Project description:Food allergy is an immune-mediated condition caused by hypersensitivity to food allergens, with fish allergens, particularly beta-parvalbumins (beta-PRVBs), being the most significant. While the only effective treatment is avoidance of the food allergen, the intracellular mechanisms of immune activation during allergen exposure are not well understood.
This study aimed to investigate critical insights into immune cell activation in a newly proposed beta-PRVB-induced fish allergy model, with a particular focus on to explore the proteomic phenotype of splenocytes and T cell activation in response to the allergen.
To establish a robust allergic response, mice were sensitized to beta-PRVB using aluminium hydroxide, a Th2-skewing adjuvant, (intraperitoneal injection) and subsequently challenged orally with beta-PRVB . This carefully designed protocol was designed to induce a Th2-type immune response, which was confirmed by detecting allergen-specific antibodies and cytokines. For proteomic analysis of the immune response, high-resolution quantitative proteomics data were generated using an advanced DIA-based ZenoSWATH-MS technology.
Project description:PCR array analysis was performed to investigate the expression of genes in the ear tissues of Ni allergy-induced miceand control mice. Ni model mouse n=3, control mouse n=3
Project description:PCR array analysis was performed to investigate the expression of genes in the ear tissues of Ni allergy-induced miceand control mice.
Project description:Comparison of gene expression profiles between pediatric patients with and without symptoms of cross-allergy (birch-apple syndrome).
Project description:The protein parvalbumin (PRV)-beta (PRVB) is the primary cause behind food allergies to bony fish. Although PRVB is a well-characterized protein in many bony fishes, little is known about the hilsa, an anadromous fish with great economic importance and mostly found in Southeast Asia. In this study, we have characterized the hilsa PRV utilizing various proteomic approaches in response to two major riverine habitats and developmental stages. Unique peptide sets correspond to three different PRV isoforms were identified in hilsa muscle tissues. Label-free quantitative proteomic analysis coupled with ELISA revealed higher levels of PRVB in young fish comparative to the adult, irrespective of their riverine habitats. A comparative quantitative analysis of PRVB further demonstrated that hilsa had less PRVB than other commonly consumed freshwater fish species. Multiple reaction monitoring (MRM)-based targeted proteomic approach showed the potential of PRV as a marker protein for allergen quantitation and authenticating the presence of hilsa in a complex freshwater fish mixture. Our findings collectively offer fundamental knowledge on hilsa parvalbumins for further investigation on the food safety and quality evaluation of hilsa fish.
Project description:Cutaneous exposure to food antigen through impaired skin barrier has been shown to induce epicutaneous sensitization, and thereby cause IgE-mediated food allergy. We examined whether skin barrier impairment deteriorated food allergy symptoms in epicutaneously sensitized mice. To clarify the association between skin inflammation and food allergy symptoms, we analyzed gene expression at skin lesions using a GeneChip.