Characterization of Alternanthera mosaic virus and its Coat Protein

A new isolate of Alternanthera mosaic 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 n...

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Autores principales: Mukhamedzhanova, Anna A, Smirnov, Alexander A, Arkhipenko, Marina V, Ivanov, Peter A, Chirkov, Sergey N, Rodionova, Nina P, Karpova, Olga V, Atabekov, Joseph G
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Open 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245411/
https://www.ncbi.nlm.nih.gov/pubmed/22216073
http://dx.doi.org/10.2174/1874357901105010136
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author Mukhamedzhanova, Anna A
Smirnov, Alexander A
Arkhipenko, Marina V
Ivanov, Peter A
Chirkov, Sergey N
Rodionova, Nina P
Karpova, Olga V
Atabekov, Joseph G
author_facet Mukhamedzhanova, Anna A
Smirnov, Alexander A
Arkhipenko, Marina V
Ivanov, Peter A
Chirkov, Sergey N
Rodionova, Nina P
Karpova, Olga V
Atabekov, Joseph G
author_sort Mukhamedzhanova, Anna A
collection PubMed
description A new isolate of Alternanthera mosaic 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.
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spelling pubmed-32454112012-01-03 Characterization of Alternanthera mosaic virus and its Coat Protein Mukhamedzhanova, Anna A Smirnov, Alexander A Arkhipenko, Marina V Ivanov, Peter A Chirkov, Sergey N Rodionova, Nina P Karpova, Olga V Atabekov, Joseph G Open Virol J Article A new isolate of Alternanthera mosaic 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. Bentham Open 2011-11-21 /pmc/articles/PMC3245411/ /pubmed/22216073 http://dx.doi.org/10.2174/1874357901105010136 Text en © Mukhamedzhanova et al.; Licensee Bentham Open. http: //creativecommons.org/licenses/by-nc/3.0/ This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http: //creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Article
Mukhamedzhanova, Anna A
Smirnov, Alexander A
Arkhipenko, Marina V
Ivanov, Peter A
Chirkov, Sergey N
Rodionova, Nina P
Karpova, Olga V
Atabekov, Joseph G
Characterization of Alternanthera mosaic virus and its Coat Protein
title Characterization of Alternanthera mosaic virus and its Coat Protein
title_full Characterization of Alternanthera mosaic virus and its Coat Protein
title_fullStr Characterization of Alternanthera mosaic virus and its Coat Protein
title_full_unstemmed Characterization of Alternanthera mosaic virus and its Coat Protein
title_short Characterization of Alternanthera mosaic virus and its Coat Protein
title_sort characterization of alternanthera mosaic virus and its coat protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245411/
https://www.ncbi.nlm.nih.gov/pubmed/22216073
http://dx.doi.org/10.2174/1874357901105010136
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