ArticleProceedings of the National Academy of Sciences of the United States of America2020
Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 65 citations in OpenAlex.
- Unmasking complex kinetics in viral entry by inferring hypoexponential models.Biophysical journal · 2025Article
- Replication in human cells supersedes serum antigenic match for the in vivo efficacy of an A/H1N1pdm09 LAIV virus.NPJ vaccines · 2025Article
- Single-Virus Lipid-Mixing Study of Sendai Virus Provides Insight into Fusion Mechanism.ACS omega · 2025Article
- Single VLP lipid-mixing measurements confirm off-pathway state in dengue virus fusion mechanism.Biophysical journal · 2025Article
- Unravelling the role of key amino acid residues of the parainfluenza fusion peptide in membrane fusion.RSC chemical biology · 2025Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- Article
- Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.Trends in biochemical sciences · 2024Review
- Modulation of human-to-swine influenza a virus adaptation by the neuraminidase low-affinity calcium-binding pocket.Communications biology · 2024Article
- Making the cut: Multiscale simulation of membrane remodeling.Current opinion in structural biology · 2024Review
- Review
- The local variation of the Gaussian modulus enables different pathways for fluid lipid vesicle fusion.Scientific reports · 2024Article
- Membrane Proteins and Membrane Curvature: Mutual Interactions and a Perspective on Disease Treatments.Biomolecules · 2023Review
- SARS-CoV-2 fusion peptide sculpting of a membrane with insertion of charged and polar groups.Structure (London, England : 1993) · 2023Article
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- Single-Virus Fusion Measurements Reveal Multiple Mechanistically Equivalent Pathways for SARS-CoV-2 Entry.Journal of virology · 2023Article
- High curvature promotes fusion of lipid membranes: Predictions from continuum elastic theory.Biophysical journal · 2023Article
- Two modes of fusogenic action for influenza virus fusion peptide.PLoS computational biology · 2023Article
- Ceramide-1-phosphate transfer protein enhances lipid transport by disrupting hydrophobic lipid-membrane contacts.PLoS computational biology · 2023Article
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Enveloped viruses enter cells via a process of membrane fusion between the viral envelope and a cellular membrane. For influenza virus, mutational data have shown that the membrane-inserted portions of the hemagglutinin protein play a critical role in achieving fusion. In contrast to the relatively well-understood ectodomain, a predictive mechanistic understanding of the intramembrane mechanisms by which influenza hemagglutinin drives fusion has been elusive. We used molecular dynamics simulations of fusion between a full-length hemagglutinin proteoliposome and a lipid bilayer to analyze these mechanisms. In our simulations, hemagglutinin first acts within the membrane to increase lipid tail protrusion and promote stalk formation and then acts to engage the distal leaflets of each membrane and promote stalk widening, curvature, and eventual fusion. These two sequential mechanisms, one occurring before stalk formation and one after, are consistent with our experimental measurements of single-virus fusion kinetics to liposomes of different sizes. The resulting model also helps explain and integrate previous mutational and biophysical data, particularly the mutational sensitivity of the fusion peptide N terminus and the length sensitivity of the transmembrane domain. We hypothesize that entry by other enveloped viruses may also use sequential processes of acyl tail exposure, followed by membrane curvature and distal leaflet engagement.
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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.