ArticleBiochimica et biophysica acta. Biomembranes2018
Structural model of the SARS coronavirus E channel in LMPG micelles.
Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
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95 citing papers in PubMed, 186 citations in OpenAlex.
- Full-length SARS-CoV-2 envelope protein adopts an interfacial topology in lipid bilayers.Biochimica et biophysica acta. Biomembranes · 2026Article
- Structural Bases for the Unconventional Activity of a Viroporin Channel.Biochemistry · 2026Article
- Pentameric Architecture of the SARS-CoV-2 Envelope Protein Revealed by SEC-MALS, Cryo-EM, and Molecular Dynamics.The journal of physical chemistry. B · 2026Article
- Phosphatidylinositol Interactions with the SARS-CoV-2 Envelope Protein Investigated by LipidBiochemistry · 2026Article
- C-terminus-outward orientation of SARS-CoV-2 envelope proteins on viral capsid enables a novel virus-cell interaction pathway.Frontiers in cellular and infection microbiology · 2026Article
- Membrane Depth Measurements of E Protein byBiophysica · 2025Article
- Highly versatile small virus-encoded proteins in cellular membranes: A structural perspective on how proteins' inherent conformational plasticity couples with host membranes' properties to control cellular processes.Journal of structural biology: X · 2025Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025Article
- Article
- Oligomeric State and Drug Binding of the SARS-CoV-2 Envelope Protein Are Sensitive to the Ectodomain.Journal of the American Chemical Society · 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
- Electrophysiological properties and structural prediction of the SARS-CoV-2 viroprotein E.Frontiers in molecular biosciences · 2024Article
- Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein.Communications biology · 2023Article
- Atomic structure of the open SARS-CoV-2 E viroporin.Science advances · 2023Article
- M Protein from Dengue virus oligomerizes to pentameric channel protein: in silico analysis study.Genomics & informatics · 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
35 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.
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