Evidence map›Paper›PMID 33709461›Full record

ArticleThe Journal of physiology2021

The envelope protein of SARS-CoV-2 increases intra-Golgi pH and forms a cation channel that is regulated by pH.

David Cabrera-Garcia, Ramsey Bekdash, Geoffrey W Abbott, Masayuki Yazawa, Neil L Harrison

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.8field-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

45 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
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  8. SARS-CoV-2 Is an Electricity-Driven Virus.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

David Cabrera-GarciaDepartment of Anesthesiology, Columbia University, New York, NY, USA.ORCID 0000-0001-9609-9102
Ramsey BekdashDepartment of Molecular Pharmacology and Therapeutics, Columbia University, New York, NY, USA.ORCID 0000-0003-1825-7130
Geoffrey W AbbottBioelectricity Laboratory, Department of Physiology and Biophysics, School of Medicine, University of California, Irvine, CA, USA.
Masayuki YazawaDepartment of Molecular Pharmacology and Therapeutics, Columbia University, New York, NY, USA.
Neil L HarrisonDepartment of Anesthesiology, Columbia University, New York, NY, USA.
Columbia University · USUniversity of California, Irvine · US

Funding

Ion Channel Transporter InteractionsR35GM130377 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI Geoffrey W Abbott · 2019 to 2026
$4.0M
Columbia Stem Cell InitiativeColumbia University Irving Medical Centre Dean's Office FundDepartment of Anesthesiology at CUIMCNIGMS NIH HHS R35 GM130377NIH, National Institute of General Medical Sciences GM130377
6 · The paper itself

Abstract

key pointsWe report a novel method for the transient expression of SARS-CoV-2 envelope (E) protein in intracellular organelles and the plasma membrane of mammalian cells and Xenopus oocytes. Intracellular expression of SARS-CoV-2 E protein increases intra-Golgi pH. By targeting the SARS-CoV-2 E protein to the plasma membrane, we show that it forms a cation channel, viroporin, that is modulated by changes of pH. This method for studying the activity of viroporins may facilitate screening for new antiviral drugs to identify novel treatments for COVID-19. ABSTRACT: The envelope (E) protein of coronaviruses such as SARS-CoV-1 is proposed to form an ion channel or viroporin that participates in viral propagation and pathogenesis. Here we developed a technique to study the E protein of SARS-CoV-2 in mammalian cells by directed targeting using a carboxyl-terminal fluorescent protein tag, mKate2. The wild-type SARS-CoV-2 E protein can be trafficked to intracellular organelles, notably the endoplasmic reticulum-Golgi intermediate complex, where its expression increases pH inside the organelle. We also succeeded in targeting SARS-CoV-2 E to the plasma membrane, which enabled biophysical analysis using whole-cell patch clamp recording in a mammalian cell line, HEK 293 cells, and two-electrode voltage clamp electrophysiology in Xenopus oocytes. The results suggest that the E protein forms an ion channel that is permeable to monovalent cations such as Na

Indexed as

COVID-19SARS-CoV-2AnimalsCationsHEK293 CellsHumansHydrogen-Ion ConcentrationCationsenvelope proteinion channelmembrane targetingSARS-CoV-2

Identifiers

PMID33709461
PMCPMC8251088
OpenAlexW3134601812

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.