Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing
Author(s) -
M. Carmen Cañizares,
KM Taylor,
George P. Lomonossoff
Publication year - 2004
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/vir.0.80454-0
Subject(s) - biology , coat protein , virology , terminal (telecommunication) , coat , cowpea mosaic virus , alfalfa mosaic virus , gene silencing , amino acid , virus , amino terminal , plant virus , mosaic virus , peptide sequence , biochemistry , rna , gene , telecommunications , paleontology , computer science
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.
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