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Characterization of Alternanthera mosaic virus and its Coat Protein.

ABSTRACT: A new isolate of Alternantheramosaic virus (AltMV-MU) was purified from Portulaca grandiflora plants. It has been shown that the AltMV-MU coat protein (CP) can be efficiently reassembled in vitro under different conditions into helical RNA-free virus-like particles (VLPs) antigenically related to native virus. The AltMV-MU and VLPs were examined by atomic force and transmission electron microscopies. The encapsidated AltMV-MU RNA is nontranslatable in vitro. However, it can be translationally activated by CP phosphorylation or by binding to the TGB1protein from the virus-coded movement triple gene block.

SUBMITTER: Mukhamedzhanova AA

PROVIDER: S-EPMC3245411 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Characterization of Alternanthera mosaic virus and its Coat Protein.

Mukhamedzhanova Anna A AA Smirnov Alexander A AA Arkhipenko Marina V MV Ivanov Peter A PA Chirkov Sergey N SN Rodionova Nina P NP Karpova Olga V OV Atabekov Joseph G JG

The open virology journal 20111121

A new isolate of Alternantheramosaic virus (AltMV-MU) was purified from Portulaca grandiflora plants. It has been shown that the AltMV-MU coat protein (CP) can be efficiently reassembled in vitro under different conditions into helical RNA-free virus-like particles (VLPs) antigenically related to native virus. The AltMV-MU and VLPs were examined by atomic force and transmission electron microscopies. The encapsidated AltMV-MU RNA is nontranslatable in vitro. However, it can be translationally a ...[more]

PMID: 22216073

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