ArticleBiophysical journal2005
The transmembrane oligomers of coronavirus protein E.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 95 citations in OpenAlex.
- 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
- Prediction of conformational states in a coronavirus channel using Alphafold-2 and DeepMSA2: Strengths and limitations.Computational and structural biotechnology journal · 2024Article
- Oligomeric State and Drug Binding of the SARS-CoV-2 Envelope Protein Are Sensitive to the Ectodomain.Journal of the American Chemical Society · 2024Article
- Membrane Activity and Viroporin Assembly for the SARS-CoV-2 E Protein Are Regulated by Cholesterol.Biomolecules · 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
- Hexamethylene amiloride binds the SARS-CoV-2 envelope protein at the protein-lipid interface.Protein science : a publication of the Protein Society · 2023Article
- Structural and non-structural proteins in SARS-CoV-2: potential aspects to COVID-19 treatment or prevention of progression of related diseases.Cell communication and signaling : CCS · 2023Review
- SARS-CoV-2 Harnesses Host Translational Shutoff and Autophagy To Optimize Virus Yields: the Role of the Envelope (E) Protein.Microbiology spectrum · 2023Article
- SARS-CoV-2 Envelope Protein Forms Clustered Pentamers in Lipid Bilayers.Biochemistry · 2022Article
- Oligomerization-Dependent Beta-Structure Formation in SARS-CoV-2 Envelope Protein.International journal of molecular sciences · 2022Article
- SARS-CoV-2 Envelope (E) Protein Binds and Activates TLR2 Pathway: A Novel Molecular Target for COVID-19 Interventions.Viruses · 2022Article
- Viroporins: Structure, function, and their role in the life cycle of SARS-CoV-2.The international journal of biochemistry & cell biology · 2022Review
- Article
- Computational Study on the Function of Palmitoylation on the Envelope Protein in SARS-CoV-2.Journal of chemical theory and computation · 2021Article
- Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study.Biochemistry and biophysics reports · 2021Article
- Characterization of the SARS-CoV-2 E Protein: Sequence, Structure, Viroporin, and Inhibitors.Protein science : a publication of the Protein Society · 2021Review
- SARS-CoV-2: Insights into its structural intricacies and functional aspects for drug and vaccine development.International journal of biological macromolecules · 2021Review
- Understanding COVID-19 via comparative analysis of dark proteomes of SARS-CoV-2, human SARS and bat SARS-like coronaviruses.Cellular and molecular life sciences : CMLS · 2021Article
- Self-Organized Morphology and Multiscale Structures of CoVE Proteins.JOM (Warrendale, Pa. : 1989) · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have tested the hypothesis that severe acute respiratory syndrome (SARS) coronavirus protein E (SCoVE) and its homologs in other coronaviruses associate through their putative transmembrane domain to form homooligomeric alpha-helical bundles in vivo. For this purpose, we have analyzed the results of molecular dynamics simulations where all possible conformational and aggregational space was systematically explored. Two main assumptions were considered; the first is that protein E contains one transmembrane alpha-helical domain, with its N- and C-termini located in opposite faces of the lipid bilayer. The second is that protein E forms the same type of transmembrane oligomer and with identical backbone structure in different coronaviruses. The models arising from the molecular dynamics simulations were tested for evolutionary conservation using 13 coronavirus protein E homologous sequences. It is extremely unlikely that if any of our assumptions were not correct we would find a persistent structure for all the sequences tested. We show that a low energy dimeric, trimeric and two pentameric models appear to be conserved through evolution, and are therefore likely to be present in vivo. In support of this, we have observed only dimeric, trimeric, and pentameric aggregates for the synthetic transmembrane domain of SARS protein E in SDS. The models obtained point to residues essential for protein E oligomerization in the life cycle of the SARS virus, specifically N15. In addition, these results strongly support a general model where transmembrane domains transiently adopt many aggregation states necessary for function.
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