Evidence map›Paper›PMID 24766462›Full record

ArticleThe Biochemical journal2014

Early and late HIV-1 membrane fusion events are impaired by sphinganine lipidated peptides that target the fusion site.

Yoel A Klug, Avraham Ashkenazi, Mathias Viard, Ziv Porat, Robert Blumenthal, Yechiel Shai

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Modulating Antimicrobial Activity and Structure of the Peptide Esc(1-21) via Site-Specific Isopeptide Bond Formation.Journal of peptide science : an official publication of the European Peptide Society · 2025
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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

6 authors at 1 institution in 1 country.

Yoel A Klug*Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Avraham Ashkenazi*Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Mathias Viard
Ziv Porat§Flow Cytometry Unit, Department of Biological Services, Weizmann Institute of Science, Rehovot 7610001, Israel.
Robert Blumenthal†Section on Membrane Structure and Function, Basic Research Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, U.S.A.
Yechiel Shai*Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Weizmann Institute of Science · IL

Funding

Mechanisms of Viral Fusion and InactivationZIABC008303 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BLUMENTHAL, ROBERT · 2009 to 2014
$2.5M
PHS HHS HHSN261200800001E
6 · The paper itself

Abstract

Lipid-conjugated peptides have advanced the understanding of membrane protein functions and the roles of lipids in the membrane milieu. These lipopeptides modulate various biological systems such as viral fusion. A single function has been suggested for the lipid, binding to the membrane and thus elevating the local concentration of the peptide at the target site. In the present paper, we challenged this argument by exploring in-depth the antiviral mechanism of lipopeptides, which comprise sphinganine, the lipid backbone of DHSM (dihydrosphingomyelin), and an HIV-1 envelope-derived peptide. Surprisingly, we discovered a partnership between the lipid and the peptide that impaired early membrane fusion events by reducing CD4 receptor lateral diffusion and HIV-1 fusion peptide-mediated lipid mixing. Moreover, only the joint function of sphinganine and its conjugate peptide disrupted HIV-1 fusion protein assembly and folding at the later fusion steps. Via imaging techniques we revealed for the first time the direct localization of these lipopeptides to the virus-cell and cell-cell contact sites. Overall, the findings of the present study may suggest lipid-protein interactions in various biological systems and may help uncover a role for elevated DHSM in HIV-1 and its target cell membranes.

Indexed as

CD4 AntigensGene ExpressionGenes, ReporterHeLa CellsHIV-1HIV Envelope Protein gp120Host-Pathogen InteractionsHumansLuciferasesMembrane FusionPeptidesProtein FoldingSphingosinetat Gene Products, Human Immunodeficiency VirusTransgenesVirus InternalizationCD4 Antigensgp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120LuciferasesPeptidessafingolSphingosinetat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID24766462
PMCPMC4072049
OpenAlexW2029255031

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.