Evidence map›Paper›PMID 41421345›Full record

ArticleStructure (London, England : 1993)2026

Probing the role of membrane in neutralizing activity of antibodies against influenza virus.

Defne G Ozgulbas, Timothy J C Tan, Po-Chao Wen, Qi Wen Teo, Huibin Lv, Zhaleh Ghaemi, Martin Frank, Nicholas C Wu, Emad Tajkhorshid

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Defne G OzgulbasTheoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Visualization, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL, USA; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA; Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Timothy J C TanCenter for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Po-Chao WenTheoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Visualization, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL, USA; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Qi Wen TeoDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA; Carl R. Woese Institute for Genomic Biology, Carle Illinois College of Medicine, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Huibin LvDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA; Carl R. Woese Institute for Genomic Biology, Carle Illinois College of Medicine, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Zhaleh GhaemiDepartment of Chemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Martin FrankBiognos AB, Göteborg, Sweden.
Nicholas C WuDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA; Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, IL, USA; Carl R. Woese Institute for Genomic Biology, Carle Illinois College of Medicine, University of Illinois Urbana-Champaign, Urbana, IL, USA. Electronic address: nicwu@illinois.edu.
Emad TajkhorshidTheoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Visualization, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL, USA; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA; Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, IL, USA; Department of Chemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA. Electronic address: emad@illinos.edu.

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SCHULTEN, KLAUS · 2012 to 2021
$19.0M
Resource for Macromolecular Modeling and VisualizationR24GM145965 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Emad Tajkhorshid · 2022 to 2026
$6.2M
Toolkit for High-Resolution Structure and Dynamics of Functional LipidsR01GM123455 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MORRISSEY, JAMES H., RIENSTRA, CHAD M · 2016 to 2020
$5.0M
Sequence-function relationship of influenza broadly neutralizing antibodiesR01AI167910 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Nicholas C. Wu · 2022 to 2026
$2.5M
High-throughput identification of antibody features for sequence-based epitope predictionDP2AT011966 · NCCIH · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI WU, NICHOLAS C. · 2021 to 2024
$2.4M
NCCIH NIH HHS DP2 AT011966NIAID NIH HHS R01 AI167910NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM123455NIGMS NIH HHS R24 GM145965
6 · The paper itself

Abstract

Influenza poses a major health issue globally. Neutralizing antibodies targeting the highly conserved stem region of hemagglutinin (HA) of the influenza virus provide considerable protection against the infection. Using an array of advanced simulation technologies, we developed a high-resolution structural model of full-length, Fab-bound HA in a native viral membrane to characterize direct membrane interactions that govern the efficacy of the antibody. We reveal functionally important residues beyond the antibody's complementary-determining regions that contribute to its membrane binding. Mutagenesis experiments and infectivity assays confirm that deactivating the membrane-binding residues of the antibody decreases its neutralization activity. Therefore, we propose that the association with the viral membrane plays a key role in the neutralization activity of these antibodies. Given the rapid evolution of the influenza virus, the developed model provides a structural framework for the rational design and development of more effective therapeutic antibodies.

Indexed as

Antibodies, NeutralizingAntibodies, ViralHemagglutinin Glycoproteins, Influenza VirusAnimalsHumansImmunoglobulin Fab FragmentsModels, MolecularMolecular Dynamics SimulationProtein BindingAntibodies, NeutralizingAntibodies, ViralHemagglutinin Glycoproteins, Influenza VirusImmunoglobulin Fab Fragmentshemagglutinininfluenza virusmembranemolecular dynamicsneutralizing antibody

Identifiers

PMID41421345
PMCPMC12780972

What OpenQuestion holds

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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.