The CUG-initiated larger form coat protein of Chinese wheat mosaic virus binds to the cysteine-rich RNA silencing suppressor
文献类型: 外文期刊
作者: Sun, Liying 1 ; Andika, Ida Sagus 1 ; Shen, Jiangfeng 2 ; Yang, Di 3 ; Ratti, Claudio 4 ; Chen, Jianping 1 ;
作者机构: 1.Zhejiang Acad Agr Sci, State Key Lab Breeding Base Zhejiang Sustainable, MoA Key Lab Plant Protect & Biotechnol, Zhejiang Prov Key Lab Plant Virol,Inst Virol & Bi, Hangzhou 310021, Zhejiang, Peoples R China
2.Zhejiang Normal Univ, Coll Chem & Life Sci, Jinhua 321004, Peoples R China
3.Anhui Agr Univ, Coll Life Sci, Hefei 230036, Peoples R China
4.Univ Bologna, DipSA Plant Pathol, I-40127 Bologna, Italy
关键词: Alternative translation initiation;Chinese wheat mosaic virus;CUG codon;Cysteine-rich suppressor;Furovirus;Larger form coat protein
期刊名称:VIRUS RESEARCH ( 影响因子:3.303; 五年影响因子:3.445 )
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收录情况: SCI
摘要: Some viruses use alternative translation initiation at non-AUG codons as a strategy to produce multiple proteins during gene expression. Here we show that, using this strategy, Chinese wheat mosaic virus (CWMV; Furovirus) expresses a larger form of coat protein (N-ext/CP) in infected plants. Site-directed mutagenesis and transient expression analysis confirmed that CWMV N-ext/CP is initiated at an upstream in-frame CUG codon at nucleotide position 207-209 of RNA 2, which adds a 39 amino acid (aa) N-terminal extension to the major CP. Interestingly, in planta and in vitro analyses indicated that CWMV N-ext/CP but not CP interacts with the CWMV cysteine-rich protein (CRP), an RNA silencing suppressor. We further determined that the N-terminal 39 aa extension, particularly the 10 aa region immediately upstream of the major CP coding region is responsible for the interaction of N-ext/CP with CRP. In an Agrobacterium co-infiltration assay, co-expression with N-ext/CP did not affect CRP silencing suppression activity. Thus the alternative translation initiation at a CUG codon provides the CWMV N-ext/CP with the ability to bind to the viral silencing suppressor.
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