ArticleJournal of physics. Condensed matter : an Institute of Physics journal2018
Norovirus-like VP1 particles exhibit isolate dependent stability profiles.
Article in Journal of physics. Condensed matter : an Institute of Physics journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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
18 citing papers in PubMed, 42 citations in OpenAlex.
- Native mass spectrometry meets X-rays for the elucidation of protein structures.Biochemical Society transactions · 2026Review
- X-ray spectroscopy meets native mass spectrometry: probing gas-phase protein complexes.Physical chemistry chemical physics : PCCP · 2025Review
- Structural and stability differences among GI norovirus virus-like particles produced in silkworm-baculovirus expression vector system.Frontiers in microbiology · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Article
- Coherent diffractive imaging of proteins and viral capsids: simulating MS SPIDOC.Analytical and bioanalytical chemistry · 2023Article
- Article
- The Efficacy of Commercial Surface Sanitizers against Norovirus on Formica Surfaces with and without Inclusion of a Wiping Step.Applied and environmental microbiology · 2022Article
- Efficacy of an alcohol-based surface disinfectant formulation against human norovirus.Journal of applied microbiology · 2022Article
- Norovirus-glycan interactions - how strong are they really?Biochemical Society transactions · 2022Article
- Review
- Glycan-Induced Protein Dynamics in Human Norovirus P Dimers Depend on Virus Strain and Deamidation Status.Molecules (Basel, Switzerland) · 2021Article
- N-terminal VP1 Truncations FavorVaccines · 2020Article
- Dynamic rotation of the protruding domain enhances the infectivity of norovirus.PLoS pathogens · 2020Article
- Exosome-mediated human norovirus infection.PloS one · 2020Article
- Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.Protein science : a publication of the Protein Society · 2019Article
- Virus-like particle size and molecular weight/mass determination applying gas-phase electrophoresis (native nES GEMMA).Analytical and bioanalytical chemistry · 2019Article
- Variation of human norovirus GII genotypes detected in Ibaraki, Japan, during 2012-2018.Gut pathogens · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Noroviruses are the main cause of viral gastroenteritis with new variants emerging frequently. There are three norovirus genogroups infecting humans. These genogroups are divided based on the sequence of their major capsid protein, which is able to form virus-like particles (VLPs) when expressed recombinantly. VLPs of the prototypical GI.1 Norwalk virus are known to disassemble into specific capsid protein oligomers upon alkaline treatment. Here, native mass spectrometry and electron microscopy on variants of GI.1 and of GII.17 were performed, revealing differences in terms of stability between these groups. Beyond that, these experiments indicate differences even between variants within a genotype. The capsid stability was monitored in different ammonium acetate solutions varying both in ionic strength and pH. The investigated GI.1 West Chester isolate showed comparable disassembly profiles to the previously studied GI.1 Norwalk virus isolate. However, differences were observed with the West Chester being more sensitive to alkaline pH. In stark contrast to that, capsids of the variant belonging to the currently prevalent genogroup GII were stable in all tested conditions. Both variants formed smaller capsid particles already at neutral pH. Certain amino acid substitutions in the S domain of West Chester relative to the Norwalk virus potentially result in the formation of these T = 1 capsids.
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.