Evidence map›Paper›PMID 31757854›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Single-molecule imaging of HIV-1 envelope glycoprotein dynamics and Gag lattice association exposes determinants responsible for virus incorporation.

Nairi Pezeshkian, Nicholas S Groves, Schuyler B van Engelenburg

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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
3.9field-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, 41 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
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  20. HIV envelope tail truncation confers resistance to SERINC5 restriction.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

3 authors at 1 institution in 1 country.

Nairi PezeshkianMolecular and Cellular Biophysics Program, Department of Biological Sciences, University of Denver, Denver, CO 80210.
Nicholas S GrovesMolecular and Cellular Biophysics Program, Department of Biological Sciences, University of Denver, Denver, CO 80210.
Schuyler B van EngelenburgMolecular and Cellular Biophysics Program, Department of Biological Sciences, University of Denver, Denver, CO 80210 schuyler.vanengelenburg@du.edu.ORCID 0000-0003-2100-3617
University of Denver · US

Funding

Identifying determinants of HIV-1 responsible for the nanoscale distribution and dynamics of virus assemblyR01AI138625 · NIAID · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI Schuyler van Engelenburg · 2018 to 2026
$3.3M
NIAID NIH HHS R01 AI138625
6 · The paper itself

Abstract

The HIV-1 envelope glycoprotein (Env) is sparsely incorporated onto assembling virus particles on the host cell plasma membrane in order for the virus to balance infectivity and evade the immune response. Env becomes trapped in a nascent particle on encounter with the polymeric viral protein Gag, which forms a dense protein lattice on the inner leaflet of the plasma membrane. While Env incorporation efficiency is readily measured biochemically from released particles, very little is known about the spatiotemporal dynamics of Env trapping events. Herein, we demonstrate, via high-resolution single-molecule tracking, that retention of Env trimers within single virus assembly sites requires the Env cytoplasmic tail (CT) and the L12 residue in the matrix (MA) domain of Gag but does not require curvature of the viral lattice. We further demonstrate that Env trimers are confined to subviral regions of a budding Gag lattice, supporting a model where direct interactions and/or steric corralling between the Env-CT and a lattice of MA trimers promote Env trapping and infectious HIV-1 assembly.

Indexed as

Virus AssemblyCell Membraneenv Gene Products, Human Immunodeficiency Virusgag Gene Products, Human Immunodeficiency VirusHIV-1HIV InfectionsHumansProtein BindingProtein DomainsSingle Molecule Imagingenv Gene Products, Human Immunodeficiency Virusgag Gene Products, Human Immunodeficiency Virushuman immunodeficiency virus 1 (HIV-1)single-particle trackingvirus assembly

Identifiers

PMID31757854
PMCPMC6911212
OpenAlexW2991106891

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.