Lescar J, Roussel A, Wien M W, Navaza J, Fuller S D, Wengler G, Wengler G, Rey F A
Laboratoire de Génétique des Virus, CNRS-UPR 9053, 1, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.
Cell. 2001 Apr 6;105(1):137-48. doi: 10.1016/s0092-8674(01)00303-8.
Semliki Forest virus (SFV) has been extensively studied as a model for analyzing entry of enveloped viruses into target cells. Here we describe the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its interactions at the surface of the virus. E1 is unexpectedly similar to the flavivirus envelope protein, with three structural domains disposed in the same primary sequence arrangement. These results introduce a new class of membrane fusion proteins which display lateral interactions to induce the necessary curvature and direct budding of closed particles. The resulting surface protein lattice is primed to cause membrane fusion when exposed to the acidic environment of the endosome.
作为分析包膜病毒进入靶细胞的模型，Semliki森林病毒（SFV）已得到广泛研究。在此，我们描述了源自3.5埃分辨率电子密度图的SFV融合糖蛋白E1的多肽链轨迹，并描述了其在病毒表面的相互作用。E1意外地与黄病毒包膜蛋白相似，具有以相同一级序列排列的三个结构域。这些结果引入了一类新的膜融合蛋白，它们通过侧向相互作用诱导产生必要的曲率并引导封闭颗粒出芽。当暴露于内体的酸性环境时，由此产生的表面蛋白晶格会引发膜融合。
