ArticleProceedings of the National Academy of Sciences of the United States of America2003
Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers.
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Who cites it
195 citing papers in PubMed, 354 citations in OpenAlex.
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- Effects of Ethanol and Opioid Receptor Antagonists Naltrexone and LY2444296 on the Organization of Cholesterol- and Sphingomyelin-Enriched Plasma Membrane Domains.ACS chemical neuroscience · 2025Article
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- Quantification of intracellular influenza A virus protein dynamics in different host cells after seed virus adaptation.Applied microbiology and biotechnology · 2025Article
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- Structure-guided assembly of an influenza spike nanobicelle vaccine provides pan H1 intranasal protection.bioRxiv : the preprint server for biology · 2024Article
- Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers.Nature communications · 2024Article
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- ProcClusterFrontiers in microbiology · 2024Article
- The Implication of Sphingolipids in Viral Infections.International journal of molecular sciences · 2023Review
- Host Membranes as Drivers of Virus Evolution.Viruses · 2023Article
- Thermoplasmonic Vesicle Fusion Reveals Membrane Phase Segregation of Influenza Spike Proteins.Nano letters · 2023Article
- Influenza A Virus M1 Protein Non-Specifically Deforms Charged Lipid Membranes and Specifically Interacts with the Raft Boundary.Membranes · 2023Article
- Breathing and Tilting: Mesoscale Simulations Illuminate Influenza Glycoprotein Vulnerabilities.ACS central science · 2022Article
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- A Glu-Glu-Tyr Sequence in the Cytoplasmic Tail of the M2 Protein Renders Influenza A Virus Susceptible to Restriction of the Hemagglutinin-M2 Association in Primary Human Macrophages.Journal of virology · 2022Article
- In Silico Studies Reveal Peramivir and Zanamivir as an Optimal Drug Treatment Even If H7N9 Avian Type Influenza Virus Acquires Further Resistance.Molecules (Basel, Switzerland) · 2022Article
135 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Lipid raft microdomains are enriched in sphingomyelin and cholesterol and function as platforms for signal transduction and as the site of budding of several enveloped viruses, including influenza virus. The influenza virus hemagglutinin (HA) glycoprotein, which mediates both viral-cell attachment and membrane fusion, associates intrinsically with lipid rafts. Residues in the HA transmembrane (TM) domain are important for raft association as sequence substitutions in the HA TM domain ablate HA association with rafts (nonraft HA). Cells expressing either WT or nonraft HA cause complete fusion (lipid mixing and content mixing) over widely varying HA expression levels. However, the number of fusion events measured for nonraft HA mutant protein at all HA surface densities was reduced to approximately 55% of the events for WT HA protein. Mutant influenza viruses were generated that contain the nonraft HA TM domain alterations. Electron microscopy experiments showed that WT HA was distributed at the cell surface in clusters of 200-280 nm in diameter, whereas nonraft HA was distributed mostly randomly at the plasma membrane. Nonraft HA virus showed reduced budding, contained reduced amounts of HA protein, was greatly reduced in infectivity, and exhibited decreased virus-membrane fusion activity. Cholesterol depletion of virus did not affect the ability of virions to cause either virus-cell lipid mixing or virus-mediated hemolysis, a surrogate for content mixing. Taken together, the data suggest that HA clusters in rafts to provide a sufficient concentration of HA in budding virus to mediate efficient virus-cell fusion.
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