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":"互花花叶病毒及其外壳蛋白的鉴定。","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":"{\"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}","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}
Characterization of Alternanthera mosaic virus and its Coat Protein.
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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