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Tytuł:
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Development of new vaccine target against SARS-CoV2 using envelope (E) protein: An evolutionary, molecular modeling and docking based study.
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Autorzy:
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Bhattacharya S; Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati, Assam, India.
Banerjee A; Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia, India.
Ray S; Amity Institute of Bioechnology, Amity University, Kolkata, India. Electronic address: .
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Źródło:
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International journal of biological macromolecules [Int J Biol Macromol] 2021 Mar 01; Vol. 172, pp. 74-81. Date of Electronic Publication: 2020 Dec 29.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
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MeSH Terms:
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Evolution, Molecular*
Molecular Docking Simulation*
COVID-19/*immunology
COVID-19 Vaccines/*immunology
Coronavirus Envelope Proteins/*immunology
SARS-CoV-2/*immunology
Amino Acid Sequence ; Coronavirus Envelope Proteins/chemistry ; Coronavirus Envelope Proteins/genetics ; Epitopes, B-Lymphocyte/chemistry ; Epitopes, B-Lymphocyte/immunology ; Epitopes, T-Lymphocyte/chemistry ; Epitopes, T-Lymphocyte/immunology ; Humans ; Hydrogen Bonding ; Kinetics ; Mutation/genetics ; Phylogeny ; Protein Binding ; Solvents ; Thermodynamics ; Viral Vaccines/immunology
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Contributed Indexing:
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Keywords: COVID-19; Epitope identification; Interactions with MHCs
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Substance Nomenclature:
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0 (COVID-19 Vaccines)
0 (Coronavirus Envelope Proteins)
0 (Epitopes, B-Lymphocyte)
0 (Epitopes, T-Lymphocyte)
0 (Solvents)
0 (Viral Vaccines)
0 (envelope protein, SARS-CoV-2)
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Entry Date(s):
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Date Created: 20210101 Date Completed: 20210223 Latest Revision: 20210223
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Update Code:
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20240105
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PubMed Central ID:
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PMC7833863
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DOI:
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10.1016/j.ijbiomac.2020.12.192
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PMID:
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33385461
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COVID-19 is one of the fatal pandemic throughout the world. For cellular fusion, its antigenic peptides are presented by major histocompatibility complex (MHC) in humans. Therefore, exploration into residual interaction details of CoV2 with MHCs shall be a promising point for instigating the vaccine development. Envelope (E) protein, the smallest outer surface protein from SARS-CoV2 genome was found to possess the highest antigenicity and is therefore used to identify B-cell and T-cell epitopes. Four novel mutations (T55S, V56F, E69R and G70del) were observed in E-protein of SARS-CoV2 after evolutionary analysis. It showed a coil➔helix transition in the protein conformation. Antigenic variability of the epitopes was also checked to explore the novel mutations in the epitope region. It was found that the interactions were more when SARS-CoV2 E-protein interacted with MHC-I than with MHC-II through several ionic and H-bonds. Tyr42 and Tyr57 played a predominant role upon interaction with MHC-I. The higher ΔG values with lesser dissociation constant values also affirm the stronger and spontaneous interaction by SARS-CoV2 proteins with MHCs. On comparison with the consensus E-protein, SARS-CoV2 E-protein showed stronger interaction with the MHCs with lesser solvent accessibility. E-protein can therefore be targeted as a potential vaccine target against SARS-CoV2.
Competing Interests: Declaration of competing interest None.
(Copyright © 2020 Elsevier B.V. All rights reserved.)
