ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structural basis for norovirus neutralization by an HBGA blocking human IgA antibody.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 57 citations in OpenAlex.
- Serum IgA proteomics reveals clonal composition and neutralization of dimeric and monomeric IgA repertoires against human norovirus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Norovirus-specific monoclonal antibodies that block histo-blood group antigen binding isolated from healthy donors.Journal of virology · 2026Article
- Molecular genetic characterisation of norovirus GII.17 strains circulating in South Korea in 2024.Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin · 2026Article
- Variable and conserved B cell epitopes of GII.4 human noroviruses.Journal of virology · 2026Review
- Norovirus replication, host interactions and vaccine advances.Nature reviews. Microbiology · 2025Review
- A broadly protective human antibody for GI genogroup noroviruses.Nature microbiology · 2025Article
- Vaccinia Virus Vector Bivalent Norovirus Vaccine.Viruses · 2025Article
- Patterns of the within-host evolution of human norovirus in immunocompromised individuals and implications for treatment.EBioMedicine · 2024Article
- A quadrivalent norovirus vaccine based on a chimpanzee adenovirus vector induces potent immunity in mice.Virologica Sinica · 2024Article
- Noroviruses: Evolutionary Dynamics, Epidemiology, Pathogenesis, and Vaccine Advances-A Comprehensive Review.Vaccines · 2024Review
- Structural analyses of the GI.4 norovirus by cryo-electron microscopy and X-ray crystallography revealing binding sites for human monoclonal antibodies.Journal of virology · 2024Article
- Article
- A single nanobody neutralizes multiple epochally evolving human noroviruses by modulating capsid plasticity.Nature communications · 2023Article
- Mapping human norovirus antigens during infection reveals the breadth of the humoral immune response.NPJ vaccines · 2023Article
- Intestinal IgA-Coated Bacteria in Healthy- and Altered-Microbiomes (Dysbiosis) and Predictive Value in Successful Fecal Microbiota Transplantation.Microorganisms · 2022Review
- Structural Basis for Rabbit Hemorrhagic Disease Virus Antibody Specificity.Journal of virology · 2022Article
- Immunodominant B-Cell Linear Epitope on the VP1 P Domain of a Feline Norovirus Cat Model.Pathogens (Basel, Switzerland) · 2022Article
- Natural extracts, honey, and propolis as human norovirus inhibitors.Scientific reports · 2022Article
- The Role of Host Glycobiology and Gut Microbiota in Rotavirus and Norovirus Infection, an Update.International journal of molecular sciences · 2021Review
- Glycan Recognition in Human Norovirus Infections.Viruses · 2021Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Human noroviruses (HuNoVs) cause sporadic and epidemic gastroenteritis worldwide. They are classified into two major genogroups (GI and GII), with each genogroup further divided into multiple genotypes. Susceptibility to these viruses is influenced by genetically determined histo-blood group antigen (HBGA) expression. HBGAs function as cell attachment factors by binding to a surface-exposed region in the protruding (P) domain of the capsid protein. Sequence variations in this region that result in differential HBGA binding patterns and antigenicity are suggested to form a basis for strain diversification. Recent studies show that serum antibodies that block HBGA binding correlate with protection against illness. Although genogroup-dependent variation in HBGA binding specificity is structurally well characterized, an understanding of how antibodies block HBGA binding and how genotypic variations affect such blockade is lacking. Our crystallographic studies of the GI.1 P domain in complex with the Fab fragment of a human IgA monoclonal antibody (IgA 5I2) with HBGA blocking activity show that the antibody recognizes a conformational epitope formed by two surface-exposed loop clusters in the P domain. The antibody engulfs the HBGA binding site but does not affect its structural integrity. An unusual feature of the antigen recognition by IgA 5I2 is the predominant involvement of the CDR light chain 1 in contrast to the commonly observed CDR heavy chain 3, providing a unique perspective into antibody diversity in antigen recognition. Identification of the antigenic site in the P domain shows how genotypic variations might allow escape from antibody neutralization and exemplifies the interplay between antigenicity and HBGA specificity in HuNoV evolution.
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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.