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

© Mukhamedzhanova et al.; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http: // which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

* 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:
Deceased on 14 April 2011.


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.

Keywords: Alternanthera mosaic virus, coat protein, potexviruses, translation activation, triple gene block protein 1, virus-like particles..