Stabilization of norovirus GII.3 virus-like particles by rational disulfide engineering.

ABSTRACT: Noroviruses are non-enveloped, single-stranded positive-sense RNA viruses and the leading cause of gastroenteritis worldwide. The major capsid protein, VP1, can self-assemble into non-infectious virus-like particles (VLPs), representing an attractive vaccine platform. It was demonstrated that engineered disulfide bonds within VP1 could significantly stabilize VLPs of the archetypal GI.1 strain. Here, we apply a similar strategy to VLPs of multiple circulating GII genotypes. We find that engineered disulfide mutations can significantly stabilize VLPs of the GII.3 strain, but not the closely related GII.6 strain. Disulfide-stabilized GII.3 VLPs (GII.3-DS1) exhibit increased yields, greater homogeneity, and higher thermal stability compared to wild-type GII.3 VLPs. GII.3-DS1 VLPs are a superi

SUBMITTER: Warren C 

PROVIDER: S-EPMC12365219 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature