Evidence map›Paper›PMID 41659401›Full record

ArticlebioRxiv : the preprint server for biology2026

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 readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 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, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Narendra Kumar GonepudiDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Junyu LiuDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Yufan HeDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Revansiddha KatteDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Ran WangDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX, USA.
Harry Baffour AwuahDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Yang HanDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.
Baoshan ZhangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Jian YuAaron Diamond AIDS Research Center, Department of Medicine, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY, USA.
Bo HuDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX, USA.
David D HoAaron Diamond AIDS Research Center, Department of Medicine, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY, USA.
Priyamvada AcharyaDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Peter D KwongVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Maolin LuDepartment of Cellular and Molecular Biology, School of Medicine, University of Texas at Tyler Health Science Center, Tyler, TX, USA.ORCID 0000-0002-8099-6447

Funding

The role of conformational dynamics of enveloped virus spike proteins in cell entryR35GM151169 · NIGMS · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI Maolin Lu · 2023 to 2026
$1.5M
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
NIAID NIH HHS R01 AI181600NIGMS NIH HHS R35 GM151169
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. 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 the sequential transition pathway. These findings reveal two modes of neutralization for gp41-directed antibodies, fixing the prefusion-closed conformation and opening it up - in both cases, with neutralization occurring via long-range allosteric control of Env dynamics.

Identifiers

PMID41659401
PMCPMC12874067

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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.