The Open Virology Journal

2011, 5 : 136-140
Published online 2011 November 21. DOI: 10.2174/1874357901105010136
Publisher ID: TOVJ-5-136

RESEARCH ARTICLE
 Characterization of 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 and 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

* 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: amukhamedzhanovamsu@gmail.com

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.

Keywords:

, coat protein, potexviruses, translation activation, triple gene block protein 1, virus-like particles..