Crystal structure of Senecavirus A 3C protease

Abstract

Senecavirus A (SVA), an emerging picornavirus in porcine population, could infect porcines of all age group and cause FMD-like symptoms. Picornaviridae, a group of RNA viruses do harm to both human and stocks; however, most of picornaviruses are lack of effective vaccines and drugs. Picornaviral 3C protease (3Cpro), as an important role in virus maturation, they basically take charge of poly-protein cleavaging, RNA replication, and multiple interventions on host cells. In this study, we successfully solved the crystal structure of 3Cpro at 1.9 [A] resolution. The results showed several differences of the binding groove within picornaviral 3Cpro, and prompted that the accommodate ability of the pocket may associate with the cleavage efficiency. The further research on 3Cpro cleavage efficiency based on structural biology, will prospectively provide an instruction on designing of efficient 3Cpro for universally proteolysis in picornaviral VLP production.