Structure of double-shelled rice dwarf virus

文献类型： 外文期刊

第一作者： Lu, GY

作者： Lu, GY;Zhou, ZH;Baker, ML;Jakana, J;Cai, DY;Wei, XC;Chen, SX;Gu, XC;Chiu, W

作者机构：

关键词： structure;rice;plant pathogens;coat proteins;electron microscopy;plant pathology;rice dwarf phytoreovirus;Oryza;plant viruses

期刊名称：JOURNAL OF VIROLOGY （ 影响因子：5.103； 五年影响因子：5.078 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： Rice dwarf phytoreovirus (RDV), a member of the Reoviridae family, is a double-stranded RNA virus. Infection of rice plants with RDV reduces crop production significantly and can pose a major economic threat to Southeast Asia. A 25-A three-dimensional structure of the 700-A-diameter RDV capsid was determined by 400-kV electron cryomicroscopy and computer reconstruction. The structure revealed 2 distinctive icosahedral shells: a T=13l outer icosahedral shell composed of 260 trimeric clusters of P8 (46 kDa) and an inner T=1 icosahedral shell of 60 dimers of P3 (114 kDa). Sequence and structural comparisons were made between the RDV outer shell trimer and the 2 crystal conformations (REF and HEX) of the VP7 trimer of bluetongue virus, an animal analogue of RDV. The low-resolution structural match of the RDV outer shell trimer to the HEX conformation of VP7 trimer led to the proposal that P8 consists of an upper domain of beta-sandwich motif and a lower domain of alpha helices. The less well fit REFconformation of VP7 to the RDV trimer may be due to the differences between VP7 and P8 in the sequence of the hinge region that connects the 2 domains. It is suggested that the additional mass density and the absence of a known signalling peptide on thesurface of the RDV outer shell trimer may be responsible for the different interactions between plants and animal reoviruses.

分类号： Q93`R37

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