ArticleProceedings of the National Academy of Sciences of the United States of America2012
Influenza virus binds its host cell using multiple dynamic interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Dynamics of viral self-assembly, viral genome packaging, and virus-cell interactions studied by optical tweezers.European biophysics journal : EBJ · 2026Review
- 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
- Article
- Mechanisms of Plasma Ozone and UV-C Sterilization of SARS-CoV-2 Explored through Atomic Force Microscopy.ACS applied materials & interfaces · 2024Article
- Quantification of the interaction forces between dengue virus and dopamine type-2 receptor using optical tweezers.Virology journal · 2024Article
- Article
- Unravelling the interaction between Influenza virus and the nuclear pore complex: insights into viral replication and host immune response.Virusdisease · 2024Review
- Atomic Force Microscopy of Viruses.Sub-cellular biochemistry · 2024Review
- Optical Tweezers to Study Viruses.Sub-cellular biochemistry · 2024Review
- Mathematical model for force and energy of virion-cell interactions during full engulfment in HIV: Impact of virion maturation and host cell morphology.Biomechanics and modeling in mechanobiology · 2023Article
- Relevance of Host Cell Surface Glycan Structure for Cell Specificity of Influenza A Viruses.Viruses · 2023Article
- Kinetic analysis of paramyxovirus-sialoglycan receptor interactions reveals virion motility.PLoS pathogens · 2023Article
- Breathing and Tilting: Mesoscale Simulations Illuminate Influenza Glycoprotein Vulnerabilities.ACS central science · 2022Article
- Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level.Nature communications · 2022Article
- Probing the Separation Distance between Biological Nanoparticles and Cell Membrane Mimics Using Neutron Reflectometry with Sub-Nanometer Accuracy.Journal of the American Chemical Society · 2022Article
- Breathing and tilting: mesoscale simulations illuminate influenza glycoprotein vulnerabilities.bioRxiv : the preprint server for biology · 2022Article
- Interferon-gamma inhibits influenza A virus cellular attachment by reducing sialic acid cluster size.iScience · 2022Article
- A Deadly Embrace: Hemagglutination Mediated by SARS-CoV-2 Spike Protein at Its 22 N-Glycosylation Sites, Red Blood Cell Surface Sialoglycoproteins, and Antibody.International journal of molecular sciences · 2022Review
- Quantifying molecular- to cellular-level forces in living cells.Journal of physics D: Applied physics · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Influenza virus belongs to a wide range of enveloped viruses. The major spike protein hemagglutinin binds sialic acid residues of glycoproteins and glycolipids with dissociation constants in the millimolar range [Sauter NK, et al. (1992) Biochemistry 31:9609-9621], indicating a multivalent binding mode. Here, we characterized the attachment of influenza virus to host cell receptors using three independent approaches. Optical tweezers and atomic force microscopy-based single-molecule force spectroscopy revealed very low interaction forces. Further, the observation of sequential unbinding events strongly suggests a multivalent binding mode between virus and cell membrane. Molecular dynamics simulations reveal a variety of unbinding pathways that indicate a highly dynamic interaction between HA and its receptor, allowing rationalization of influenza virus-cell binding quantitatively at the molecular level.
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