Evidence map›Paper›PMID 36403071›Full record

ArticleRetrovirology2022

The envelope proteins from SARS-CoV-2 and SARS-CoV potently reduce the infectivity of human immunodeficiency virus type 1 (HIV-1).

Wyatt Henke, Hope Waisner, Sachith Polpitiya Arachchige, Maria Kalamvoki, Edward Stephens

Open access · goldAbstract read
In one paragraph

Article in Retrovirology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Wyatt HenkeDepartment of Microbiology, Molecular Genetics and ImmunologyUniversity of Kansas Medical Center, 2000 Hixon Hall 3901 Rainbow Blvd, Kansas, KS, 66160, USA.
Hope WaisnerDepartment of Microbiology, Molecular Genetics and ImmunologyUniversity of Kansas Medical Center, 2000 Hixon Hall 3901 Rainbow Blvd, Kansas, KS, 66160, USA.
Sachith Polpitiya ArachchigeDepartment of Microbiology, Molecular Genetics and ImmunologyUniversity of Kansas Medical Center, 2000 Hixon Hall 3901 Rainbow Blvd, Kansas, KS, 66160, USA.
Maria KalamvokiDepartment of Microbiology, Molecular Genetics and ImmunologyUniversity of Kansas Medical Center, 2000 Hixon Hall 3901 Rainbow Blvd, Kansas, KS, 66160, USA.
Edward StephensDepartment of Microbiology, Molecular Genetics and ImmunologyUniversity of Kansas Medical Center, 2000 Hixon Hall 3901 Rainbow Blvd, Kansas, KS, 66160, USA. estephen@kumc.edu.
University of Kansas Medical Center · US

Funding

RADx-UP: Improving the Response of Local Urban and Rural Communities to Disparities in Covid-19 TestingUL1TR002366 · NCATS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI Mario Castro, JAMES STEVEN LEEDER · 2017 to 2026
$44.3M
Cargo, biogenesis and functions of extracellular vesicles released during HSV-1 infectionR01AI162784 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI Maria Kalamvoki · 2021 to 2026
$2.4M
Immunomodulatory effects of coronavirus membrane proteins E, M, and S.R21AI158229 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI KALAMVOKI, MARIA, STEPHENS, EDWARD BRICE · 2020 to 2020
$421k
NCATS NIH HHS UL1 TR002366NIAID NIH HHS R01 AI162784NIAID NIH HHS R21 AI158229
6 · The paper itself

Abstract

backgroundViroporins are virally encoded ion channels involved in virus assembly and release. Human immunodeficiency virus type 1 (HIV-1) and influenza A virus encode for viroporins. The human coronavirus SARS-CoV-2 encodes for at least two viroporins, a small 75 amino acid transmembrane protein known as the envelope (E) protein and a larger 275 amino acid protein known as Orf3a. Here, we compared the replication of HIV-1 in the presence of four different β-coronavirus E proteins.

resultsWe observed that the SARS-CoV-2 and SARS-CoV E proteins reduced the release of infectious HIV-1 yields by approximately 100-fold while MERS-CoV or HCoV-OC43 E proteins restricted HIV-1 infectivity to a lesser extent. Mechanistically, neither reverse transcription nor mRNA synthesis was involved in the restriction. We also show that all four E proteins caused phosphorylation of eIF2-α at similar levels and that lipidation of LC3-I could not account for the differences in restriction. However, the level of caspase 3 activity in transfected cells correlated with HIV-1 restriction in cells. Finally, we show that unlike the Vpu protein of HIV-1, the four E proteins did not significantly down-regulate bone marrow stromal cell antigen 2 (BST-2).

conclusionsThe results of this study indicate that while viroporins from homologous viruses can enhance virus release, we show that a viroporin from a heterologous virus can suppress HIV-1 protein synthesis and release of infectious virus.

Indexed as

COVID-19HIV-1Amino AcidsHumansSARS-CoV-2Viroporin ProteinsVirus ReplicationAmino AcidsViroporin Proteins

Identifiers

PMID36403071
PMCPMC9675205
OpenAlexW4309562194

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.