The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

被引:40
作者
Carvalho, CM
Wellink, J
Ribeiro, SG
Goldbach, RW
van Lent, JWM
机构
[1] Univ Wageningen & Res Ctr, Dept Plant Sci, Virol Lab, NL-6709 PD Wageningen, Netherlands
[2] Univ Wageningen & Res Ctr, Dept Plant Sci, Mol Biol Lab, NL-6703 HA Wageningen, Netherlands
关键词
D O I
10.1099/vir.0.19101-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Cowpea mosaic virus (CPMV) moves from cell to cell as virus particles which are translocated through a plasmodesmata-penetrating transport tubule made up of viral movement protein (MP) copies. To gain further insight into the roles of the viral MP and capsid proteins (CP) in virus movement, full-length and truncated forms of the IMP were expressed in insect cells using the baculovirus expression system. Using ELISA and blot overlay assays, affinity purified IMP was shown to bind specifically to intact CPMV virions and to the large CP, but not to the small CP. This binding was not observed with a C-terminal deletion mutant of the IMP, although this mutant retained the capacity to bind to other MP molecules and to form tubules. These results suggest that the C-terminal 48 amino acids constitute the virion-binding domain of the MP.
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页码:2271 / 2277
页数:7
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