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.
Department of Virology, Moscow State University, Moscow 119991, Russia.
Anna A
AA
Mukhamedzhanova
Alexander A
AA
Smirnov
Marina V
MV
Arkhipenko
Peter A
PA
Ivanov
Sergey N
SN
Chirkov
Nina P
NP
Rodionova
Olga V
OV
Karpova
Joseph G
JG
Atabekov