Proteomic characterization of cellular responses to the fish allergen β-parvalbumin using ZenoSWATH-MS.

β-Parvalbumin (β-PRVB) is a calcium-binding protein and the major allergenic macromolecule responsible for most IgE-mediated fish allergy reactions. Despite its clinical relevance, the molecular mechanisms underlying interactions between β-PRVB and host cellular systems remain incompletely understood. In this study, high-resolution quantitative proteomics using data-independent acquisition ZenoSWATH-MS was applied to investigate cellular responses associated with exposure to β-PRVB in a controlled experimental model. Proteomic profiling of sensitized splenocytes following ex vivo stimulation with β-PRVB quantified 4784 proteins and identified 324 differentially regulated proteins. Functional enrichment analysis linked these changes to antigen processing and immune signaling pathways. Notably, β-PRVB exposure was associated with coordinated upregulation of immunoproteasome subunits together with components of the JAK/STAT and Notch signaling pathways. These results indicate that β-PRVB modulates intracellular protein networks involved in antigen processing and immune activation. This proteomic characterization provides molecular insight into the biological activity of the fish allergen β-parvalbumin and highlights cellular pathways associated with its allergenic potential.