In Vitro Synthesis of Cowpea Chlorotic Mottle Virus Polypeptides

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Virion swelling is not required for cotranslational disassembly of cowpea chlorotic mottle virus in vitro.

The mechanism by which virions of cowpea chlorotic mottle virus (CCMV) disassemble and allow for translation of the virion RNA is not well understood. Previous models have suggested that virion swelling is required to expose the virion RNA for translation in a process referred to as cotranslational disassembly (M. Brisco, R. Hull, and T. M. A. Wilson, Virology 148:210-217, 1986; J. W. Roenhorst...

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The structure of cucumber mosaic virus and comparison to cowpea chlorotic mottle virus.

The structure of cucumber mosaic virus (CMV; strain Fny) has been determined to a 3.2-A resolution using X-ray crystallography. Despite the fact that CMV has only 19% capsid protein sequence identity (34% similarity) to cowpea chlorotic mottle virus (CCMV), the core structures of these two members of the Bromoviridae family are highly homologous. As suggested by a previous low-resolution struct...

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Structural rigidity in the capsid assembly of cowpea chlorotic mottle virus

The cowpea chlorotic mottle virus (CCMV) has a protein cage, or capsid, which encloses its genetic material. The structure of the capsid consists of 180 copies of a single protein that self-assemble inside a cell to form a complete capsid with icosahedral symmetry. The icosahedral surface can be naturally divided into pentagonal and hexagonal faces, and the formation of either of these faces ha...

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Replication and Properties of Cowpea Chlorotic Mottle Virus in Resistant Cowpeas

WYATT, S. D., and C. W. KUHN. 1979. Replication and properties of cowpea chlorotic mottle virus in resistant cowpeas. Phytopathology 69:125129. Although cowpea chlorotic mottle virus (CCMV) caused no symptoms pool of RNA formed soon after inoculation. Several properties of CCMV on cowpea P1 186465, virus could be isolated from the inoculated primary produced in the resistant plants were similar...

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Versatile post-functionalization of the external shell of cowpea chlorotic mottle virus by using click chemistry.

We present the modification of the outer protein shell of cowpea chlorotic mottle virus (CCMV) with linear and strained alkyne groups. These functionalized protein capsids constitute valuable platforms for post-functionalization via click chemistry. After modification, the integrity of the capsid and the reversible disassembly behavior are preserved.

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ژورنال

عنوان ژورنال: Journal of General Virology

سال: 1979

ISSN: 0022-1317,1465-2099

DOI: 10.1099/0022-1317-44-2-545