Computational identification of conserved B- and T-cell epitopes for multi-epitope peptide vaccine design against bovine leukemia virus
Virus Genes, 2026 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Basım Tarihi: 2026
- Doi Numarası: 10.1007/s11262-026-02279-y
- Dergi Adı: Virus Genes
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Chemical Abstracts Core, EMBASE, MEDLINE, Natural Science Collection (ProQuest), Biological Science Database (ProQuest), Biomedical Reference Collection: Corporate Edition (EBSCO), Health Research Premium Collection (ProQuest), Pharma Collection (ProQuest)
- Anahtar Kelimeler: Bovine leukemia virus, Immunoinformatics, Multi-epitope peptide vaccine, Multiple sequence alignment, Reverse vaccinology
- Yozgat Bozok Üniversitesi Adresli: Evet
Özet
Bovine leukosis continues to impose significant economic losses on the global cattle industry due to its persistent infection and widespread prevalence worldwide. Although control strategies such as test-and-cull programs have been implemented in some countries, an effective and safe vaccine remains unavailable. In this study, an immunoinformatics-based approach combined with reverse vaccinology was applied to design a multi-epitope peptide (MEP) vaccine candidate against Bovine leukemia virus (BLV). Conserved protein regions were analyzed to identify potential immune targets, resulting in the selection of five epitopes, including three cytotoxic T-lymphocyte (CTL) epitopes, one helper T-lymphocyte (Th) epitope, and one linear B-cell epitope derived from the highly conserved BLV Gag and RT-IN proteins. These epitopes were assembled using AAY and GPGPG linkers to generate a 67-amino-acid MEP construct. In silico evaluation indicated that the designed construct possesses favorable immunological properties, including high predicted antigenicity (VaxiJen score: 0.6511, which is notably higher than the baseline score of 0.4784 for the native viral proteins; Pr44: 0.4784, RT-IN: 0.4214), non-allergenic characteristics, and absence of predicted toxic motifs. Homology analysis against the Bos taurus proteome revealed no significant similarity, suggesting a low risk of host cross-reactivity. Structural analyses using PSIPRED and AlphaFold 3 predicted localized secondary structural elements within an overall flexible peptide architecture; this flexibility is highly advantageous for optimal proteasomal cleavage, efficient antigen processing, and MHC presentation. Taken together, these findings provide a rational framework for the development of a BLV MEP vaccine candidate and support further experimental validation to evaluate its predicted immunogenic potential.