ArticleJournal of virology2012
Multiple antigenic sites are involved in blocking the interaction of GII.4 norovirus capsid with ABH histo-blood group antigens.
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.
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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.
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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
44 citing papers in PubMed, 63 citations in OpenAlex.
- Emergence of a novel GII.17 variant is associated with immune evasion rather than an altered HBGA-binding profile.PLoS pathogens · 2026Article
- Balancing under constraint: Structural insights into norovirus evolution and antigenic innovation.PLoS pathogens · 2026Article
- Structural and genetic analysis of neutralizing antibodies reveals mechanisms of GII.4 norovirus antigenic evolution.Research square · 2026Article
- Variable and conserved B cell epitopes of GII.4 human noroviruses.Journal of virology · 2026Review
- GII.17 norovirus re-emerged in the 2020s as a result of dynamic and adaptive evolutionary processes.Nature communications · 2025Article
- Manipulation of immunodominant variable epitopes of norovirus capsid protein elicited cross-blocking antibodies to different GII.4 variants despite the low potency of the polyclonal sera.Journal of virology · 2025Article
- The saga to monitor and control norovirus: the rise of GII.17.The Journal of general virology · 2025Review
- Reconstitution of Norovirus-Specific T-Cell Responses Following Hematopoietic Stem Cell Transplantation in Patients With Inborn Errors of Immunity and Chronic Norovirus Infection.The Journal of infectious diseases · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Identification of a GII.6 norovirus blockade antibody epitope.Virus research · 2023Article
- Mapping human norovirus antigens during infection reveals the breadth of the humoral immune response.NPJ vaccines · 2023Article
- Minimal Antigenic Evolution after a Decade of Norovirus GII.4 Sydney_2012 Circulation in Humans.Journal of virology · 2023Article
- Long Term Norovirus Infection in a Patient with Severe Common Variable Immunodeficiency.Viruses · 2022Article
- Identification and genetic characterization of a minor norovirus genotype, GIX.1[GII.P15], from China.BMC genomic data · 2022Article
- Cross-reactive neutralizing human monoclonal antibodies mapping to variable antigenic sites on the norovirus major capsid protein.Frontiers in immunology · 2022Article
- A luciferase-based approach for measuring HBGA blockade antibody titers against human norovirus.Journal of virological methods · 2021Article
- Antigenic cartography reveals complexities of genetic determinants that lead to antigenic differences among pandemic GII.4 noroviruses.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Characterization of Antigenic Relatedness Among GI Norovirus Genotypes Using Serum Samples From Norovirus-Infected Patients and Mouse Sera.Frontiers in microbiology · 2020Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Noroviruses are major etiological agents of acute viral gastroenteritis. In 2002, a GII.4 variant (Farmington Hills cluster) spread so rapidly in the human population that it predominated worldwide and displaced previous GII.4 strains. We developed and characterized a panel of six monoclonal antibodies (MAbs) directed against the capsid protein of a Farmington Hills-like GII.4 norovirus strain that was associated with a large hospital outbreak in Maryland in 2004. The six MAbs reacted with high titers against homologous virus-like particles (VLPs) by enzyme-linked immunoassay but did not react with denatured capsid protein in immunoblots. The expression and self-assembly of newly developed genogroup I/II chimeric VLPs showed that five MAbs bound to the GII.4 protruding (P) domain of the capsid protein, while one recognized the GII.4 shell (S) domain. Cross-competition assays and mutational analyses showed evidence for at least three distinct antigenic sites in the P domain and one in the S domain. MAbs that mapped to the P domain but not the S domain were able to block the interaction of VLPs with ABH histo-blood group antigens (HBGA), suggesting that multiple antigenic sites of the P domain are involved in HBGA blocking. Further analysis showed that two MAbs mapped to regions of the capsid that had been associated with the emergence of new GII.4 variants. Taken together, our data map antibody and HBGA carbohydrate binding to proximal regions of the norovirus capsid, showing that evolutionary pressures on the norovirus capsid protein may affect both antigenic and carbohydrate recognition phenotypes.
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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.