An intermolecular salt bridge linking substrate binding and P1 substrate specificity switch of arterivirus 3C-like proteases.

ABSTRACT: Equine arteritis virus (EAV) and porcine reproductive and respiratory syndrome virus (PRRSV) represent two members of the family Arteriviridae and pose a major threat to the equine- and swine-breeding industries throughout the world. Previously, we and others demonstrated that PRRSV 3C-like protease (3CL^pro) had very high glutamic acid (Glu)-specificity at the P1 position (P1-Glu). Comparably, EAV 3CL^pro exhibited recognition of both Glu and glutamine (Gln) at the P1 position. However, the underlying mechanisms of the P1 substrate specificity shift of arterivirus 3CL^pro remain unclear. We systematically screened the specific amino acids in the S1 subsite of arterivirus 3CL^pro using a cyclized luciferase-based biosensor and identified Gly11

SUBMITTER: Chen Q 

PROVIDER: S-EPMC9271976 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature