Characterization of Alternanthera mosaic virus and its Coat Protein
Anna A Mukhamedzhanova*, 1, Alexander A Smirnov 1, Marina V Arkhipenko 1, Peter A Ivanov 1, Sergey N Chirkov 1, Nina P Rodionova 1, †, Olga V Karpova 1, Joseph G Atabekov 1, 2
1 Department of Virology, Moscow State University, Moscow 119991, Russia
2 A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119991, Russia
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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* Address correspondence to this author at the Department of Virology, Moscow State University, Moscow 119991, Russia; Tel: +7 495 939 33 47; Fax: +7 495 938 0601; E-mail: email@example.com†Deceased on 14 April 2011.