Evidence map›Paper›PMID 33871352›Full record

ArticleeLife2021

Structure of HIV-1 gp41 with its membrane anchors targeted by neutralizing antibodies.

Christophe Caillat, Delphine Guilligay, Johana Torralba, Nikolas Friedrich, Jose L Nieva, Alexandra Trkola, Christophe J Chipot, François L Dehez, Winfried Weissenhorn

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Structural basis of membrane engagement and polyreactivity control in HIV-1 MPER broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

9 authors at 3 institutions in 4 countries.

Christophe Caillat *Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), Grenoble, France.ORCID 0000-0003-2959-1871
Delphine Guilligay *Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), Grenoble, France.
Johana TorralbaInstituto Biofisika (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Bilbao, Spain.
Nikolas FriedrichInstitute of Medical Virology, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-0694-657X
Jose L NievaInstituto Biofisika (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Bilbao, Spain.
Alexandra TrkolaInstitute of Medical Virology, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-1013-876X
Christophe J ChipotLaboratoire de Physique et Chimie Théoriques (LPCT), University of Lorraine, Vandoeuvre-lès-Nancy, France.ORCID 0000-0002-9122-1698
François L DehezLaboratoire de Physique et Chimie Théoriques (LPCT), University of Lorraine, Vandoeuvre-lès-Nancy, France.
Winfried WeissenhornUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), Grenoble, France.ORCID 0000-0001-5532-4959
Centre National de la Recherche Scientifique · FRUniversity of the Basque Country · ESUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The HIV-1 gp120/gp41 trimer undergoes a series of conformational changes in order to catalyze gp41-induced fusion of viral and cellular membranes. Here, we present the crystal structure of gp41 locked in a fusion intermediate state by an MPER-specific neutralizing antibody. The structure illustrates the conformational plasticity of the six membrane anchors arranged asymmetrically with the fusion peptides and the transmembrane regions pointing into different directions. Hinge regions located adjacent to the fusion peptide and the transmembrane region facilitate the conformational flexibility that allows high-affinity binding of broadly neutralizing anti-MPER antibodies. Molecular dynamics simulation of the MPER Ab-stabilized gp41 conformation reveals a possible transition pathway into the final post-fusion conformation with the central fusion peptides forming a hydrophobic core with flanking transmembrane regions. This suggests that MPER-specific broadly neutralizing antibodies can block final steps of refolding of the fusion peptide and the transmembrane region, which is required for completing membrane fusion.

Indexed as

Antibody SpecificityBinding Sites, AntibodyBroadly Neutralizing AntibodiesHEK293 CellsHIV-1HIV AntibodiesHIV Envelope Protein gp41HumansLipid BilayersMembrane FusionMolecular Dynamics SimulationProtein BindingProtein ConformationProtein FoldingProtein StabilitySingle-Domain AntibodiesBroadly Neutralizing AntibodiesHIV AntibodiesHIV Envelope Protein gp41Lipid BilayersSingle-Domain Antibodies2H104E10gp41HIV-1infectious diseaseLN01membrane fusionmicrobiologymolecular biophysicsstructural biologyvirus

Identifiers

PMID33871352
PMCPMC8084527
OpenAlexW3154123704

What Socratic 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 Socratic graph.