表示，如果能找到具备“堵锁孔”能力的化合物，防止“钥匙插入锁孔”，就有望开发出新的抗麻疹病毒药物。
婴幼儿时期接种疫苗是预防麻疹的有效方法，但由于近年来不曾接种疫苗人数增多或疫苗作用随接种者年龄增长而下降等原因，麻疹疫情在世界范围内出现反弹。
原文出处：
Nature Structural " Molecular Biology doi:10.1038/nsmb.1969
Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
Takao Hashiguchi,Toyoyuki Ose,Marie Kubota,Nobuo Maita,Jun Kamishikiryo,Katsumi Maenaka" Yusuke Yanagi
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.
