Key result
The crystal structure of Senecavirus A 3C protease was solved at 1.9 Å resolution, revealing a wider S4 pocket and smaller S1 and S1' pockets compared to other picornaviral 3C proteases.
Why the study?
Most picornaviruses lack effective vaccines and drugs, and the 3C protease plays a critical role in virus maturation.
The determination of the SVA 3C protease crystal structure provides structural insights that may guide the design of efficient 3C proteases for picornaviral virus-like particle production.
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 (3C pro ), 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 3C pro at 1.9 Å resolution. The results showed several differences of the binding groove within picornaviral 3C pro , and prompted that the accommodate ability of the pocket may associate with the cleavage efficiency. The further research on 3C pro cleavage efficiency based on structural biology, will prospectively provide an instruction on designing of efficient 3C pro for universally proteolysis in picornaviral VLP production.
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Meng et al. (2020) studied Senecavirus A. X-ray crystallography was evaluated on Crystal structure resolution. The crystal structure of Senecavirus A 3C protease was solved at 1.9 Å resolution, revealing a wider S4 pocket and smaller S1 and S1' pockets compared to other picornaviral 3C proteases.
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