STRUCTURE OF CORRECTLY SELF-ASSEMBLED BLUETONGUE VIRUS-LIKE PARTICLES
STRUCTURE OF CORRECTLY SELF-ASSEMBLED BLUETONGUE VIRUS-LIKE PARTICLES
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DOI：
10.1006/jsbi.1994.1019
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发表时间：
1994-05-01
影响因子：
3
通讯作者：
ROY, P
中科院分区：
文献类型：
--
作者：
HEWAT, EA;BOOTH, TF;ROY, P
用重组杆状病毒共表达VP2、VP3、VP5和VP7合成的蓝舌病毒样颗粒(VLP)进行了冷冻电子显微镜和图像分析。对这些VLP的三维重建显示了一个直径为86 nm的二十面体结构，其特征与天然蓝舌病毒(BTV)颗粒基本相同。因此，VLP含有作为天然病毒颗粒的四种组成蛋白，其中每一种蛋白的位置都被高度占据。由于VP3和VP7共表达形成的BTV核心样颗粒在五重轴周围各缺少五个VP7三聚体，因此外衣壳蛋白VP2和VP5的存在似乎是这些VP7三聚体围绕五重轴黏附所必需的。在没有BTV非结构蛋白的情况下观察到的完整VLP的自发形成表明，非结构蛋白不是形成双壳病毒衣壳所必需的。然而，非结构蛋白可能参与基因组复制和包装的不同方面。(C)1994年学术出版社。
Bluetongue virus-like particles (VLPs), synthesized by coexpression of VP2, VP3, VP5, and VP7 using recombinant baculoviruses, have been examined by cryoelectron microscopy and image analysis. The 3-D reconstruction of these VLPs reveals an icosahedral structure 86 nm in diameter with essentially the same features as for the native Bluetongue virus (BTV) particle. The VLP is thus shown to contain the four constituent proteins as the native virus particle, with each of the protein positions highly occupied. Since the BTV core-like particle formed by coexpression of VP3 and VP7 lacks five VP7 trimers around each of the five-fold axes, it appears that the presence of the outer capsid proteins VP2 and VP5 is necessary for the adhesion of these VP7 trimers around the five-fold axes. The observed spontaneous formation of complete VLP in the absence of the BTV nonstructural proteins implies that the nonstructural proteins are not necessary for the formation of the double-shelled viral capsid. However, the nonstructural proteins may be involved in different aspects of genome replication and packaging. (C) 1994 Academic Press, Inc.