Anna A Mukhamedzhanova, Alexander A Smirnov, Marina V Arkhipenko, Peter A Ivanov, Sergey N Chirkov, Nina P Rodionova, Olga V Karpova, Joseph G Atabekov
{"title":"Characterization of Alternanthera mosaic virus and its Coat Protein.","authors":"Anna A Mukhamedzhanova, Alexander A Smirnov, Marina V Arkhipenko, Peter A Ivanov, Sergey N Chirkov, Nina P Rodionova, Olga V Karpova, Joseph G Atabekov","doi":"10.2174/1874357901105010136","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":23111,"journal":{"name":"The Open Virology Journal","volume":"5 ","pages":"136-40"},"PeriodicalIF":0.0000,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2174/1874357901105010136","citationCount":"15","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Open Virology Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1874357901105010136","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2011/11/21 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15
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.
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