ArticleIn silico pharmacology2023
Development of conserved multi-epitopes based hybrid vaccine against SARS-CoV-2 variants: an immunoinformatic approach.
Article in In silico pharmacology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 0 citations in OpenAlex.
- Toward a Vaccine Against Multidrug-Resistant Elizabethkingia anophelis: Comprehensive Immunoinformatics-Based Design of a Multi-Epitope Vaccine and mRNA Construct.Probiotics and antimicrobial proteins · 2026Article
- Integrative immunoinformatics and structural modeling for the rational design of a multi-epitope vaccine candidate against human cytomegalovirus.Scientific reports · 2026Article
- A chimeric trivalent Echovirus vaccine designed by loop substitution elicits cross-neutralizing immunity against serotypes 11, 18, and 30.Journal of virology · 2026Article
- From Sequence to Solution: Computational Design of a Multi-Epitope Vaccine Candidate Against Francisella tularensis.Probiotics and antimicrobial proteins · 2026Article
- Development of a Novel Pan-Species Multi-Epitope Vaccine (PS-MEV) Targeting Nine Staphylococcus Species to Combat Antibiotic Resistance.Probiotics and antimicrobial proteins · 2026Article
- Bioinformatics and immunoinformatics approaches in the design of a multi-epitope vaccine targeting CTLA-4 for melanoma treatment.Molecular diversity · 2025Article
- In Silico Development of a Chimeric Multi-Epitope Vaccine TargetingPharmaceuticals (Basel, Switzerland) · 2025Article
- TLR2 Activation as a Marker of Severe COVID-19 and a Potential Therapeutic Target.Current medicinal chemistry · 2025Review
- Immunoinformatics design of a multi-epitope vaccine for Chlamydia trachomatis major outer membrane proteins.Scientific reports · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The world has faced unprecedented disruptions like global quarantine and the COVID-19 pandemic due to SARS-CoV-2. To combat these unsettling situations, several effective vaccines have been developed and are currently being used. However, the emergence of new variants due to the high mutation rate of SARS-CoV-2 challenges the efficacy of existing vaccines and has highlighted the need for novel vaccines that will be effective against various SARS-CoV-2 variants. In this study, we exploited the four structural proteins of SARS-CoV-2 to execute a potential multi-epitope vaccine against SARS-CoV-2 and its variants. The vaccine was designed by utilizing the antigenic, non-toxic, and non-allergenic B-cell and T-cell epitopes, which were selected from conserved regions of viral proteins. To build a vaccine construct, epitopes were connected through different linkers and an adjuvant was also attached at the start of the construct to enhance the immunogenicity and specificity of the epitopes. The vaccine construct was then screened through the aforementioned filters and it scored 0.6019 against the threshold of 0.4 on VexiJen 2.0 which validates its antigenicity. Toll-like receptors (i.e., TLR2, TLR3, TLR4, TLR5, and TLR8) and vaccine construct were docked by Cluspro 2.0, and TLR8 showed strong interaction with construct having a maximum negative binding energy of - 1577.1 kCal/mole. C-IMMSIM's immune simulations over three doses of the vaccine and iMODS' molecular dynamic simulations were executed to assess the reliability of the docked complexes. The stability of the vaccine construct was evaluated through the physicochemical analyses and the findings suggested that the manufactured vaccine is stable under a wide range of circumstances and can trigger immune responses against various SARS-CoV-2 variants (due to conserved epitopes). However, to strengthen the formulation of the vaccine and assess its safety and effectiveness, additional investigations and studies are required to support the computational data of this research at Supplementary Information: The online version contains supplementary material available at 10.1007/s40203-023-00156-2.
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