Evidence map›Paper›PMID 26992353›Full record

ArticleJournal of molecular biology2016

Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein.

Peter Y Mercredi, Nadine Bucca, Burk Loeliger, Christy R Gaines, Mansi Mehta, Pallavi Bhargava, Philip R Tedbury, Landry Charlier, Nicolas Floquet, Delphine Muriaux and 5 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Insect cell production of chimeric virus-like particles based on human immunodeficiency virus GAG proteins and yellow fever virus envelope protein.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  10. Article
  11. Article
  12. The "basics" of HIV-1 assembly.PLoS pathogens · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  17. Article
  18. Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Review
  20. Review

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

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

15 authors at 6 institutions in 2 countries.

Peter Y MercrediDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
Nadine BuccaDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
Burk LoeligerDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
Christy R GainesDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
Mansi MehtaDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
Pallavi BhargavaDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
Philip R TedburyVirus-Cell Interaction Section, HIV Dynamics and Replication Program, National Cancer Institute at Fredrick, Fredrick, MD 21702-1201, USA.
Landry CharlierInstitut des Biomolécules Max Mousseron, CNRS UMR5247, Université Montpellier, Faculté de Pharmacie, Montpellier Cedex 05, France.
Nicolas FloquetInstitut des Biomolécules Max Mousseron, CNRS UMR5247, Université Montpellier, Faculté de Pharmacie, Montpellier Cedex 05, France.
Delphine MuriauxCentre d'études d'agents Pathogénes et Biotechnologies pour la Santé CNRS-UMR 5236, Université Montpellier, Montpellier Cedex 5, France.
Cyril FavardCentre d'études d'agents Pathogénes et Biotechnologies pour la Santé CNRS-UMR 5236, Université Montpellier, Montpellier Cedex 5, France.
Charles R SandersDepartment of Biochemistry, Center for Structural Biology, and Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37240-7917, USA.
Eric O FreedVirus-Cell Interaction Section, HIV Dynamics and Replication Program, National Cancer Institute at Fredrick, Fredrick, MD 21702-1201, USA. Electronic address: efreed@mail.nih.gov.
Jan MarchantDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA. Electronic address: janm@umbc.edu.
Michael F SummersDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA. Electronic address: summers@hhmi.umbc.edu.
Howard Hughes Medical Institute · USCentre National de la Recherche Scientifique · FRUniversity of Maryland, Baltimore County · USScience Applications International Corporation (United States) · USInstitut des Biomolécules Max Mousseron · FRVanderbilt University · US

Funding

The Center for HIV RNA Studies (CRNA)P50GM103297 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAYIE, KWAKU · 2012 to 2016
$21.7M
EXPAND PARTICIPATION BY MINORITIES IN BIOMEDICAL SCIENCER25GM055036 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1996 to 2021
$16.9M
HIV-1 Gag Assembly and MaturationZIABC011720 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FREED, ERIC · 2016 to 2025
$7.2M
NMR STUDIES OF HIV1 PROTEINSR37AI030917 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1997 to 2015
$4.9M
Cholesterol and the Amyloid Precursor ProteinR01GM106672 · NIGMS · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 2013 to 2016
$1.2M
Retroviral Gag Trafficking, Env Incorporation, and Virus AssemblyZ01BC010775 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FREED, ERIC · 2007 to 2008
$961k
NMR STUDIES OF HIV-1 PROTEINSR01AI030917 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI SUMMERS, MICHAEL F. · 1991 to 1996
–
Howard Hughes Medical InstituteIntramural NIH HHS Z01 BC010775NIAID NIH HHS AI30917NIAID NIH HHS R37 AI030917NIGMS NIH HHS GM103297NIGMS NIH HHS GM106672NIGMS NIH HHS P50 GM103297NIGMS NIH HHS R01 GM106672NIGMS NIH HHS R25 GM055036NIGMS NIH HHS R25-GM55036
6 · The paper itself

Abstract

Assembly of HIV-1 particles is initiated by the trafficking of viral Gag polyproteins from the cytoplasm to the plasma membrane, where they co-localize and bud to form immature particles. Membrane targeting is mediated by the N-terminally myristoylated matrix (MA) domain of Gag and is dependent on the plasma membrane marker phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2]. Recent studies revealed that PI(4,5)P2 molecules containing truncated acyl chains [tr-PI(4,5)P2] are capable of binding MA in an "extended lipid" conformation and promoting myristoyl exposure. Here we report that tr-PI(4,5)P2 molecules also readily bind to non-membrane proteins, including HIV-1 capsid, which prompted us to re-examine MA-PI(4,5)P2 interactions using native lipids and membrane mimetic liposomes and bicelles. Liposome binding trends observed using a recently developed NMR approach paralleled results of flotation assays, although the affinities measured under the equilibrium conditions of NMR experiments were significantly higher. Native PI(4,5)P2 enhanced MA binding to liposomes designed to mimic non-raft-like regions of the membrane, suggesting the possibility that binding of the protein to disordered domains may precede Gag association with, or nucleation of, rafts. Studies with bicelles revealed a subset of surface and myr-associated MA residues that are sensitive to native PI(4,5)P2, but cleft residues that interact with the 2'-acyl chains of tr-PI(4,5)P2 molecules in aqueous solution were insensitive to native PI(4,5)P2 in bicelles. Our findings call to question extended-lipid MA:membrane binding models, and instead support a model put forward from coarse-grained simulations indicating that binding is mediated predominantly by dynamic, electrostatic interactions between conserved basic residues of MA and multiple PI(4,5)P2 and phosphatidylserine molecules.

Indexed as

Cell Membranegag Gene Products, Human Immunodeficiency VirusHIV-1LipidsLiposomesMagnetic Resonance SpectroscopyMembrane MicrodomainsPhosphatidylinositol 4,5-DiphosphatePhosphatidylserinesProtein BindingProtein Structure, Tertiarygag Gene Products, Human Immunodeficiency VirusLipidsLiposomesPhosphatidylinositol 4,5-DiphosphatePhosphatidylserinesbicellesHIV-1 matrix proteinmembrane targetingPIP2polysomes

Identifiers

PMID26992353
PMCPMC4836608
OpenAlexW2300191215

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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.