ArticleThe FEBS journal2021
Second sialic acid-binding site of influenza A virus neuraminidase: binding receptors for efficient release.
Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 52 citations in OpenAlex.
- Substitutions affecting the HA-NA-receptor balance preceded the emergence of the pandemic 2009 H1N1 virus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Isolation and characterization of a clade 2.3.4.4b genotype D1.1 H5N1 virus from dairy cattle in Wisconsin.Journal of virology · 2026Article
- Rapid Detection of N9 Subtype Avian Influenza Viruses Using an NA-Targeting Lateral Flow Immunoassay.Viruses · 2026Article
- Evolutionary Rate Variation at Predicted PTM Sites Reveals Localized Host-Associated Patterns in Influenza A Virus.Genome biology and evolution · 2026Article
- The emergence and molecular evolution of H5N1 influenza viruses in United States dairy cattle.bioRxiv : the preprint server for biology · 2026Article
- Protocol to measure the kinetics of MHC class II-influenza A binding using biolayer interferometry.STAR protocols · 2025Article
- Genetic Optimization of Early 2009 Pandemic H1N1 Vaccine Strains for Improved Replication in Embryonated Chicken Eggs.Journal of microbiology and biotechnology · 2025Article
- Rapid surge of reassortant A(H1N1) influenza viruses in Danish swine and their zoonotic potential.Emerging microbes & infections · 2025Article
- Avian influenza overview June-September 2025.EFSA journal. European Food Safety Authority · 2025Article
- Phylogenetic analysis of H5N1 influenza viruses isolated from dairy cattle in Texas in December 2024.Journal of virology · 2025Article
- Avian influenza overview March-June 2025.EFSA journal. European Food Safety Authority · 2025Article
- H5N1 2.3.4.4b: a review of mammalian adaptations and risk of pandemic emergence.The Journal of general virology · 2025Review
- Avian influenza overview December 2024-March 2025.EFSA journal. European Food Safety Authority · 2025Article
- The global H5N1 influenza panzootic in mammals.Nature · 2025Review
- Emerging threats of HPAI H5N1 clade 2.3.4.4b in swine: knowledge gaps and the imperative for a One Health approach.Frontiers in veterinary science · 2025Review
- Review
- Triton X-100-treated virus-based ELLA demonstrates discordant antigenic evolution of influenza B virus hemagglutinin and neuraminidase.Journal of virology · 2024Article
- Unraveling dynamics of paramyxovirus-receptor interactions using nanoparticles displaying hemagglutinin-neuraminidase.PLoS pathogens · 2024Article
- Highly pathogenic avian influenza A(H5N1) virus infections on fur farms connected to mass mortalities of black-headed gulls, Finland, July to October 2023.Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin · 2024Article
- Molecular Markers and Mechanisms of Influenza A Virus Cross-Species Transmission and New Host Adaptation.Viruses · 2024Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A viruses (IAVs) are a major cause of human respiratory tract infections and cause significant disease and mortality. Human IAVs originate from animal viruses that breached the host species barrier. IAV particles contain sialoglycan receptor-binding hemagglutinin (HA) and receptor-destroying neuraminidase (NA) in their envelope. When IAV crosses the species barrier, the functional balance between HA and NA needs to be adjusted to the sialoglycan repertoire of the novel host species. Relatively little is known about the role of NA in host adaptation in contrast to the extensively studied HA. NA prevents virion aggregation and facilitates release of (newly assembled) virions from cell surfaces and from decoy receptors abundantly present in mucus and cell glycocalyx. In addition to a highly conserved catalytic site, NA carries a second sialic acid-binding site (2SBS). The 2SBS preferentially binds α2,3-linked sialic acids and enhances activity of the neighboring catalytic site by bringing/keeping multivalent substrates in close contact with this site. In this way, the 2SBS contributes to the HA-NA balance of virus particles and affects virus replication. The 2SBS is highly conserved in all NA subtypes of avian IAVs, with some notable exceptions associated with changes in the receptor-binding specificity of HA and host tropism. Conservation of the 2SBS is invariably lost in human (pandemic) viruses and in several other viruses adapted to mammalian host species. Preservation or loss of the 2SBS is likely to be an important factor of the viral host range.
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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.