The CUG-initiated larger form coat protein of Chinese wheat mosaic virus binds to the cysteine-rich RNA silencing suppressor

Liying Sun, Ida Bagus Andika, Jiangfeng Shen, Di Yang, Claudio Ratti, Jianping Chen

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)66-74
Number of pages9
JournalVirus research
Volume177
Issue number1
DOIs
Publication statusPublished - Oct 1 2013

Keywords

  • Alternative translation initiation
  • CUG codon
  • Chinese wheat mosaic virus
  • Cysteine-rich suppressor
  • Furovirus
  • Larger form coat protein

ASJC Scopus subject areas

  • Cancer Research
  • Virology
  • Infectious Diseases

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