ArticleBiophysical journal1997
Interaction of the influenza hemagglutinin fusion peptide with lipid bilayers: area expansion and permeation.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 82 citations in OpenAlex.
- Switchable positioning of plate-like inclusions in lipid membranes: Elastically mediated interactions of planar colloids in 2D fluids.Science advances · 2021Article
- Lipid-dependence of target membrane stability during influenza viral fusion.Journal of cell science · 2018Article
- Insertion of Dengue E into lipid bilayers studied by neutron reflectivity and molecular dynamics simulations.Biochimica et biophysica acta. Biomembranes · 2018Article
- Mode of Action of Antimicrobial Peptides on E. coli Spheroplasts.Biophysical journal · 2016Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Large effect of membrane tension on the fluid-solid phase transitions of two-component phosphatidylcholine vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Line-tension controlled mechanism for influenza fusion.PloS one · 2012Article
- A Generalized System for Photo-Responsive Membrane Rupture in Polymersomes.Advanced functional materials · 2010Article
- Architecture of a nascent viral fusion pore.The EMBO journal · 2010Article
- Fusion peptide from influenza hemagglutinin increases membrane surface order: an electron-spin resonance study.Biophysical journal · 2009Article
- Films of agarose enable rapid formation of giant liposomes in solutions of physiologic ionic strength.Journal of the American Chemical Society · 2009Article
- Infectious Disease: Connecting Innate Immunity to Biocidal Polymers.Materials science & engineering. R, Reports : a review journal · 2007Article
- Triggering and visualizing the aggregation and fusion of lipid membranes in microfluidic chambers.Biophysical journal · 2006Article
- Elasticity and phase behavior of DPPC membrane modulated by cholesterol, ergosterol, and ethanol.Biophysical journal · 2005Article
- Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein.Biophysical journal · 2005Article
- Interactions of membrane-active peptides with thick, neutral, nonzwitterionic bilayers.The journal of physical chemistry. B · 2005Article
- The influence of short-chain alcohols on interfacial tension, mechanical properties, area/molecule, and permeability of fluid lipid bilayers.Biophysical journal · 2004Article
- Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization.Biophysical journal · 2004Article
- Material studies of lipid vesicles in the L(alpha) and L(alpha)-gel coexistence regimes.Biophysical journal · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Fusion is a crucial event in the infection of animal cells by enveloped viruses (e.g., HIV or influenza). Viral fusion is mediated by glycoproteins, spanning the viral envelope, which attach to a membrane surface and induce fusion of the viral envelope to the cellular membrane. Influenza fusion protein (hemagglutinin) contains an amino-terminal segment critical to fusion, referred to as the fusion peptide. We show here that the native fusion peptide (wt-20) of hemagglutinin destabilizes membranes formed of 99% 1 -stearoyl-2-oleoylphosphatidylcholine (SOPC). The first step in destabilization is rapid insertion of the peptide into the membrane, in which membrane area increases by as much as 11% in just seconds. We visualized and quantified the area expansion by using optical video microscopy combined with micropipette aspiration. This rapid membrane area expansion is followed by the formation of membrane defects in the size range of 0.5 nm, and results in membrane rupture. Both the rate of area increase and maximum area increase are significantly higher at a pH near 5.0 compared to pH 7.0. These results suggest that enhanced membrane insertion of wt-20 and accompanying area expansion at pH 5.0 are responsible for the relatively greater lytic activity at this pH. We show that a deletion of the N-terminal glycine of wt-20 results in a lack of area expansion or membrane perturbation at pH 5.0.
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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.