The nonstructural protein 13 of porcine deltacoronavirus coordinates ATP-driven duplex unwinding and ATP-independent strand annealing for nucleic acid remodeling.

ABSTRACT:

Background

Swine diarrheal death caused by intestinal coronavirus is a key problem that needs to be solved urgently in pig production. Porcine deltacoronavirus (PDCoV) is a novel enteropathogenic coronavirus that causes acute diarrhea in suckling piglets, resulting in serious economic losses to the cultivation industry. PDCoV helicase NSP13 plays a pivotal role in virus replication and is regarded as an ideal drug target, but its enzymatic characteristics remain poorly characterized.

Results

In this study, we systematically investigated the biochemical properties of PDCoV NSP13 through recombinant expression and functional assays. Our findings revealed that PDCoV NSP13 exhibited a 5'-to-3' directional unwinding activity powered by broad-spectrum nucleoside triphosphate hydro

SUBMITTER: Tao L 

PROVIDER: S-EPMC12220409 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature