ArticleCell host & microbe2017
Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.
Article in Cell host & microbe, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 64 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.
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Who cites it
64 citing papers in PubMed, 95 citations in OpenAlex.
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Scanning the horizon: deep mutational scanning approaches in virology.Journal of virology · 2026Review
- Pathogenicity and immune response of turkey A(H1N2) influenza virus of swine-origin on turkeys and mice.Veterinary research · 2026Article
- A monoclonal antibody-based, time-resolved fluorescence microsphere immunochromatographic testing strip for rapid and sensitive detection of H7 avian influenza viruses.BMC veterinary research · 2026Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza haemagglutinin.Nature ecology & evolution · 2026Article
- Article
- Isolation, identification, and whole genome sequencing analysis of influenza A virus clinical isolates from Shanghai, China, during 2022-2023.Virology journal · 2026Article
- Host switching mutations in H5N1 influenza hemagglutinin suppress site-specific activation dynamics.Nature communications · 2025Article
- High-throughput neutralization measurements correlate strongly with evolutionary success of human influenza strains.bioRxiv : the preprint server for biology · 2025Article
- Host Switching Mutations in H5N1 Influenza Hemagglutinin Suppress Site-specific Activation Dynamics.bioRxiv : the preprint server for biology · 2025Article
- Seasonal Influenza Viruses Show Distinct Adaptive Dynamics During Growth in Chicken Eggs.Molecular biology and evolution · 2025Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza hemagglutinin.bioRxiv : the preprint server for biology · 2025Article
- Structural and functional analysis of VYD222: a broadly neutralizing antibody against SARS-CoV-2 variants.bioRxiv : the preprint server for biology · 2025Article
- Article
- Analysis of Epidemiological and Evolutionary Characteristics of Seasonal Influenza Viruses in Shenzhen City from 2018 to 2024.Viruses · 2025Article
- Antigenic drift expands influenza viral escape pathways from recalled humoral immunity.Immunity · 2025Article
- A Susceptible Cell-Selective Delivery (SCSD) of mRNA-Encoded Cas13d Against Influenza Infection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Influenza A Virus H7 nanobody recognizes a conserved immunodominant epitope on hemagglutinin head and confers heterosubtypic protection.Nature communications · 2025Article
- High-throughput sequencing-based neutralization assay reveals how repeated vaccinations impact titers to recent human H1N1 influenza strains.Journal of virology · 2024Article
- Delineating the functional activity of antibodies with cross-reactivity to SARS-CoV-2, SARS-CoV-1 and related sarbecoviruses.PLoS pathogens · 2024Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Influenza A virus hemagglutinin (HA) initiates viral entry by engaging host receptor sialylated glycans via its receptor-binding site (RBS). The amino acid sequence of the RBS naturally varies across avian and human influenza virus subtypes and is also evolvable. However, functional sequence diversity in the RBS has not been fully explored. Here, we performed a large-scale mutational analysis of the RBS of A/WSN/33 (H1N1) and A/Hong Kong/1/1968 (H3N2) HAs. Many replication-competent mutants not yet observed in nature were identified, including some that could escape from an RBS-targeted broadly neutralizing antibody. This functional sequence diversity is made possible by pervasive epistasis in the RBS 220-loop and can be buffered by avidity in viral receptor binding. Overall, our study reveals that the HA RBS can accommodate a much greater range of sequence diversity than previously thought, which has significant implications for the complex evolutionary interrelationships between receptor specificity and immune escape.
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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.