Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6140357 | Virology | 2014 | 7 Pages |
â¢The 21 kDa major CP is the product of direct translation of a sgRNA.â¢The 24 kDa minor CP is a cleavage product derived in two ways.â¢Cleavage occurs at an LXG[G/A] motif.â¢Relevant to viruses using papain-like proteases for polyprotein processing.â¢Relevant to protection against degradation via the ubiquitin-proteasome system.
Oat blue dwarf virus (OBDV) is a member of the genus Marafivirus whose genome encodes a 227Â kDa polyprotein (p227) ostensibly processed post-translationally into its functional components. Encoded near the 3' terminus and coterminal with the p227 ORF are ORFs specifying major and minor capsid proteins (CP). Since the CP expression strategy of marafiviruses has not been thoroughly investigated, we produced a series of point mutants in the OBDV CP encoding gene and examined expression in protoplasts. Results support a model in which the 21Â kDa major CP is the product of direct translation of a sgRNA, while the 24Â kDa minor CP is a cleavage product derived from both the polyprotein and a larger ~26Â kDa precursor translated directly from the sgRNA. Cleavage occurs at an LXG[G/A] motif conserved in many viruses that use papain-like proteases for polyprotein processing and protection against degradation via the ubiquitin-proteasome system.