ArticleJournal of virology2012
Structural basis for norovirus inhibition and fucose mimicry by citrate.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 84 citations in OpenAlex.
- Multi-Ligand Interactions Shape Human Norovirus Persistence, Transmission, and Control in Food Matrices.Viruses · 2026Review
- Large-scale gastroenteritis outbreaks occurring in a university town of Guangzhou city during the global wave of the norovirus in China.Virology journal · 2026Article
- Lemon Juice Activity Against Caprine Alphaherpesvirus-1: An In Vitro Study.Antibiotics (Basel, Switzerland) · 2026Article
- Virucidal Activity of Lemon Juice Against Feline Calicivirus, Surrogate of Norovirus.Antibiotics (Basel, Switzerland) · 2025Article
- Antiviral Activity of Natural Compounds for Food Safety.Food and environmental virology · 2024Review
- Development of a broad-spectrum therapeutic Fc-nanobody for human noroviruses.Journal of virology · 2024Article
- Article
- Natural extracts, honey, and propolis as human norovirus inhibitors.Scientific reports · 2022Article
- Norovirus-glycan interactions - how strong are they really?Biochemical Society transactions · 2022Article
- Evolution of the interactions between GII.4 noroviruses and histo-blood group antigens: Insights from experimental and computational studies.PLoS pathogens · 2021Article
- NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins.Viruses · 2021Article
- Nanobody-Mediated Neutralization Reveals an Achilles Heel for Norovirus.Journal of virology · 2020Article
- F-Specific RNA Bacteriophages Model the Behavior of Human Noroviruses during Purification of Oysters: the Main Mechanism Is Probably Inactivation Rather than Release.Applied and environmental microbiology · 2020Article
- Human Norovirus Proteins: Implications in the Replicative Cycle, Pathogenesis, and the Host Immune Response.Frontiers in immunology · 2020Review
- Norovirus Attachment and Entry.Viruses · 2019Review
- Norovirus antivirals: Where are we now?Medicinal research reviews · 2019Review
- A post-translational modification of human Norovirus capsid protein attenuates glycan binding.Nature communications · 2019Article
- Structural Basis of Nanobodies Targeting the Prototype Norovirus.Journal of virology · 2019Article
- Foodborne viruses: Detection, risk assessment, and control options in food processing.International journal of food microbiology · 2018Review
- Quantifying the binding stoichiometry and affinity of histo-blood group antigen oligosaccharides for human noroviruses.Glycobiology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Human noroviruses bind with their capsid-protruding domains to histo-blood-group antigens (HBGAs), an interaction thought to direct their entry into cells. Although human noroviruses are the major cause of gastroenteritis outbreaks, development of antivirals has been lacking, mainly because human noroviruses cannot be cultivated. Here we use X-ray crystallography and saturation transfer difference nuclear magnetic resonance (STD NMR) to analyze the interaction of citrate with genogroup II (GII) noroviruses. Crystals of citrate in complex with the protruding domain from norovirus GII.10 Vietnam026 diffracted to 1.4 Å and showed a single citrate bound at the site of HBGA interaction. The citrate interaction was coordinated with a set of capsid interactions almost identical to that involved in recognizing the terminal HBGA fucose, the saccharide which forms the primary conserved interaction between HBGAs and GII noroviruses. Citrate and a water molecule formed a ring-like structure that mimicked the pyranoside ring of fucose. STD NMR showed the protruding domain to have weak affinity for citrate (460 μM). This affinity, however, was similar to the affinities of the protruding domain for fucose (460 μM) and H type 2 trisaccharide (390 μM), an HBGA shown previously to be specifically recognized by human noroviruses. Importantly, competition STD NMR showed that citrate could compete with HBGA for norovirus binding. Together, the results suggest that citrate and other glycomimetics have the potential to block human noroviruses from binding to HBGAs.
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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.