Key result
Specific residues on the surface of the FMDV 3C protein opposite the catalytic site are essential for interaction with cre/bus RNA, VPg uridylylation, and efficient virus replication.
Population
In vitro model of foot-and-mouth disease virus (FMDV) replication components (3B, 3Dpol, 3CD, RNA template)
Design
Preclinical
Authors
Loading...
May guide FMDV antiviral design; leaves open in vivo efficacy and therapeutic translation.
Identifies specific RNA sequences and 3C protein residues essential for VPg uridylylation and FMDV replication in vitro.
Nayak et al. (2006) studied Foot-and-Mouth Disease Virus (FMDV) replication. FMDV 3C protein mutations and RNA structure modifications vs. Wild-type FMDV 3C protein and RNA was evaluated on VPg uridylylation activity and virus replication. Specific residues on the surface of the FMDV 3C protein opposite the catalytic site are essential for interaction with cre/bus RNA, VPg uridylylation, and efficient virus replication.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: