Key Points
- Map the primary translation and cleavage products of foot-and-mouth disease virus (FMDV) to establish the gene order across its viral genome.
- Infected BHK 21 cells with FMDV and monitored protein processing using amino acid analogues and proteolytic enzyme inhibitors.
- Mapped the sequential order of structural and non-structural cleavage products across the viral genome using emetine.
- Identified four primary cleavage products (P100, P88, P56, and P52), with no detectable precursor polyprotein representing their combined molecular weight.
- Mapped the 5'-terminal precursor P88 to capsid polypeptides in the order VP4-VP2-VP3-VP1, followed downstream by P52, P56 (identical to virus infection-associated antigen), and P100.
- Showed that FMDV encodes an extra primary cleavage product compared to other picornaviruses, reflecting translation of a larger portion of the viral genome.
Structured PICO
PPopulationBHK 21 cells infected with foot-and-mouth disease virus (FMDV)
IInterventionAmino acid analogues, proteolytic enzyme inhibitors, and emetine
OOutcomeIdentification and mapping of primary cleavage products and structural polypeptidessurrogate
FMDV differs from other picornaviruses by having an extra primary cleavage product, with its structural polypeptides ordered as VP4, VP2, VP3, VP1.