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
Identifiers and Pagination:Year: 2011
First Page: 136
Last Page: 140
Publisher Id: TOVJ-5-136
Article History:Received Date: 5/7/2011
Revision Received Date: 9/9/2011
Acceptance Date: 21/9/2011
Electronic publication date: 21/11/2011
Collection year: 2011
open-access license: 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.
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.