Roche Stéphane, Rey Félix A, Gaudin Yves, Bressanelli Stéphane
CNRS, Unité Mixte de Recherche (UMR) 2472, Institut National de la Recherche Agronomique (INRA), UMR 1157, Institut Fédératif de Recherche 115, Laboratoire de Virologie Moléculaire et Structurale, 91198, Gif sur Yvette, France.
Science. 2007 Feb 9;315(5813):843-8. doi: 10.1126/science.1135710.
Glycoprotein G of the vesicular stomatitis virus triggers membrane fusion via a low pH-induced structural rearrangement. Despite the equilibrium between the pre- and postfusion states, the structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G. Comparison with the structure of the postfusion form suggests a pathway for the conformational change. In the prefusion form, G has the shape of a tripod with the fusion loops exposed, which point toward the viral membrane, and with the antigenic sites located at the distal end of the molecule. A large number of G glycoproteins, perhaps organized as in the crystals, act cooperatively to induce membrane merging.
水疱性口炎病毒的糖蛋白G通过低pH诱导的结构重排触发膜融合。尽管融合前和融合后状态之间存在平衡，但以3.0埃分辨率确定的融合前形式的结构表明，融合转变需要G进行广泛的结构重组。与融合后形式的结构比较提示了构象变化的途径。在融合前形式中，G呈三脚架形状，融合环暴露，指向病毒膜，抗原位点位于分子的远端。大量的G糖蛋白，可能如晶体中那样组织，协同作用诱导膜融合。
