Production of virus-like particles of FMDV by 3C protease cleaving precursor polyprotein P1 in vitro.

ABSTRACT: Nonstructural protein 3C, a master protease of Picornaviridae, plays a critical role in viral replication by directly cleaving the viral precursor polyprotein to form the viral capsid protein and antagonizing the host antiviral response. Additionally, 3C protease, as a tool enzyme, is involved in regulating polyprotein expression. Here, the 3C mutant gene (3Cm), fused with a small ubiquitin-like modifier (SUMO) tag at the N-terminal and featuring a mutation at position 127, was inserted into the cold-shock plasmid pCold of Escherichia coli for expression. Meanwhile, the P1-∆2A plasmid was constructed for expression in Pichia pastoris. The expressions of 3C protein and P1 precursor protein were confirmed by polymerase chain reaction (PCR), polyacrylamide gel electrophoresis (SDS-PAGE), and

SUBMITTER: Li Z 

PROVIDER: S-EPMC11668828 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature