is a pathogen that causes infections in various parts of the body, with high mortality rates reported in antibiotic-resistant cases. Treating at-risk individuals requires crucial vaccination efforts due to the challenges that exist. This research involved designing a multi-epitope vaccine from 's fimbriae antigens. Optimal T-cell and B-cell epitopes were chosen through studies including epitope-HLAs molecular docking. The multi-epitope was created, featuring antigenic T- and B-cell epitopes, β-defensin as an adjuvant, the PADRE sequence to boost immunogenicity and well-suited linkers. The tertiary structure of the multi-epitope was achieved through modeling and molecular dynamics-based refinements. The construct underwent scrutiny for structural traits, physicochemical properties, conformational B epitope prediction, immune responses simulation, cloning, molecular docking for assay binding to toll-like receptors (TLRs), and deformability studies. The outcomes indicated the vaccine candidate's positive attributes, encompassing immunogenicity, structure, physicochemical properties, solubility, TLR binding, toxicity, stability, allergenicity, and cross-reactivity. The multi-epitope vaccine candidate exhibits the potential for provoking diverse immune responses against . Nevertheless, additional and experimental tests are necessary to substantiate its efficacy.

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http://dx.doi.org/10.1080/07391102.2025.2472407DOI Listing

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