ArticleFrontiers in microbiology2025
Structural and stability differences among GI norovirus virus-like particles produced in silkworm-baculovirus expression vector system.
Article in Frontiers in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Engineering strategies and decision frameworks for virus-like particle-based vaccines against infectious diseases.Frontiers in microbiology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Norovirus (NoV) is a leading cause of acute gastroenteritis worldwide, with genogroups I and II (GI and GII) most frequently detected. NoV Virus-like particles (VLPs) composed of the major capsid protein VP1 (~60 kDa) are essential for vaccine development, yet GI VLPs remain poorly characterized. In this study, VP1 from four epidemiologically relevant GI genotypes was expressed using the silkworm-baculovirus system, and purification conditions were optimized in a genotype-specific manner. Purified VLPs were analyzed using size-exclusion chromatography (SEC), dynamic light scattering (DLS), transmission electron microscopy (TEM), and differential scanning fluorimetry (DSF), and their functional epitopes confirmed via binding to histo-blood group antigens (HBGAs) mimics. Stability assessments revealed genotype-dependent differences in pH and thermal tolerance, including aggregation and structural transitions. Collectively, these findings define genotype-specific purification, structural characterization, and stability profiles for four GI NoV VLPs. This work provides the first systematic framework for understanding GI-specific constraints in VLP production and offers foundational data that directly inform the design and formulation of multivalent NoV vaccines.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.