ArticleJournal of virology2018
Enhanced Human-Type Receptor Binding by Ferret-Transmissible H5N1 with a K193T Mutation.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.
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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
30 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- Transmission Pathways of Zoonotic Influenza Viruses and Influencing Factors: A Systematic Review of Recent Findings.Viruses · 2025Pooled it
- Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.Journal of virology · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Divergent Avian Influenza H10 Viruses from Sympatric Waterbird Species in Italy: Zoonotic Potential Assessment by Molecular Markers.Microorganisms · 2025Article
- Epistasis in the receptor-binding domain of contemporary H3N2 viruses that reverted to bind sialylated di-LacNAc repeats.Cell reports · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.bioRxiv : the preprint server for biology · 2025Article
- Pathogenic and Antigenic Analyses of H5N1 High Pathogenicity Avian Influenza Virus Isolated in the 2022/2023 Season From Poultry Farms in Izumi City, Japan.Transboundary and emerging diseases · 2025Article
- A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors.Science (New York, N.Y.) · 2024Article
- HA N193D substitution in the HPAI H5N1 virus alters receptor binding affinity and enhances virulence in mammalian hosts.Emerging microbes & infections · 2024Article
- Article
- Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites.Npj viruses · 2024Article
- Molecular Markers and Mechanisms of Influenza A Virus Cross-Species Transmission and New Host Adaptation.Viruses · 2024Review
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding.Protein science : a publication of the Protein Society · 2024Article
- Article
- Vaccination and Antiviral Treatment against Avian Influenza H5Nx Viruses: A Harbinger of Virus Control or Evolution.Vaccines · 2023Review
- Highly Pathogenic H5 Influenza Viruses Isolated between 2016 and 2017 in Vietnamese Live Bird Markets.Viruses · 2023Article
- Article
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
All human influenza pandemics have originated from avian influenza viruses. Although multiple changes are needed for an avian virus to be able to transmit between humans, binding to human-type receptors is essential. Several research groups have reported mutations in H5N1 viruses that exhibit specificity for human-type receptors and promote respiratory droplet transmission between ferrets. Upon detailed analysis, we have found that these mutants exhibit significant differences in fine receptor specificity compared to human H1N1 and H3N2 and retain avian-type receptor binding. We have recently shown that human influenza viruses preferentially bind to α2-6-sialylated branched N-linked glycans, where the sialic acids on each branch can bind to receptor sites on two protomers of the same hemagglutinin (HA) trimer. In this binding mode, the glycan projects over the 190 helix at the top of the receptor-binding pocket, which in H5N1 would create a stearic clash with lysine at position 193. Thus, we hypothesized that a K193T mutation would improve binding to branched N-linked receptors. Indeed, the addition of the K193T mutation to the H5 HA of a respiratory-droplet-transmissible virus dramatically improves both binding to human trachea epithelial cells and specificity for extended α2-6-sialylated N-linked glycans recognized by human influenza viruses.
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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.