Evidence map›Paper›PMID 17526585›Full record

ArticleBiophysical journal2007

HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates.

Stephanie Tristram-Nagle, John F Nagle

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 105 citations in OpenAlex.

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  11. Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021
    Review
  12. RapidBiochemistry · 2021
    Article
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  18. Biochimica et biophysica acta. Biomembranes · 2020
    Article
  19. Review
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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

2 authors at 1 institution in 1 country.

Stephanie Tristram-NagleBiological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA. stn@cmu.edu
John F Nagle
Carnegie Mellon University · US

Funding

STRUCTURE OF LIPID BILAYERSR01GM044976 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI NAGLE, JOHN F, TRISTRAM-NAGLE, STEPHANIE · 1990 to 2014
$3.1M
NIGMS NIH HHS DMR-0225180NIGMS NIH HHS GM 44976NIGMS NIH HHS R01 GM044976
6 · The paper itself

Abstract

A crucial step in human immunodeficiency virus (HIV) infection is fusion between the viral envelope and the T-cell membrane, which must involve intermediate membrane states with high curvature. Our main result from diffuse x-ray scattering is that the bending modulus K(C) is greatly reduced upon addition of the HIV fusion peptide FP-23 to lipid bilayers. A smaller bending modulus reduces the free energy barriers required to achieve and pass through the highly curved intermediate states and thereby facilitates fusion and HIV infection. The reduction in K(C) is by a factor of 13 for the thicker, stiffer 1,2-sn-dierucoylphosphatidylcholine bilayers and by a factor of 3 for 1,2-sn-dioleoylphosphatidylcholine bilayers. The reduction in K(C) decays exponentially with concentration of FP-23, and the 1/e concentration is <1 mol % peptide/lipid, which is well within the physiological range for a fusion site. A secondary result is, when FP-23 is added to the samples which consist of stacks of membranes, that the distance between membranes increases and eventually becomes infinite at full hydration (unbinding); we attribute this both to electrostatic repulsion of the positively charged arginine in the FP-23 and to an increase in the repulsive fluctuation interaction brought about by the smaller K(C). Although this latter interaction works against membrane fusion, our results show that the energy that it requires of the fusion protein machinery to bring the HIV envelope membrane and the target T-cell membrane into close contact is negligible.

Indexed as

Biophysical PhenomenaBiophysicsHIV-1HumansLipid BilayersMembrane FusionModels, BiologicalRetroviridae ProteinsThermodynamicsViral Fusion ProteinsLipid BilayersRetroviridae ProteinsViral Fusion Proteins

Identifiers

PMID17526585
PMCPMC1959562
OpenAlexW2140393378

What OpenQuestion holds

Textmetadata
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.