Turnip crinkle virus coat protein mediates suppression of RNA silencing in Nicotiana benthamiana

被引:162
作者
Thomas, CL
Leh, V
Lederer, C
Maule, AJ
机构
[1] John Innes Ctr Plant Sci Res, Norwich NR4 7UH, Norfolk, England
[2] Inst Bot, UPRESA 7010, Lab Dynam Evolut & Express Gnomes Microorganismes, F-67083 Strasbourg, France
[3] Cyprus Inst Neurol & Genet, Nicosia, Cyprus
基金
英国生物技术与生命科学研究理事会;
关键词
turnip crinkle virus; RNA silencing; suppressor; coat protein; capsid; resistance; Nicotiana; Arabidopsis;
D O I
10.1016/S0042-6822(02)00018-1
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
All of the protein products of Turnip crinkle virus (TCV; Tombusviridae, Carmovirus) were tested for their ability to suppress RNA silencing of a reporter gene after transient expression in Agrobacterium-infiltrated Nicotiana benthamiana leaves. Only the capsid protein, P38, showed suppression activity, although this was not obvious when P38 was expressed as part of a TCV infection of the same tissues. When P38 was expressed from a PVX vector, symptoms with enhanced severity that correlated with increased PVX RNA accumulation were observed. This contradiction between ectopic expression of P38 and TCV infection could be accounted for if the active determinant of suppressor activity within P38 was sequestered within the capsid protein structure. The N-terminal 25 amino acids were shown to be important for this activity. This region forms part of the unexposed R-domain that interacts with the RNA within the virus particle. This observation throws light on some of the complex biology exhibited by TCV. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:33 / 41
页数:9
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