ArticleNPJ vaccines2025
Stabilization of norovirus GII.3 virus-like particles by rational disulfide engineering.
Article in NPJ vaccines, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Mucosal Vaccine Development: From Adjuvant Design to Next-Generation Delivery Strategies.Biomedicines · 2026Review
- Engineering strategies and decision frameworks for virus-like particle-based vaccines against infectious diseases.Frontiers in microbiology · 2026Review
Corrections and comments
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Authors and funding
17 authors.
Funding
No grant is acknowledged in the PubMed record.
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 superior reagent in immunological assays compared to the wild-type counterpart. Importantly, mRNA encoding GII.3-DS1 elicits superior humoral immune responses compared to wild-type GII.3 mRNA in mice. These results demonstrate the utility of rational VLP stabilization for advancing vaccine development efforts.
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Registered trials
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