ArticlePLoS pathogens2009
Structure and inhibition of the SARS coronavirus envelope protein ion channel.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04420260 (Scheme of Primary Prevention of Infection by COVID-19, in Workers), which is not on this map. Cited by 155 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
Scheme of Primary Prevention of Infection by COVID-19, in Workers: Phase II Controlled Clinical Trial, to be Carried Out in Medellín-Antioquia
Who cites it
155 citing papers in PubMed, 1 synthesis or guideline pooled it, 260 citations in OpenAlex.
- Drug targets for corona virus: A systematic review.Indian journal of pharmacologyPooled it
- Structural insights into an aptainhibitor of the SARS-CoV-2 E protein using molecular docking, molecular dynamics, and biophysical analyses.Molecular therapy. Nucleic acids · 2026Article
- Unraveling the Mystery: COVID-19 and Diabetic Complications - A Journey from Pathophysiology to Treatment.Current diabetes reviews · 2026Review
- Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025Article
- Molecular Dynamics Simulation of SARS-CoV-2 E Ion Channel: The Study of Lone Protein and its Conformational Changes in Complex with Potential Cage Inhibitors.Current computer-aided drug design · 2025Article
- Prediction of conformational states in a coronavirus channel using Alphafold-2 and DeepMSA2: Strengths and limitations.Computational and structural biotechnology journal · 2024Article
- Coronavirus envelope protein activates TMED10-mediated unconventional secretion of inflammatory factors.Nature communications · 2024Article
- Transmembrane conformation of the envelope protein of an alpha coronavirus, NL63.Protein science : a publication of the Protein Society · 2024Article
- Developing inhibitory peptides against SARS-CoV-2 envelope protein.PLoS biology · 2024Article
- Membrane Condensation and Curvature Induced by SARS-CoV-2 Envelope Protein.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Analysis of SARS-CoV-2 genome evolutionary patterns.Microbiology spectrum · 2024Article
- A short sequence in the tail of SARS-CoV-2 envelope protein controls accessibility of its PDZ-binding motif to the cytoplasm.The Journal of biological chemistry · 2024Article
- Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein.Communications biology · 2023Article
- Reply to: Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection.Nature chemical biology · 2023Article
- Atomic structure of the open SARS-CoV-2 E viroporin.Science advances · 2023Article
- Hexamethylene amiloride binds the SARS-CoV-2 envelope protein at the protein-lipid interface.Protein science : a publication of the Protein Society · 2023Article
- The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization.International journal of molecular sciences · 2023Article
- Patch-clamp studies and cell viability assays suggest a distinct site for viroporin inhibitors on the E protein of SARS-CoV-2.Virology journal · 2023Article
- SARS-CoV-2 Nucleocapsid Protein Is a Potential Therapeutic Target for Anticoronavirus Drug Discovery.Microbiology spectrum · 2023Article
- Article
95 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The envelope (E) protein from coronaviruses is a small polypeptide that contains at least one alpha-helical transmembrane domain. Absence, or inactivation, of E protein results in attenuated viruses, due to alterations in either virion morphology or tropism. Apart from its morphogenetic properties, protein E has been reported to have membrane permeabilizing activity. Further, the drug hexamethylene amiloride (HMA), but not amiloride, inhibited in vitro ion channel activity of some synthetic coronavirus E proteins, and also viral replication. We have previously shown for the coronavirus species responsible for severe acute respiratory syndrome (SARS-CoV) that the transmembrane domain of E protein (ETM) forms pentameric alpha-helical bundles that are likely responsible for the observed channel activity. Herein, using solution NMR in dodecylphosphatidylcholine micelles and energy minimization, we have obtained a model of this channel which features regular alpha-helices that form a pentameric left-handed parallel bundle. The drug HMA was found to bind inside the lumen of the channel, at both the C-terminal and the N-terminal openings, and, in contrast to amiloride, induced additional chemical shifts in ETM. Full length SARS-CoV E displayed channel activity when transiently expressed in human embryonic kidney 293 (HEK-293) cells in a whole-cell patch clamp set-up. This activity was significantly reduced by hexamethylene amiloride (HMA), but not by amiloride. The channel structure presented herein provides a possible rationale for inhibition, and a platform for future structure-based drug design of this potential pharmacological target.
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Registered trials
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.