Evidence map›Paper›PMID 30150411›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.

Jesper J Madsen, John M A Grime, Jeremy S Rossman, Gregory A Voth

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025
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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

4 authors at 2 institutions in 2 countries.

Jesper J MadsenDepartment of Chemistry, The University of Chicago, Chicago, IL 60637.
John M A GrimeDepartment of Chemistry, The University of Chicago, Chicago, IL 60637.
Jeremy S RossmanSchool of Biosciences, University of Kent, Canterbury, CT2 7NJ Kent, United Kingdom.
Gregory A VothDepartment of Chemistry, The University of Chicago, Chicago, IL 60637; gavoth@uchicago.edu.
University of Chicago · USUniversity of Kent · GB

Funding

New Method for Biomembrane SimulationsR01GM063796 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 2001 to 2025
$6.3M
Medical Research Council MR/L00870X/1Medical Research Council MR/L018578/1NIGMS NIH HHS R01 GM063796
6 · The paper itself

Abstract

The influenza A matrix 2 (M2) transmembrane protein facilitates virion release from the infected host cell. In particular, M2 plays a role in the induction of membrane curvature and/or in the scission process whereby the envelope is cut upon virion release. Here we show using coarse-grained computer simulations that various M2 assembly geometries emerge due to an entropic driving force, resulting in compact clusters or linearly extended aggregates as a direct consequence of the lateral membrane stresses. Conditions under which these protein assemblies will cause the lipid membrane to curve are explored, and we predict that a critical cluster size is required for this to happen. We go on to demonstrate that under the stress conditions taking place in the cellular membrane as it undergoes large-scale membrane remodeling, the M2 protein will, in principle, be able to both contribute to curvature induction and sense curvature to line up in manifolds where local membrane line tension is high. M2 is found to exhibit linactant behavior in liquid-disordered-liquid-ordered phase-separated lipid mixtures and to be excluded from the liquid-ordered phase, in near-quantitative agreement with experimental observations. Our findings support a role for M2 in membrane remodeling during influenza viral budding both as an inducer and a sensor of membrane curvature, and they suggest a mechanism by which localization of M2 can occur as the virion assembles and releases from the host cell, independent of how the membrane curvature is produced.

Indexed as

Virus AssemblyVirus ReleaseAlgorithmsAnimalsCell MembraneDogsEntropyHost-Pathogen InteractionsMadin Darby Canine Kidney CellsMembrane LipidsMicroscopy, ElectronModels, BiologicalMolecular Dynamics SimulationViral Matrix ProteinsViroporin ProteinsM2 protein, Influenza A virusMembrane LipidsViral Matrix ProteinsViroporin Proteinsbuddinglipid-phase behaviormembrane curvatureprotein clusteringwedging mechanism

Identifiers

PMID30150411
PMCPMC6140502
OpenAlexW2795101715

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.