Affiliation:
1. Department of Metabolic Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK
Abstract
The small (S) coat protein of Cowpea mosaic virus (CPMV) has been identified previously as a virus-encoded suppressor of post-transcriptional gene silencing (PTGS). Deletions within the C-terminal 24 aa of this protein affect the yield and systemic spread of the virus, suggesting that the C-terminal amino acids of the S protein, which are exposed on the surface of assembled virus particles, may be responsible for the suppressor activity. To investigate this, versions of CPMV RNA-2 with deletions at the C terminus of the S protein were tested for their ability to counteract PTGS in leaf-patch tests. The results showed that the C-terminal 16 aa of the S protein are particularly important for suppressing PTGS and that these amino acids are virus-specific and cannot be substituted by the equivalent sequence from the related virus Bean pod mottle virus.
Cited by
37 articles.
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