Activity and cryo-EM structure of the polymerase domain of the human norovirus ProPol precursor.

ABSTRACT: Human norovirus (HuNV) is a leading cause of acute gastroenteritis worldwide with most infections caused by genogroup I and genogroup II (GII) viruses. Replication of HuNV generates both precursor and mature proteins during processing of the viral polyprotein that are essential to the viral lifecycle. One such precursor is protease-polymerase (ProPol), a multi-functional enzyme comprised of the norovirus protease and polymerase proteins. This work investigated HuNV ProPol by determining the de novo polymerase activity, protein structure, and antiviral inhibition profile. The GII ProPol de novo enzymatic efficiencies (k_cat/K_m) for RNA templates and ribonucleotides were equal or superior to those of mature GII Pol on all templates measured. F

SUBMITTER: McSweeney AM 

PROVIDER: S-EPMC11575396 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature