利用冷冻电子显微镜观察蓝舌病病毒颗粒的结构

Structure of bluetongue virus particles by cryoelectron microscopy.

作者信息

Hewat E A, Booth T F, Roy P

机构信息

Laboratoire de Biologie Structurale, CEA and CNRS URA 1333, Grenoble, France.

出版信息

J Struct Biol. 1992 Jul-Aug;109(1):61-9. doi: 10.1016/1047-8477(92)90068-l.

DOI:10.1016/1047-8477(92)90068-l

PMID:1337461

Abstract

The structure of the bluetongue virus (BTV) particle, determined by cryoelectron microscopy and image analysis, reveals a well-ordered outer shell which differs markedly from other known Reoviridae. The inner shell is known to have an icosahedral structure with 260 triangular spikes of VP7 trimers arranged on a T = 13,l lattice. The outer shell is seen to consist of 120 globular regions (possibly VP5), which sit neatly on each of the six-membered rings of VP7 trimers. "Sail"-shaped spikes located above 180 of the VP7 trimers form 60 triskelion-type motifs which cover all but 20 of the VP7 trimers. These spikes are possibly the hemagglutinating protein VP2 which contains a virus neutralization epitope. Thus, VP2 and VP5 together form a continuous layer around the inner shell except for holes on the 5-fold axis.

摘要

通过冷冻电子显微镜和图像分析确定的蓝舌病毒（BTV）颗粒结构显示出一个排列有序的外壳，这与其他已知呼肠孤病毒科病毒明显不同。已知内壳具有二十面体结构，由260个VP7三聚体的三角形刺突排列在T = 13，l晶格上。外壳由120个球状区域（可能是VP5）组成，它们整齐地位于VP7三聚体的每个六元环上。位于180个VP7三聚体上方的“帆”形刺突形成60个三叉戟型基序，覆盖了除20个VP7三聚体之外的所有VP7三聚体。这些刺突可能是含有病毒中和表位的血凝素蛋白VP2。因此，VP2和VP5一起在内壳周围形成一个连续层，但在五重轴上有孔。