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dc.creatorRouka E., Gourgoulianis K.I., Zarogiannis S.G.en
dc.date.accessioned2023-01-31T09:51:51Z
dc.date.available2023-01-31T09:51:51Z
dc.date.issued2021
dc.identifier10.1152/AJPLUNG.00443.2020
dc.identifier.issn10400605
dc.identifier.urihttp://hdl.handle.net/11615/78561
dc.description.abstractViroporins, integral viral membrane ion channel proteins, interact with host-cell proteins deregulating physiological processes and activating inflammasomes. Severity of COVID-19 might be associated with hyperinflammation, thus we aimed at the complete immunoinformatic analysis of the SARS-CoV-2 viroporin E, P0DTC4. We also identified the human proteins interacting with P0DTC4 and the enriched molecular functions of the corresponding genes. The complete sequence of P0DTC4 in FASTA format was processed in 10 databases relative to secondary and tertiary protein structure analyses and prediction of optimal vaccine epitopes. Three more databases were accessed for the retrieval and the molecular functional characterization of the P0DTC4 human interactors. The immunoinformatics analysis resulted in the identification of 4 discontinuous B-cell epitopes along with 1 linear B-cell epitope and 11 T-cell epitopes which were found to be antigenic, immunogenic, nonallergen, nontoxin, and unable to induce autoimmunity thus fulfilling prerequisites for vaccine design. The functional enrichment analysis showed that the predicted host interactors of P0DTC4 target the cellular acetylation network. Two of the identified host-cell proteins – BRD2 and BRD4 – have been shown to be promising targets for antiviral therapy. Thus, our findings have implications for COVID-19 therapy and indicate that viroporin E could serve as a promising vaccine target against SARS-CoV-2. Validation experiments are required to complement these in silico results. Copyright © 2021 the American Physiological Societyen
dc.language.isoenen
dc.sourceAmerican Journal of Physiology - Lung Cellular and Molecular Physiologyen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85108124233&doi=10.1152%2fAJPLUNG.00443.2020&partnerID=40&md5=f884c231aa8bcd0882f20734cbacdd30
dc.subjectmembrane proteinen
dc.subjectPODTC4 proteinen
dc.subjectunclassified drugen
dc.subjectviroporinen
dc.subjectcell cycle proteinen
dc.subjectepitopeen
dc.subjecttranscription factoren
dc.subjectacetylationen
dc.subjectantigenicityen
dc.subjectArticleen
dc.subjectcomputer modelen
dc.subjectcontrolled studyen
dc.subjectfunctional enrichment analysisen
dc.subjectimmunogenicityen
dc.subjectimmunoinformaticsen
dc.subjectprotein protein interactionen
dc.subjectprotein targetingen
dc.subjectprotein tertiary structureen
dc.subjectSevere acute respiratory syndrome coronavirus 2en
dc.subjectstructure analysisen
dc.subjectamino acid sequenceen
dc.subjectcomputer simulationen
dc.subjecthumanen
dc.subjectimmunologyen
dc.subjectprevention and controlen
dc.subjectAmino Acid Sequenceen
dc.subjectCell Cycle Proteinsen
dc.subjectComputer Simulationen
dc.subjectCOVID-19en
dc.subjectCOVID-19 Vaccinesen
dc.subjectEpitopes, B-Lymphocyteen
dc.subjectEpitopes, T-Lymphocyteen
dc.subjectHumansen
dc.subjectSARS-CoV-2en
dc.subjectTranscription Factorsen
dc.subjectViroporin Proteinsen
dc.subjectAmerican Physiological Societyen
dc.titleIn silico investigation of the viroporin E as a vaccine target against SARS-CoV-2en
dc.typejournalArticleen


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