Evidence map›Paper›PMID 9008705›Full record

ArticleThe Journal of cell biology1997

An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids.

L V Chernomordik, E Leikina, V Frolov, P Bronk, J Zimmerberg

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

101 citing papers in PubMed, 217 citations in OpenAlex.

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  11. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  18. Mechanics of nuclear membranes.Journal of cell science · 2019
    Review
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  20. Article

41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

L V ChernomordikLaboratary of Cellular and Molecular Biophysics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA. lchern@helix.nih.gov
E Leikina
V Frolov
P Bronk
J Zimmerberg
Frumkin Institute of Physical Chemistry and Electrochemistry · RUNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While the specificity and timing of membrane fusion in diverse physiological reactions, including virus-cell fusion, is determined by proteins, fusion always involves the merger of membrane lipid bilayers. We have isolated a lipid-dependent stage of cell-cell fusion mediated by influenza hemagglutinin and triggered by cell exposure to mildly acidic pH. This stage preceded actual membrane merger and fusion pore formation but was subsequent to a low pH-induced change in hemagglutinin conformation that is required for fusion. A low pH conformation of hemagglutinin was required to achieve this lipid-dependent stage and also, downstream of it, to drive fusion to completion. The lower the pH of the medium applied to trigger fusion and, thus, the more hemagglutinin molecules activated, the less profound was the dependence of fusion on lipids. Membrane-incorporated lipids affected fusion in a manner that correlated with their dynamic molecular shape, a characteristic that determines a lipid monolayer's propensity to bend in different directions. The lipid sensitivity of this stage, i.e., inhibition of fusion by inverted cone-shaped lysophosphatidylcholine and promotion by cone-shaped oleic acid, was consistent with the stalk hypothesis of fusion, suggesting that fusion proteins begin membrane merger by promoting the formation of a bent, lipid-involving, stalk intermediate.

Indexed as

Membrane Lipids3T3 CellsAnimalsEndopeptidase KErythrocyte MembraneHemagglutinin Glycoproteins, Influenza VirusHydrogen-Ion ConcentrationLysophosphatidylcholinesMembrane FusionMiceNeuraminidaseOleic AcidPatch-Clamp TechniquesProtein ConformationEndopeptidase KHemagglutinin Glycoproteins, Influenza VirusLysophosphatidylcholinesMembrane LipidsNeuraminidaseOleic Acid

Identifiers

PMID9008705
PMCPMC2132452
OpenAlexW2152568411

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.