ArticleVirology2015
Strain-specific interaction of a GII.10 Norovirus with HBGAs.
Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Intestinal Norovirus Binding Patterns in Nonsecretor Individuals.Journal of virology · 2022Article
- Evolutionary Analysis of theFrontiers in microbiology · 2019Article
- Structural basis of host ligand specificity change of GII porcine noroviruses from their closely related GII human noroviruses.Emerging microbes & infections · 2019Article
- Quantifying the binding stoichiometry and affinity of histo-blood group antigen oligosaccharides for human noroviruses.Glycobiology · 2018Article
- Development of a Surrogate Neutralization Assay for Norovirus Vaccine Evaluation at the Cellular Level.Viruses · 2018Article
- Characterization of the new GII.17 norovirus variant that emerged recently as the predominant strain in China.The Journal of general virology · 2016Article
- An outbreak caused by GII.17 norovirus with a wide spectrum of HBGA-associated susceptibility.Scientific reports · 2015Article
- A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface.PLoS pathogens · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Noroviruses (NoVs), an important cause of gastroenteritis in humans, recognize human histo-blood group antigens (HBGAs) as receptors. The crystal structures of the protruding (P) domain of a GII.10 NoV (Vietnam 026) in complex with various HBGA oligosaccharides were elucidated. However, the HBGA binding profile of this virus remains unknown. In this study, we determined the saliva and oligosaccharide binding profiles of this virus and the roles of amino acids that are involved in HBGA binding. Our data showed that Vietnam 026 bound to all ABO secretor and non-secretor saliva with clear signals detected by monoclonal antibodies against H3, H1, Le(y), Le(a) and sialyl Le(a). Mutagenesis study confirmed the binding site determined by the crystallography study, in which single mutations wiped out the binding function. We also identified amino acids surrounding the central binding pocket that may participate in the binding by affecting the HBGA binding specificity of the GII.10 NoV.
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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.