María Gasset

Phospholipid‑bound docosahexaenoic acid (PL‑DHA) has been proposed to enhance DHA bioavailability, yet its role in food allergy remains insufficiently defined. In this study, we investigated the protective effects of PL‑DHA in a wheat protein-induced food allergy model in BALB/c mice and examined associated immune‑metabolic mechanisms. PL‑DHA supplementation reduced allergic symptom scores, lowered serum IgE levels, and mitigated jejunum injury. It also attenuated Th2‑skewed immunity, evidenced by decreased IL‑4, IL‑13, and GATA3 expression. Besides, PL‑DHA increased FOXP3 and IL‑10, reduced RORγt and IL‑17A, and improved Foxp3/Rorc and Il10/Il17a ratios, indicating restoration of Treg/Th17 balance and broader enhancement of intestinal immune tolerance. These immunological changes were accompanied by elevated PPARγ expression and increased levels of fatty acid oxidation–related proteins, including CPT1A and ACOX1. Molecular simulation and proteomic analyses further supported PL‑DHA–mediated PPARγ‑linked metabolic regulation. Collectively, these findings identify PL‑DHA as a promising dietary lipid candidate for food allergy intervention.

Seaweed farming is widely promoted for climate change mitigation ^1,2 , yet its potential unintended consequences on the stratospheric ozone layer via emissions of ozone-depleting short-lived halogens ^3,4 is seldom acknowledged and remains unquantified. Applying newly developed observations-based seaweed-farming emission scenarios to a state-of-the-art Earth system model ⁵ , reveals substantial global ozone depletion and increased surface shortwave radiation in the latter half of this century. Expansion of seaweed farming is projected to lead to Antarctic ozone declining below the historical minimum by the 2060s under 20% annual growth and by the 2090s under 12% annual growth, while a business-as-usual 6% annual growth would still substantially slow down ozone recovery. These findings serve as a warning that seaweed farming at scales proposed for global sustainability targets could pose a serious unintended risk to the ozone layer.

The protein parvalbumin (PRV)-beta (PRVB) is the primary cause of 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 predominantly found in Southeast Asia. In this study, we characterized the Hilsa PRV utilizing various proteomic approaches in response to two major riverine habitats and developmental stages. Unique peptide sets corresponding to three PRV isoforms were identified in Hilsa muscle tissues. Label-free quantitative proteomic analysis coupled with ELISA revealed higher levels of PRVB in young fish compared to adults, 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 PRVs for further investigation on the food safety and quality evaluation of Hilsa fish.

Introduction: Fish β-parvalbumins are common targets of allergy-causing immunity. The nature of antibody responses to such allergens determines the biological outcome following exposure to fish. Specific epitopes on these allergens recognised by antibodies are incompletely characterised.Methods: High-content peptide microarrays offer a solution to the identification of linear epitopes recognised by antibodies. We characterized IgG and IgG4 recognition of linear epitopes of fish β-parvalbumins defined in the WHO/IUIS allergen database as such responses hold the potential to counter an allergic reaction to these allergens. Peripheral blood samples, collected over three years, of 15 atopic but not fish-allergic subjects were investigated using a microarray platform that carried every possible 16-mer peptide of known isoforms and isoallergens of these and other allergens.Results: Interindividual differences in epitope recognition patterns were observed. In contrast, reactivity patterns in a given individual were by comparison more stable during the 3 years-course of the study. Nevertheless, evidence of the induction of novel specificities over time was identified across multiple regions of the allergens. Particularly reactive epitopes were identified in the D helix of Cyp c 1 and in the C-terminus of Gad c 1 and Gad m 1.02. Residues important for the recognition of certain linear epitopes were identified. Patterns of differential recognition of isoallergens were observed in some subjects.Conclusions: Altogether, comprehensive analysis of antibody recognition of linear epitopes of multiple allergens enables characterisation of the nature of the antibody responses targeting this important set of food allergens.

The RNA binding protein TDP-43 forms cytoplasmic inclusions via its C-terminal prion-like domain in several neurodegenerative diseases. Aberrant TDP-43 aggregation arises upon phase de-mixing and transitions from liquid to solid states, following still unknown structural conversions which are primed by oxidative stress and chaperone inhibition. Despite the well-established protective roles for molecular chaperones against protein aggregation pathologies, knowledge on the determinants of chaperone recognition in disease-related prions is scarce. Here we show that chaperones and co-chaperones primarily recognize the structured elements in TDP-43´s prion-like domain. Significantly, while HSP70 and HSP90 chaperones promote TDP-43 phase separation, co-chaperones from the three classes of the large human HSP40 family (namely DNAJA2, DNAJB1, DNAJB4 and DNAJC7) show strikingly different effects on TDP-43 de-mixing. Dismantling of the second helical element in TDP-43 prion-like domain by methionine sulfoxidation impacts phase separation and amyloid formation, abrogates chaperone recognition and alters phosphorylation by casein kinase-1δ. Our results show that metamorphism in the post-translationally modified TDP-43 prion-like domain encodes determinants that command mechanisms with major relevance in disease.

Development of efficient peptide-based immunotherapy for shrimp allergy relies on the identification of the dominant T-cell epitopes of its major allergen, tropomyosin. In this study, immunoinformatic tools, T-cell proliferation, cytokine release, IgG/IgE binding, and degranulation assays were used to identify and characterize the T-cell epitopes in Lit v 1 in comparison with previously validated B-cell epitopes. The results showed that of the six in silico predicted T-cell epitopes only one (T2: VQESLLKANIQLVEK, 60–74) promoted T-cell proliferation, the release of IL-2, and upregulated secretion of Th2-associated cytokines in the absence of IgG/IgE binding and degranulation activities. These findings support T2 as a candidate for the development of an efficient peptide-based vaccine for the immunotherapy for shrimp-allergic patients.