Structure of Senecavirus A 3C Protease Revealed the Cleavage Pattern of 3C Protease in Picornaviruses.

ABSTRACT: Senecavirus A (SVA) is an emerging picornavirus infecting porcine of all age groups and causing foot and mouth disease (FMD)-like symptoms. One of its key enzymes is the 3C protease (3C^pro), which is similar to other picornaviruses and essential for virus maturation by controlling polyprotein cleavage and RNA replication. In this study, we reported the crystal structure of SVA 3C^pro at a resolution of 1.9 Å and a thorough structural comparison against all published picornavirus 3C^pro structures. Using statistical and graphical visualization techniques, we also investigated the sequence specificity of the 3C^pro. The structure revealed that SVA 3C^pro adopted a typical chymotrypsin-like fold with the S1 subsite as the most conservative si

SUBMITTER: Meng K 

PROVIDER: S-EPMC9278111 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature