ArticlePoultry science2026
Development and evaluation of a multi-epitope subunit vaccine against Salmonella Enteritidis infection.
Article in Poultry science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salmonella Enteritidis (S. Enteritidis) is a major pathogen causing foodborne diseases worldwide, posing a serious threat to public health security and the sustainable development of the poultry industry. To overcome the limitations of conventional vaccines in terms of efficacy, safety, and cross-protection, a novel multi-epitope subunit vaccine (SEMV) was designed and constructed using an immunoinformatics-based strategy. Through systematic screening of epitopes from key immunogenic proteins of S. Enteritidis (SseB, SipC, OmpD and TolC), a total of 8 B-cell epitopes, 4 MHC-I-restricted epitopes, and 8 MHC-II-restricted epitopes were identified. These epitopes were linked together with optimized linkers and an adjuvant to produce the recombinant SEMV protein. Bioinformatic evaluation confirmed that the vaccine candidate exhibited favorable antigenicity, non-allergenicity, and structural stability. Molecular docking analysis showed that SEMV formed a stable complex with TLR15, with a docking score of -479.08, a confidence score of 0.9986, and an MM/GBSA binding free energy of ‑36.34 kcal/mol. Molecular dynamics simulation further demonstrated that the complex reached equilibrium after 95 ns (RMSD ≈ 0.8 nm), maintained an average of approximately six hydrogen bonds, and exhibited an MM/PBSA binding free energy of ‑25.94 kcal/mol; key residues such as B:ILE258, A:PRO706, and A:GLU740 played critical roles in binding. In chicken immunization and challenge experiments, SEMV induced high levels of specific antibodies and cellular immune responses, significantly reduced bacterial loads in visceral organs, and alleviated histopathological damage. The vaccine demonstrated reliable immune protective efficacy against both homologous and heterologous Salmonella challenges. Collectively, these findings indicate that SEMV is a highly promising multi-epitope subunit vaccine candidate against Salmonella, laying an important foundation for subsequent preclinical and clinical studies.
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