ArticleFrontiers in microbiology2022
Proteome-Wide and Protein-Specific Multi-Epitope Vaccine Constructs Against the Rift Valley Fever Virus Outbreak Using Integrated Omics Approaches.
Article in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 8 citations in OpenAlex.
- Immunoinformatics-guided design of a multi-epitope vaccine targeting the envelopment polyprotein of oropouche virus.Molecular genetics and genomics : MGG · 2026Article
- Multi-Epitope mRNA Vaccine TargetingBioinformatics and biology insights · 2026Article
- Immunoinformatics-driven design of multi-epitope vaccine targeting antibiotic-resistant Salmonella typhimurium.PloS one · 2026Article
- Subtractive proteomic analysis to identify highly antigenic proteins and reverse vaccinology based novel vaccine development against Haemophillius parainfluenzae.Scientific reports · 2025Article
- Proteomics-based vaccine targets annotation and design of multi-epitope vaccine against antibiotic-resistant Streptococcus gallolyticus.Scientific reports · 2024Article
- Rapid and simultaneous multiepitope antigen-based detection ofFrontiers in microbiology · 2024Article
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1 author at 1 institution in 1 country.
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Abstract
Rift Valley fever (RVF) is a viral disease caused by a member of the Bunyavirales family causing severe infections in humans. The RVF virus is an enveloped, negative-sense, single-stranded RNA virus that can infect both animals and humans. The symptoms associated with these infections span from minor (fever and headaches) to severe (meningoencephalitis and hemorrhagic fever syndrome) symptoms. Despite the outbreaks of the RVF virus being reported in different parts of the world, no effective therapy is available. Herein, the development of an efficient vaccine is critical for the control of infections associated with the RVF virus. Moreover, computational vaccine approaches are helpful in the design of specific, safe, and stable peptide-based designs when compared to the conventional methods of vaccine development. In this study, the whole proteome of the virus, comprising four proteins (NP, L, GP, and NSP), was screened to find putative vaccine epitope sequences (T cell, B cell, and HTL) specific for each protein. These shortlisted epitopes were then combined with flexible linkers to design protein-specific and proteome-wide immunogenic multi-epitope-based vaccine constructs. The results revealed that these multi-epitope vaccine constructs (MEVCs) are strongly antigenic and non-allergenic in nature. The efficacy of these constructs was further validated by docking with immune receptors, which revealed strong binding interactions with human TLR8. Using the MD simulation approach, the binding stability and residual flexibility of the best vaccine construct (proteome-wide) were confirmed, which revealed stable dynamic and favorable features. Furthermore,
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