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Updated: Jun 13, 2025

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Designing of an innovative conserved multiepitope subunit vaccine targeting SARS-CoV-2 glycoprotein and nucleoprotein
Temitope Isaac Adelusi1,2,3, Abdeen Tunde Ogunlana4, Moyosoluwa Precious Oyewole4
1Computational Biology and Drug Discovery Laboratory, Department of Biochemistry, Ladoke Akintola University of Technology, Ogbomoso, Oyo State, Nigeria. tiadelusi@lautech.edu.ng.
Abstract:
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has imposed substantial challenges on our society due to the COVID-19 pandemic. This virus relies heavily on its surface glycoprotein (S-glycoprotein) to facilitate attachment, fusion, and entry into host cells. While the nucleoprotein (N) in the ribonucleoprotein core binds to the viral RNA genome. Therefore, our objective is to develop a novel vaccine candidate targeting the dominant T-cell and B-cell epitopes of the immune system. On the S-glycoprotein and nucleoprotein. Employing an immunoinformatic approach, we constructed a vaccine candidate with 13 highly antigenic B-cell epitopes, 19 HTL antigenic epitopes, and 18 CTL epitopes following a rigorous assessment. The multi-epitope construct successfully passed three-fold toxicity, allergenicity, and antigenicity tests, affirming its non-toxic, non-allergenic, and antigenic nature. This demonstrates the potentiality of the vaccine design to trigger an immunological response. Furthermore, the vaccine-ACE-2 receptor complex was tested, confirming its ability to interact with ACE-2's core pocket and induce an immunological response. Additionally, the vaccine's binding prowess for human toll-like receptors (TLR) (1, 3, 4, and 8) was investigated. According to the Ramachandran plot, 77.46% of the construct's amino acid residues fall within a favorable zone, establishing it as a viable vaccine candidate.
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