Evidence map›Paper›PMID 36807531›Full record

ArticleJournal of cell science2023

SARS-CoV-2 infection alkalinizes the ERGIC and lysosomes through the viroporin activity of the viral envelope protein.

Wen-An Wang, Amado Carreras-Sureda, Nicolas Demaurex

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.5field-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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  8. Nonlytic Egress and Transmission in the Virus World.Annual review of biochemistry · 2025
    Review
  9. The peptidoglycan ofScience translational medicine · 2025
    Article
  10. Article
  11. Review
  12. SARS-CoV-2 Is an Electricity-Driven Virus.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  13. Review
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  15. Article
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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

3 authors at 1 institution in 1 country.

Wen-An WangDepartment of Cell Physiology and Metabolism, University of Geneva, Geneva 1211, Switzerland.ORCID 0000-0003-3871-0174
Amado Carreras-SuredaDepartment of Cell Physiology and Metabolism, University of Geneva, Geneva 1211, Switzerland.ORCID 0000-0002-9032-5639
Nicolas DemaurexDepartment of Cell Physiology and Metabolism, University of Geneva, Geneva 1211, Switzerland.ORCID 0000-0002-9933-6772
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The coronavirus SARS-CoV-2, the agent of the deadly COVID-19 pandemic, is an enveloped virus propagating within the endocytic and secretory organelles of host mammalian cells. Enveloped viruses modify the ionic homeostasis of organelles to render their intra-luminal milieu permissive for viral entry, replication and egress. Here, we show that infection of Vero E6 cells with the delta variant of the SARS-CoV-2 alkalinizes the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) as well as lysosomes, mimicking the effect of inhibitors of vacuolar proton ATPases. We further show the envelope protein of SARS-CoV-2 accumulates in the ERGIC when expressed in mammalian cells and selectively dissipates the ERGIC pH. This viroporin action is prevented by mutations of Val25 but not Asn15 within the channel pore of the envelope (E) protein. We conclude that the envelope protein acts as a proton channel in the ERGIC to mitigate the acidity of this intermediate compartment. The altered pH homeostasis of the ERGIC likely contributes to the virus fitness and pathogenicity, making the E channel an attractive drug target for the treatment of COVID-19.

Indexed as

COVID-19Viral Envelope ProteinsAnimalsGolgi ApparatusHumansLysosomesMammalsPandemicsProtonsSARS-CoV-2Viroporin ProteinsProtonsViral Envelope ProteinsViroporin ProteinsCoronavirusCOVID-19Ion channelViroporinVirus–host interactions

Identifiers

PMID36807531
PMCPMC10112968
OpenAlexW4321454620

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.