The study clarifies the biochemical map of foot-and-mouth disease virus RNA, identifying three primary protein products and alternative cleavage pathways for P100.
Challenges prior FMDV polyprotein mapping; reassigns P56 as a P100 cleavage product rather than primary.
The proteins induced by infection of BHK 21 cells with foot-and-mouth disease virus have been compared by tryptic peptide analysis. The results indicate that there are three primary products 5'--P88, P52, P100--3'. The polypeptide P56, which we considered previously to be a primary product, is derived from the region of the genome that codes for P100. The results indicate that there are alternative cleavage pathways of P100, the polypeptide coded for by the 3' end of the genome.
No takes yet. Share an insight, caveat, or question.
Doel et al. (1978) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: