Evidence map›Paper›PMID 42826053›Full record

ArticleeLife2026

Distinct allosteric remodeling of HIV-1 Env dynamics on virions by gp41-directed antibodies reveals two modes of neutralization.

Wang Xu, Narendra Kumar Gonepudi, Junyu Liu, Yufan He, Revansiddha Katte, Ran Wang, Harry Baffour Awuah, Yang Han, Baoshan Zhang, Jian Yu and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors.

Wang XuDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.ORCID https://orcid.org/0000-0003-4452-9240
Narendra Kumar GonepudiDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.
Junyu LiuDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.
Yufan HeDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.
Revansiddha KatteDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.
Ran WangDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, United States.
Harry Baffour AwuahDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.
Yang HanDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.
Baoshan ZhangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Jian YuAaron Diamond AIDS Research Center, Department of Medicine, Vagelos College of Physicians and Surgeons, Columbia University, New York, United States.
Bo HuDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, United States.
David D HoAaron Diamond AIDS Research Center, Department of Medicine, Vagelos College of Physicians and Surgeons, Columbia University, New York, United States.
Priyamvada AcharyaDuke Human Vaccine Institute, Duke University, Durham, United States.ORCID https://orcid.org/0000-0002-0089-277X
Peter D KwongVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.ORCID https://orcid.org/0000-0003-3560-232X
Maolin LuDepartment of Cellular and Molecular Biology, School of Medicine, The University of Texas at Tyler Health Science Center, Tyler, United States.ORCID https://orcid.org/0000-0002-8099-6447

Funding

Probing real-time conformational dynamics and allosteric cooperativity of the HIV-1 envelope glycoprotein during virus entryR01AI181600 · NIAID · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI Maolin Lu · 2024 to 2026
$1.3M
National Institute of Allergy and Infectious Diseases R01AI181600NIAID NIH HHS R01 AI181600
6 · The paper itself

Abstract

HIV-1 envelope glycoprotein (Env), a gp120-gp41 trimer, undergoes coordinated conformational changes that drive membrane fusion and allow immune evasion by transiently concealing neutralization-sensitive epitopes. Most broadly neutralizing antibodies (bNAbs) target gp120, whereas a distinct subset recognizes conserved gp41 regions, such as the fusion peptide and the membrane-proximal external region; however, their impact on Env dynamics and associated neutralization mechanisms remains unclear. By using bioorthogonal tagging for single-molecule FRET, we monitored real-time bNAb-induced conformational sampling of Env on intact virions. Most gp41-directed bNAbs allosterically stabilized the prefusion-closed (PC) state, whereas the bivalent 10E8.4/iMab favored both PC and CD4-bound open (predominant) states. Antibodies redistributed the conformational populations of Env with modest kinetic effects, preserving a sequential transition pathway. These findings reveal two modes of neutralization for gp41-directed antibodies, fixing the PC conformation and opening it up - in both cases, with neutralization occurring via long-range allosteric control of Env dynamics.

Indexed as

Antibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV-1HIV AntibodiesHIV Envelope Protein gp41VirionAllosteric RegulationFluorescence Resonance Energy TransferHumansProtein ConformationSingle Molecule ImagingAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency Virusgp41 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp41allosteric modelingantibody neutralizationHIV-1 envelopeiMabinfectious diseasemicrobiologymolecular biophysicsMPERsingle-molecule FRETstructural biologyviruses

Identifiers

PMID42826053
PMCPMC13633075

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.