Böttcher B, Kiselev N A, Stel'Mashchuk V Y, Perevozchikova N A, Borisov A V, Crowther R A
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
J Virol. 1997 Jan;71(1):325-30. doi: 10.1128/JVI.71.1.325-330.1997.
Infectious bursal disease virus (IBDV), a member of the Birnaviridae group, is a commercially important pathogen of chickens. From electron micrographs of frozen, hydrated, unstained specimens, we have computed a three-dimensional map of IBDV at about 2 nm resolution. The map shows that the structure of the virus is based on a T=13 lattice and that the subunits are predominantly trimer clustered. The subunits close to the fivefold symmetry axes are at a larger radius than those close to the two- or threefold axes, giving the capsid a markedly nonspherical shape. The trimer units on the outer surface protrude from a continuous shell of density. On the inner surface, the trimers appear as Y-shaped units, but the set of units surrounding the fivefold axes appears to be missing. It is likely that the outer trimers correspond to the protein VP2, carrying the dominant neutralizing epitope, and the inner trimers correspond to protein VP3, which has a basic carboxy-terminal tail expected to interact with the packaged RNA.
传染性法氏囊病病毒(IBDV)是双RNA病毒科的成员,是鸡的一种具有重要商业意义的病原体。通过对冷冻、水合、未染色标本的电子显微镜照片,我们计算出了分辨率约为2纳米的IBDV三维图谱。该图谱显示,病毒的结构基于T=13晶格,亚基主要是三聚体簇集。靠近五重对称轴的亚基半径比靠近二重或三重对称轴的亚基大,使衣壳呈现出明显的非球形形状。外表面的三聚体单元从连续的密度壳中突出。在内表面,三聚体呈现为Y形单元,但围绕五重轴的一组单元似乎缺失。外层三聚体可能对应携带主要中和表位的蛋白VP2,内层三聚体可能对应蛋白VP3,其具有预期与包装RNA相互作用的碱性羧基末端尾巴。