Evidence map›Paper›PMID 29544440›Full record

ArticleBMC cell biology2018

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

Jackie Perrin, Aurélie Bary, Alexandre Vernay, Pierre Cosson

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 46% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. 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

4 authors at 1 institution in 1 country.

Jackie PerrinDepartment of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1 rue Michel Servet, 1211, Geneva 4, Switzerland. jackie.perrin-simonnot@unige.ch.ORCID 0000-0003-1519-1244
Aurélie BaryDepartment of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1 rue Michel Servet, 1211, Geneva 4, Switzerland.
Alexandre VernayDepartment of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1 rue Michel Servet, 1211, Geneva 4, Switzerland.
Pierre CossonDepartment of Cell Physiology and Metabolism, Faculty of Medicine, University of Geneva, 1 rue Michel Servet, 1211, Geneva 4, Switzerland.
University of Geneva · CH

Funding

Swiss National Science Foundation 31003A-172951
6 · The paper itself

Abstract

backgroundThe envelope protein of lentiviruses are type I transmembrane proteins, and their transmembrane domain contains conserved potentially charged residues. This highly unusual feature would be expected to cause endoplasmic reticulum (ER) localization. The aim of this study was to determine by which means the HIV-1 Env protein is transported to the cell surface although its transmembrane domain contains a conserved arginine residue.

resultsWe expressed various chimeric proteins and analyzed the influence of their transmembrane domain on their intracellular localization. The transmembrane domain of the HIV-1 Env protein does not cause ER retention. This is not due to the presence of conserved glycine residues, or to the position of the arginine residue, but to the length of the transmembrane domain. A shortened version of the Env transmembrane domain causes arginine-dependent ER targeting. Remarkably, the transmembrane domain of the HIV-1 Env protein, although it does not confer ER retention, interacts efficiently with negatively charged residues in the membrane.

conclusionThese results suggest that the intrinsic properties of the HIV-1 Env transmembrane domain allow the protein to escape ER-retention mechanisms, while maintaining its ability to interact with cellular proteins and to influence cellular physiology.

Indexed as

Amino AcidsAmino Acid SequenceCell MembraneEndoplasmic Reticulumenv Gene Products, Human Immunodeficiency VirusHeLa CellsHIV-1HumansIntracellular SpaceLentivirusProtein DomainsProtein TransportStructure-Activity RelationshipAmino Acidsenv Gene Products, Human Immunodeficiency VirusEndoplasmic reticulumEnvelope proteingp160HIV-1Secretory pathwayTransmembrane domain

Identifiers

PMID29544440
PMCPMC5856207
OpenAlexW2803815732

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.