Prasad B V, Matson D O, Smith A W
Verna and Marrs Mclean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030.
J Mol Biol. 1994 Jul 15;240(3):256-64. doi: 10.1006/jmbi.1994.1439.
The Caliciviridae comprise a new family of single-stranded RNA viruses. While human caliciviruses cause gastroenteritis, the animal caliciviruses cause a wide range of diseases. We have determined the three-dimensional structure of a primate calicivirus using electron cryomicroscopy and computer image-processing techniques. Calicivirus is one of the rare animal viruses whose capsid is made of a single structural protein. The three-dimensional structure of the virus is distinct from that of any other animal virus. However, there are several architectural similarities with plant viruses such as tomato bushy stunt virus and turnip crinkle virus. The calicivirions are 405 A in diameter and exhibit T = 3 icosahedral symmetry. The main features of the three-dimensional structure are the 32 large surface hollows, 50 A deep and 90 A wide, at the icosahedral 5-fold and 3-fold axes, and the 90 distinctive arch-like capsomeres surrounding these hollows at the local and strict 2-fold axes. Each capsomere is a dimer of the capsid protein. Despite noticeable differences, the three quasi-equivalent subunits show common structural features: the upper bilobed domain, the central stem domain, and the lower shell domain. The 2-fold related capsid proteins interact through the bilobed domains to form the top of the arch. The structural differences between the connectors of the stem and the shell domain among the three subunits suggest the presence of a hinge region that may facilitate the capsid protein to adapt to the three quasi-equivalent environments of the T = 3 icosahedral structure. The shell domains of the pentavalent and hexavalent capsid proteins associate to form a continuous shell between the radii of 115 and 150 A. A beta-barrel structure has been suggested for the shell domain. The mass density in the inner shell between the radius of 85 and 110 A may contain a portion of the capsid protein interacting with the RNA. The features between the 45 and 85 A radius are suggestive of ordered RNA.
杯状病毒科是一类新的单链RNA病毒。人类杯状病毒可引起肠胃炎,而动物杯状病毒会引发多种疾病。我们利用电子低温显微镜和计算机图像处理技术确定了一种灵长类杯状病毒的三维结构。杯状病毒是罕见的衣壳由单一结构蛋白构成的动物病毒之一。该病毒的三维结构与其他任何动物病毒都不同。然而,它与植物病毒(如番茄丛矮病毒和芜菁皱缩病毒)在结构上有一些相似之处。杯状病毒粒子直径为405埃,呈T = 3二十面体对称。三维结构的主要特征是在二十面体的五重轴和三重轴上有32个大的表面凹陷,深50埃、宽90埃,以及在局部和严格的二重轴上围绕这些凹陷的90个独特的拱形衣壳粒。每个衣壳粒是衣壳蛋白的二聚体。尽管存在明显差异,但三个准等价亚基具有共同的结构特征:上部双叶结构域、中央茎结构域和下部壳结构域。二重相关的衣壳蛋白通过双叶结构域相互作用形成拱形的顶部。三个亚基的茎和壳结构域的连接体之间的结构差异表明存在一个铰链区,这可能有助于衣壳蛋白适应T = 3二十面体结构的三个准等价环境。五价和六价衣壳蛋白的壳结构域相互关联,在半径115至150埃之间形成一个连续的壳。有人提出壳结构域具有β桶状结构。半径85至110埃之间内壳的质量密度可能包含一部分与RNA相互作用的衣壳蛋白。半径45至85埃之间的特征表明存在有序的RNA。