Effects of the Cowpea chlorotic mottle bromovirus β-hexamer structure on virion assembly
Effects of the Cowpea chlorotic mottle bromovirus β-hexamer structure on virion assembly
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DOI:
10.1016/s0042-6822(02)00054-5
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发表时间:
2003-02-15
期刊:
影响因子:
3.7
通讯作者:
Young, MJ
中科院分区:
文献类型:
--
作者:
Willits, D;Zhao, X;Young, MJ
The X-ray crystal structure of Cowpea chlorotic mottle bromovirus (CCMV) revealed a unique tubular structure formed by the interaction of the N-termini from six coat protein subunits at each three-fold axis of the assembled virion. This structure, termed the beta-hexamer, consists of six short beta-strands. The beta-hexamer was postulated to play a critical role in the assembly and stability of the virion by stabilizing hexameric capsomers (Speir et al., 1995). Mutational analyses of the beta-hexamer structure, utilizing both in vitro and in vivo assembly assays, demonstrate that this structure is not required for virion formation devoid of nucleic acids in vitro or for RNA-containing virions in vivo. However, the beta-hexamer structure does contribute to virion stability in vitro and modulates disease expression in vivo. These results support a model for CCMV assembly through pentamer intermediates. (C) 2003 Elsevier Science (USA). All rights reserved.