Evidence map›Paper›PMID 39116647›Full record

ArticleVirology2024

Conserved sequence features in intracellular domains of viral spike proteins.

Vinh-Nhan Ngo, David P Winski, Brandon Aho, Pauline L Kamath, Benjamin L King, Hang Waters, Joshua Zimmerberg, Alexander Sodt, Samuel T Hess

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
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

9 authors.

Vinh-Nhan NgoDepartment of Physics and Astronomy, 120 Bennett Hall, University of Maine, Orono, ME, 04469-5709, USA.
David P WinskiDepartment of Physics and Astronomy, 120 Bennett Hall, University of Maine, Orono, ME, 04469-5709, USA.
Brandon AhoDepartment of Physics and Astronomy, 120 Bennett Hall, University of Maine, Orono, ME, 04469-5709, USA.
Pauline L KamathSchool of Food and Agriculture, 342 Hitchner Hall, University of Maine, And Maine Center for Genetics in the Environment, Orono, ME, USA. Electronic address: pauline.kamath@maine.edu.
Benjamin L KingDepartment of Molecular and Biomedical Sciences, 5735 Hitchner Hall, University of Maine, Orono, ME, USA. Electronic address: benjamin.l.king@maine.edu.
Hang WatersSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Joshua ZimmerbergSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Alexander SodtUnit on Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Samuel T HessDepartment of Physics and Astronomy, 120 Bennett Hall, University of Maine, Orono, ME, 04469-5709, USA. Electronic address: samuel.hess@maine.edu.

Funding

The Maine Biomedical Research Network (INBRE)P20GM103423 · NIGMS · MOUNT DESERT ISLAND BIOLOGICAL LAB · PI JAMES A COFFMAN · 2012 to 2026
$60.0M
Membrane Remodeling in Viral Infection, Parasite Replication, and Traumatic Brain InjuryZIAHD001409 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ZIMMERBERG, JOSHUA · 2009 to 2025
$29.9M
Regulation of Cellular Behavior in Response to Extracellular CuesP20GM144265 · NIGMS · UNIVERSITY OF MAINE ORONO · PI Benjamin L King · 2023 to 2026
$11.8M
Molecular simulations of lipid curvature stress and its effect on transmembrane proteinsZIAHD008955 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SODT, ALEXANDER · 2016 to 2025
$6.2M
Mechanism of Interaction between Influenza Hemagglutinin and Host Cell PhosphoinositidesR15GM139070 · NIGMS · UNIVERSITY OF MAINE ORONO · PI HESS, SAMUEL T · 2020 to 2020
$428k
NIGMS NIH HHS P20 GM103423NIGMS NIH HHS P20 GM144265NIGMS NIH HHS R15 GM139070
6 · The paper itself

Abstract

Viral spike proteins mutate frequently, but conserved features within these proteins often have functional importance and can inform development of anti-viral therapies which circumvent the effects of viral sequence mutations. Through analysis of large numbers of viral spike protein sequences from several viral families, we found highly (>99%) conserved patterns within their intracellular domains. The patterns generally consist of one or more basic amino acids (arginine or lysine) adjacent to a cysteine, many of which are known to undergo acylation. These patterns were not enriched in cellular proteins in general. Molecular dynamics simulations show direct electrostatic and hydrophobic interactions between these conserved residues in hemagglutinin (HA) from influenza A and B and the phosphoinositide PIP2. Super-resolution microscopy shows nanoscale colocalization of PIP2 and several of the same viral proteins. We propose the hypothesis that these conserved viral spike protein features can interact with phosphoinositides such as PIP2.

Indexed as

Conserved SequenceMolecular Dynamics SimulationAmino Acid SequenceHumansHydrophobic and Hydrophilic InteractionsInfluenza A virusProtein DomainsSpike Glycoprotein, CoronavirusSpike Glycoprotein, CoronavirusAcylationConservationInfluenzaMembranePhosphoinositidesPolybasicSpike

Identifiers

PMID39116647
PMCPMC11383743

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.