Abstract
Background: The control of the Covid-19 epidemic depends on designing a novel, effec-tive vaccine against it. Currently, available vaccines cannot provide complete protection against various mutants of Covid-19. Objective: The present investigation aimed to design a new multi-epitope vaccine by using in silico tools. Methods: In the present study, the spike-glycoprotein was targeted, desirably stimulating both B and T-cell lymphocytes, providing effective and safe responses in the host immune system. The de-sired vaccine has been found to possess 448 amino acids of spike glycoprotein. The prognosticated epitopes included 10 CTL, 4 linear B-cells, and 14 HTL, including the 128 amino acid sequence of 50S ribosomal protein adjuvant joined by GPGPG and AAY linkers on the N terminus of linear B-cell, HTL, and CTL epitopes, and the C-terminal joined with HHHHHH (6HIS) linker, indicating stability for vaccine structure. Results: The molecular docking has revealed the protein-protein restricting communication between the immunization construct and the TLR-3-resistant receptor. The vaccine has been developed through selected epitopes, an adjuvant, and an additional epitope. Docking assays with toll-like re-ceptor 3 have been run on a three-dimensional structural model of the vaccine to gauge its immuno-logical potency. Our findings support the hypothesis that our vaccination will activate TLR-mediated downstream immune pathways by aggressively interacting with the innate receptor. Conclusion: The results suggest that the proposed chimeric peptide could initiate an efficient and safe immune response against Covid-19. The proposed vaccine has been proven safe in all critical parameters.
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