Evidence map›Paper›PMID 32644803›Full record

ArticleThe journal of physical chemistry. B2020

Cholesterol Alters the Orientation and Activity of the Influenza Virus M2 Amphipathic Helix in the Membrane.

Agnieszka Martyna, Basma Bahsoun, Jesper J Madsen, Frederic St J S Jackson, Matthew D Badham, Gregory A Voth, Jeremy S Rossman

Open access · bronzeAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 3 institutions in 2 countries.

Agnieszka MartynaSchool of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom.
Basma BahsounSchool of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom.
Jesper J MadsenDepartment of Chemistry and Chicago Center for Theoretical Chemistry, The University of Chicago, Chicago, Illinois 60637, United States.ORCID 0000-0003-1411-9080
Frederic St J S JacksonSchool of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom.
Matthew D BadhamSchool of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom.
Gregory A VothDepartment of Chemistry and Chicago Center for Theoretical Chemistry, The University of Chicago, Chicago, Illinois 60637, United States.ORCID 0000-0002-3267-6748
Jeremy S RossmanSchool of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom.ORCID 0000-0001-6124-4103
University of Kent · GBUniversity of Chicago · USUniversity of South Florida · US

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 virus M2 amphipathic helix (M2AH) alters membrane curvature in a cholesterol-dependent manner, mediating viral membrane scission during influenza virus budding. Here, we have investigated the biophysical effects of cholesterol on the ability of an M2AH peptide to manipulate membrane properties. We see that the ability of the M2AH to interact with membranes and form an α-helix is independent of membrane cholesterol concentration; however, cholesterol affects the angle of the M2AH peptide within the membrane. This change in membrane orientation affects the ability of the M2AH to alter lipid order. In low-cholesterol membranes, the M2AH is inserted near the level of the lipid head groups, increasing lipid order, which may contribute to generation of the membrane curvature. As the cholesterol content increases, the M2AH insertion becomes flatter and slightly deeper in the membrane below the lipid headgroups, where the polar face can continue to interact with the headgroups while the hydrophobic face binds cholesterol. This changed orientation minimizes lipid packing defects and lipid order changes, likely reducing the generation of membrane curvature. Thus, cholesterol regulates M2 membrane scission by precisely modulating M2AH positioning within the membrane. This has implications for the understanding of many of amphipathic-helix-driven cellular budding processes that occur in specific lipid environments.

Indexed as

OrthomyxoviridaeViral Matrix ProteinsCell MembraneCholesterolLipid BilayersVirus ReleaseCholesterolLipid BilayersViral Matrix Proteins

Identifiers

PMID32644803
PMCPMC7515559
OpenAlexW3041583295

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.