ArticleJournal of virology2008
Crystal structure of unliganded influenza B virus hemagglutinin.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 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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Who cites it
97 citing papers in PubMed, 150 citations in OpenAlex.
- Epidemiological and Evolutionary Dynamics of Influenza B Viruses in Malaysia, 2012-2014.PloS one · 2015Trial
- Epistasis facilitates the long-term antigenic evolution of the influenza B virus hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- Strain Matching of Seasonal Influenza Vaccines and Emergence of Neuraminidase Inhibitor Resistance in China from 2015 to 2025.Vaccines · 2026Article
- Retooling a novel influenza B hemagglutinin to redirect neutralizing antibodies against B/Victoria strains.Vaccine · 2026Article
- Influenza B mosaic HA mRNA-LNP vaccines are cross-reactive and protective in mice.Molecular therapy. Nucleic acids · 2026Article
- Molecular and antigenic characteristics of the influenza B virus in Guangzhou, 2022-2023.Virology journal · 2026Article
- Genomic Characterization and Phylogenetic Analysis ofViruses · 2026Article
- Genetic characterization and whole-genome sequencing-based genetic analysis of influenza B in Shandong Province during 2015-2024.Scientific reports · 2026Article
- Viral pathogens in the etiology of acute respiratory infections in Bulgaria during the 2024-2025 season and genetic diversity of circulating influenza viruses.Frontiers in microbiology · 2026Article
- A single mutation at position 214 of influenza B hemagglutinin enhances cross-neutralization.Emerging microbes & infections · 2025Article
- Unraveling the mechanism behind the probable extinction of the B/Yamagata lineage of influenza B viruses.Nature communications · 2025Article
- N-glycosylation at the receptor binding site drives differences in receptor binding specificity between influenza B virus lineages.Journal of virology · 2025Article
- Unsupervised classification of influenza virus surface spikes from cryo-EM reconstructions using head-to-stem width ratio.Virology journal · 2025Article
- Article
- Epidemiological dynamics of influenza B virus across multiple seasons in Kenya and Uganda inferred from sequence data, 2010-2021.BMC infectious diseases · 2025Article
- Molecular and phylogenetic analysis of influenza A and B viruses circulating in Sri Lanka following the COVID-19 pandemic.Virus genes · 2025Article
- Seroprevalence of anti-influenza antibodies in humans and characterization of seasonal influenza viruses isolated in Russia during the 2023-2024 flu season.Archives of virology · 2025Article
- Neuraminidase-specific antibodies drive differential cross-protection between contemporary FLUBV lineages.Science advances · 2025Article
- Article
- Antigenic analysis of the influenza B virus hemagglutinin protein.Virologica Sinica · 2025Article
37 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 A. At a sequence identity of approximately 25% to influenza A virus HAs, B/HK HA shares a similar overall structure and domain organization. More than two dozen amino acid substitutions on influenza B virus HAs have been identified to cause antigenicity alteration in site-specific mutants, monoclonal antibody escape mutants, or field isolates. Mapping these substitutions on the structure of B/HK HA reveals four major epitopes, the 120 loop, the 150 loop, the 160 loop, and the 190 helix, that are located close in space to form a large, continuous antigenic site. Moreover, a systematic comparison of known HA structures across the entire influenza virus family reveals evolutionarily conserved ionizable residues at all regions along the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins.
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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.