ArticleJournal of virology2019
Human Norovirus Neutralized by a Monoclonal Antibody Targeting the Histo-Blood Group Antigen Pocket.
Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- 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
- 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
- Current Perspectives and Future Directions in the Immunogenicity Landscape of Norovirus Vaccines.Journal of microbiology and biotechnology · 2025Review
- Molecular Evolution and Epidemiology of Norovirus GII.4 Viruses in the United States.The Journal of infectious diseases · 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
- Norovirus replication, host interactions and vaccine advances.Nature reviews. Microbiology · 2025Review
- A broadly protective human antibody for GI genogroup noroviruses.Nature microbiology · 2025Article
- Article
- In Vitro Culture of Human Norovirus in the Last 20 Years.Biomedicines · 2024Review
- Development of a broad-spectrum therapeutic Fc-nanobody for human noroviruses.Journal of virology · 2024Article
- 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
- Human norovirus cultivation systems and their use in antiviral research.Journal of virology · 2024Review
- Linear epitopes on the capsid protein of norovirus commonly elicit high antibody response among past-infected individuals.Virology journal · 2023Article
- Mapping human norovirus antigens during infection reveals the breadth of the humoral immune response.NPJ vaccines · 2023Article
- Emergent variant modeling of the serological repertoire to norovirus in young children.Cell reports. Medicine · 2023Article
- Structural Basis for Rabbit Hemorrhagic Disease Virus Antibody Specificity.Journal of virology · 2022Article
- Feasibility of Polyclonal Avian Immunoglobulins (IgY) as Prophylaxis against Human Norovirus Infection.Viruses · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Temporal changes in the GII.4 human norovirus capsid sequences occasionally result in the emergence of genetic variants capable of causing new epidemics. The persistence of GII.4 is believed to be associated with the recognition of numerous histo-blood group antigen (HBGA) types and antigenic drift. We found that one of the earliest known GII.4 isolates (in 1974) and a more recent epidemic GII.4 variant (in 2012) had varied norovirus-specific monoclonal antibody (MAb) reactivities but similar HBGA binding profiles. To better understand the binding interaction of one MAb (10E9) that had varied reactivity with these GII.4 variants, we determined the X-ray crystal structure of the NSW-2012 GII.4 P domain 10E9 Fab complex. We showed that the 10E9 Fab interacted with conserved and variable residues, which could be associated with antigenic drift. Interestingly, the 10E9 Fab binding pocket partially overlapped the HBGA pocket and had direct competition for conserved HBGA binding residues (i.e., Arg345 and Tyr444). Indeed, the 10E9 MAb blocked norovirus virus-like particles (VLPs) from binding to several sources of HBGAs. Moreover, the 10E9 antibody completely abolished virus replication in the human norovirus intestinal enteroid cell culture system. Our new findings provide the first direct evidence that competition for GII.4 HBGA binding residues and steric obstruction could lead to norovirus neutralization. On the other hand, the 10E9 MAb recognized residues flanking the HBGA pocket, which are often substituted as the virus evolves. This mechanism of antigenic drift likely influences herd immunity and impedes the possibility of acquiring broadly reactive HBGA-blocking antibodies.
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