ArticleMolecular biology of the cell2000
The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
52 citing papers in PubMed, 94 citations in OpenAlex.
- Targeting Human Proteins for Antiviral Drug Discovery and Repurposing Efforts: A Focus on Protein Kinases.Viruses · 2023Review
- Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins.Nature communications · 2022Article
- Physico-Chemical Mechanisms of the Functioning of Membrane-Active Proteins of Enveloped Viruses.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022Article
- Myomerger promotes fusion pore by elastic coupling between proximal membrane leaflets and hemifusion diaphragm.Nature communications · 2021Article
- Ectodomain Pulling Combines with Fusion Peptide Inserting to Provide Cooperative Fusion for Influenza Virus and HIV.International journal of molecular sciences · 2020Article
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020Review
- Article
- Article
- Transmembrane Domains of Highly Pathogenic Viral Fusion Proteins Exhibit Trimeric AssociationmSphere · 2018Article
- Nanodisc-cell fusion: control of fusion pore nucleation and lifetimes by SNARE protein transmembrane domains.Scientific reports · 2016Article
- Herpesvirus gB: A Finely Tuned Fusion Machine.Viruses · 2015Review
- IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion.PLoS pathogens · 2014Article
- Anionic lipids are required for vesicular stomatitis virus G protein-mediated single particle fusion with supported lipid bilayers.The Journal of biological chemistry · 2013Article
- Review
- Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.Journal of virology · 2012Article
- Cell entry of enveloped viruses.Current opinion in virology · 2011Review
- The final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusion.The Journal of biological chemistry · 2011Article
- Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Imaging single retrovirus entry through alternative receptor isoforms and intermediates of virus-endosome fusion.PLoS pathogens · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
GPI-linked hemagglutinin (GPI-HA) of influenza virus was thought to induce hemifusion without pore formation. Cells expressing either HA or GPI-HA were bound to red blood cells, and their fusion was compared by patch-clamp capacitance measurements and fluorescence microscopy. It is now shown that under more optimal fusion conditions than have been used previously, GPI-HA is also able to induce fusion pore formation before lipid dye spread, although with fewer pores formed than those induced by HA. The GPI-HA pores did not enlarge substantially, as determined by the inability of a small aqueous dye to pass through them. The presence of 1,1'-dioctadecyl-3, 3,3',3'-tetramethylindocarbocyanine perchlorate or octadecylrhodamine B in red blood cells significantly increased the probability of pore formation by GPI-HA; the dyes affected pore formation to a much lesser degree for HA. This greater sensitivity of pore formation to lipid composition suggests that lipids are a more abundant component of a GPI-HA fusion pore than of an HA pore. The finding that GPI-HA can induce pores indicates that the ectodomain of HA is responsible for all steps up to the initial membrane merger and that the transmembrane domain, although not absolutely required, ensures reliable pore formation and is essential for pore growth. GPI-HA is the minimal unit identified to date that supports fusion to the point of pore formation.
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Registered trials
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.