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pubmed-article:12642101pubmed:abstractTextThe 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. 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.lld:pubmed
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pubmed-article:12642101pubmed:articleTitleEffects of the cowpea chlorotic mottle bromovirus beta-hexamer structure on virion assembly.lld:pubmed
pubmed-article:12642101pubmed:affiliationDepartment of Plant Sciences Plant Pathology, Montana State University, Bozeman, MT 59717, USA.lld:pubmed
pubmed-article:12642101pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12642101pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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