Hewat E A, Neumann E, Conway J F, Moser R, Ronacher B, Marlovits T C, Blaas D
Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble, France.
EMBO J. 2000 Dec 1;19(23):6317-25. doi: 10.1093/emboj/19.23.6317.
Human rhinovirus serotype 2 (HRV2) belongs to the minor group of HRVs that bind to members of the LDL-receptor family including the very low density lipoprotein (VLDL)-receptor (VLDL-R). We have determined the structures of the complex between HRV2 and soluble fragments of the VLDL-R to 15 A resolution by cryo-electron microscopy. The receptor fragments, which include the first three ligand-binding repeats of the VLDL-R (V1-3), bind to the small star-shaped dome on the icosahedral 5-fold axis. This is in sharp contrast to the major group of HRVs where the receptor site for ICAM-1 is located at the base of a depression around each 5-fold axis. Homology models of the three domains of V1-3 were used to explore the virus-receptor interaction. The footprint of VLDL-R on the viral surface covers the BC- and HI-loops on VP1.
人鼻病毒2型（HRV2）属于鼻病毒的次要组，可与低密度脂蛋白（LDL）受体家族成员结合，包括极低密度脂蛋白（VLDL）受体（VLDL-R）。我们通过冷冻电子显微镜确定了HRV2与VLDL-R可溶性片段之间复合物的结构，分辨率达到15埃。受体片段包括VLDL-R的前三个配体结合重复序列（V1-3），它们结合在二十面体5重轴上的小星形圆顶处。这与主要组鼻病毒形成鲜明对比，在主要组鼻病毒中，细胞间黏附分子-1（ICAM-1）的受体位点位于每个5重轴周围凹陷的底部。利用V1-3三个结构域的同源模型来探索病毒-受体相互作用。VLDL-R在病毒表面的足迹覆盖了VP1上的BC环和HI环。
