Evidence map›Paper›PMID 31375589›Full record

ArticleJournal of virology2019

Analysis of HIV-1 Matrix-Envelope Cytoplasmic Tail Interactions.

Ayna Alfadhli, August O Staubus, Philip R Tedbury, Mariia Novikova, Eric O Freed, Eric Barklis

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 43 citations in OpenAlex.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
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  14. 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
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  16. Review
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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

6 authors at 2 institutions in 1 country.

Ayna AlfadhliDepartment of Molecular Microbiology and Immunology, Oregon Health & Sciences University, Portland, Oregon, USA.
August O StaubusDepartment of Molecular Microbiology and Immunology, Oregon Health & Sciences University, Portland, Oregon, USA.
Philip R TedburyVirus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.ORCID 0000-0001-8151-4967
Mariia NovikovaVirus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.
Eric O FreedVirus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.
Eric BarklisDepartment of Molecular Microbiology and Immunology, Oregon Health & Sciences University, Portland, Oregon, USA barklis@ohsu.edu.
Frederick National Laboratory for Cancer Research · USOregon Health & Science University · US

Funding

In Vitro Analysis of HIV Gag Protein InteractionsR01GM060170 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 1999 to 2019
$5.9M
HIV-1 Gag Precursor Protein InteractionsR01AI152579 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 2020 to 2024
$2.5M
NIAID NIH HHS R01 AI152579NIGMS NIH HHS R01 GM060170
6 · The paper itself

Abstract

The matrix (MA) domains of HIV-1 precursor Gag (PrGag) proteins direct PrGag proteins to plasma membrane (PM) assembly sites where envelope (Env) protein trimers are incorporated into virus particles. MA targeting to PM sites is facilitated by its binding to phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2], and MA binding to cellular RNAs appears to serve a chaperone function that prevents MA from associating with intracellular membranes prior to arrival at the PI(4,5)P2-rich PM. Investigations have shown genetic evidence of an interaction between MA and the cytoplasmic tails (CTs) of Env trimers that contributes to Env incorporation into virions, but demonstrations of direct MA-CT interactions have proven more difficult. In direct binding assays, we show here that MA binds to Env CTs. Using MA mutants, matrix-capsid (MACA) proteins, and MA proteins incubated in the presence of inositol polyphosphate, we show a correlation between MA trimerization and CT binding. RNA ligands with high affinities for MA reduced MA-CT binding levels, suggesting that MA-RNA binding interferes with trimerization and/or directly or indirectly blocks MA-CT binding. Rough-mapping studies indicate that C-terminal CT helices are involved in MA binding and are in agreement with cell culture studies with replication-competent viruses. Our results support a model in which full-length HIV-1 Env trimers are captured in assembling PrGag lattices by virtue of their binding to MA trimers.

Indexed as

Virus ReplicationBinding SitesCell MembraneCytosolgag Gene Products, Human Immunodeficiency VirusHumansModels, MolecularProtein BindingProtein ConformationProtein DomainsProtein MultimerizationViral Envelope ProteinsViral Matrix ProteinsViriongag Gene Products, Human Immunodeficiency VirusViral Envelope ProteinsViral Matrix Proteinshuman immunodeficiency virus

Identifiers

PMID31375589
PMCPMC6803273
OpenAlexW2966842897

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.