ArticleMolecular biology of the cell1999
A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 174 citations in OpenAlex.
- The Conserved Fusion Peptide Sequence of SARS-CoVs is Insensitive to CaThe Journal of membrane biology · 2026Article
- The Interplay of Lipids and Peptides in Membrane Merger.Advances in experimental medicine and biology · 2026Review
- Unravelling the role of key amino acid residues of the parainfluenza fusion peptide in membrane fusion.RSC chemical biology · 2025Article
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
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- SARS-CoV-2-host cell surface interactions and potential antiviral therapies.Interface focus · 2022Review
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- RapidBiochemistry · 2021Article
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- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A conserved histidine in Group-1 influenza subtype hemagglutinin proteins is essential for membrane fusion activity.Virology · 2019Article
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- Interferon-induced transmembrane protein 3 blocks fusion of sensitive but not resistant viruses by partitioning into virus-carrying endosomes.PLoS pathogens · 2019Article
- The fusion pore, 60 years after the first cartoon.FEBS letters · 2018Review
- Functional Study of the C-Terminal Part of the Hepatitis C Virus E1 Ectodomain.Journal of virology · 2018Article
39 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We showed previously that substitution of the first residue of the influenza hemagglutinin (HA) fusion peptide Gly1 with Glu abolishes fusion activity. In the present study we asked whether this striking phenotype was due to the charge or side-chain volume of the substituted Glu. To do this we generated and characterized six mutants with substitutions at position 1: Gly1 to Ala, Ser, Val, Glu, Gln, or Lys. We found the following. All mutants were expressed at the cell surface, could be cleaved from the precursor (HA0) to the fusion permissive form (HA1-S-S-HA2), bound antibodies against the major antigenic site, bound red blood cells, and changed conformation at low pH. Only Gly, Ala, and Ser supported lipid mixing during fusion with red blood cells. Only Gly and Ala supported content mixing. Ser HA, therefore, displayed a hemifusion phenotype. The hemifusion phenotype of Ser HA was confirmed by electrophysiological studies. Our findings indicate that the first residue of the HA fusion peptide must be small (e.g., Gly, Ala, or Ser) to promote lipid mixing and must be small and apolar (e.g., Gly or Ala) to support both lipid and content mixing. The finding that Val HA displays no fusion activity underscores the idea that hydrophobicity is not the sole factor dictating fusion peptide function. The surprising finding that Ser HA displays hemifusion suggests that the HA ectodomain functions not only in the first stage of fusion, lipid mixing, but also, either directly or indirectly, in the second stage of fusion, content mixing.
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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.