Evidence map›Paper›PMID 29961575›Full record

ArticleCell2018

Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers.

Dibyendu Kumar Das, Ramesh Govindan, Ivana Nikić-Spiegel, Florian Krammer, Edward A Lemke, James B Munro

Abstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing 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

110 citing papers in PubMed.

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  19. Virion-associated influenza hemagglutinin clusters upon sialic acid binding visualized by cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Review

50 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Dibyendu Kumar DasDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine and Sackler School of Graduate Biomedical Sciences, Boston, MA 02111, USA. Electronic address: dibyendu_kumar.das@tufts.edu.
Ramesh GovindanDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine and Sackler School of Graduate Biomedical Sciences, Boston, MA 02111, USA.
Ivana Nikić-SpiegelWerner Reichardt Centre for Integrative Neuroscience, University of Tuebingen, 72076 Tuebingen, Germany.
Florian KrammerDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Edward A LemkeDepartments of Biology and Chemistry, Pharmacy, and Geosciences, Johannes Gutenberg-University Mainz, Johannes-von-Mullerweg 6, 55128 Mainz, Germany; Institute of Molecular Biology (IMB), Ackermannweg 4, 55128 Mainz, Germany; Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany.
James B MunroDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine and Sackler School of Graduate Biomedical Sciences, Boston, MA 02111, USA. Electronic address: james.munro@tufts.edu.

Funding

Structural dynamics of single Ebolavirus GP molecules.DP2AI124384 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MUNRO, JAMES B · 2015 to 2015
$2.5M
HIV-1 Env antagonism by ground state stabilizationK22AI116262 · NIAID · TUFTS UNIVERSITY BOSTON · PI MUNRO, JAMES B · 2015 to 2016
$266k
NIAID NIH HHS DP2 AI124384NIAID NIH HHS K22 AI116262
6 · The paper itself

Abstract

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of pH and receptor binding shifts the dynamic equilibrium of HA2 in favor of forward progression along the membrane-fusion reaction coordinate. Interaction with the target membrane promotes irreversible transition of HA2 to the post-fusion state. The reversibility of HA2 conformation may protect against transition to the post-fusion state prior to arrival at the target membrane.

Indexed as

A549 CellsCell MembraneFluorescence Resonance Energy TransferHEK293 CellsHemagglutinin Glycoproteins, Influenza VirusHemagglutininsHumansHydrogen-Ion ConcentrationInfluenza A virusInfluenza, HumanProtein BindingProtein ConformationSingle Molecule ImagingVirus InternalizationHemagglutinin Glycoproteins, Influenza VirusHemagglutininsmembrane fusionprotein dynamicssingle-molecule fluorescencesmFRETvirus entry

Identifiers

PMID29961575
PMCPMC6086748

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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.