ArticleScientific reports2017
Influenza A virus hemagglutinin and neuraminidase act as novel motile machinery.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 138 citations in OpenAlex.
- Neuraminidase of influenza A viruses induces global desialylation of host cells via its intracellular function.Microbiology spectrum · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
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- Implications of morphological variation in influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025Review
- Enhanced visualization of influenza A virus entry into living cells using virus-view atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Virion motility of sialoglycan-cleaving respiratory viruses.Npj viruses · 2025Review
- Single-molecule localisation microscopy approaches reveal envelope glycoprotein clusters in single-enveloped viruses: a potential functional role?Biochemical Society transactions · 2025Review
- Cell-based sialoglycan arrays for directly comparing influenza A virus receptor requirements for binding and infection.iScience · 2025Article
- Kinetic MUNANA assay reveals functionally relevant antibody epitopes on Influenza A virus neuraminidase.Npj viruses · 2025Article
- Poly-sialylated glycan of cervicovaginal fluid can be a potential marker of preterm birth.Scientific reports · 2025Article
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- DNA and protein-generated chimeric molecules for delivery of influenza viral epitopes in mouse and humanized NSG transfer models.Human vaccines & immunotherapeutics · 2024Review
- Recent advances in the influenza virus vaccine landscape: a comprehensive overview of technologies and trials.Clinical microbiology reviews · 2024Review
- Hemagglutinin glycosylation pattern-specific effects: implications for the fitness of H9.4.2.5-branched H9N2 avian influenza viruses.Emerging microbes & infections · 2024Article
- Hopping and crawling DNA-coated colloids.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Modulation of human-to-swine influenza a virus adaptation by the neuraminidase low-affinity calcium-binding pocket.Communications biology · 2024Article
- PK/PD investigation of antiviral host matriptase/TMPRSS2 inhibitors in cell models.Scientific reports · 2024Article
- Article
- Unraveling dynamics of paramyxovirus-receptor interactions using nanoparticles displaying hemagglutinin-neuraminidase.PLoS pathogens · 2024Article
- Sialic acids in infection and their potential use in detection and protection against pathogens.RSC chemical biology · 2024Review
21 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus (IAV) membrane proteins hemagglutinin (HA) and neuraminidase (NA) are determinants of virus infectivity, transmissibility, pathogenicity, host specificity, and major antigenicity. HA binds to a virus receptor, a sialoglycoprotein or sialoglycolipid, on the host cell and mediates virus attachment to the cell surface. The hydrolytic enzyme NA cleaves sialic acid from viral receptors and accelerates the release of progeny virus from host cells. In this study, we identified a novel function of HA and NA as machinery for viral motility. HAs exchanged binding partner receptors iteratively, generating virus movement on a receptor-coated glass surface instead of a cell surface. The virus movement was also dependent on NA. Virus movement mediated by HA and NA resulted in a three to four-fold increase in virus internalisation by cultured cells. We concluded that cooperation of HA and NA moves IAV particles on a cell surface and enhances virus infection of host cells.
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