The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus.
The core protein P3 of Rice dwarf virus constructs asymmetric dimers, one of which is inserted by the amino-terminal region of another P3 protein. The P3 proteins with serial amino-terminal deletions, expressed in a baculovirus system, formed particles with gradually decreasing stability. The capacity for self-assembly disappeared when 52 of the amino-terminal amino acids had been deleted. These results demonstrated that insertion of the amino-terminal arm of one P3 protein into another appears to play an important role in stabilizing the core particles.
Laboratory of Virology, National Agricultural Research Center, Tsukuba, Ibaraki 305-8666, Japan.
Kyoji
K
Hagiwara
Takahiko
T
Higashi
Naoyuki
N
Miyazaki
Hisashi
H
Naitow
R Holland
RH
Cheng
Atsushi
A
Nakagawa
Hiroshi
H
Mizuno
Tomitake
T
Tsukihara
Toshihiro
T
Omura
D000818:Animals; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D019281:Dimerization; D017353:Gene Deletion; D008958:Models, Molecular; D017924:Nucleopolyhedroviruses; D012275:Oryza / Q000821:virology*; D012087:Reoviridae / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014771:Virion / Q000378:metabolism*; D019065:Virus Assembly
D036022:Capsid Proteins