This study aimed to screen for mimotopes for the peanut allergen Ara h 5 using a phage display random heptapeptide library. Recombinant Ara h 5, obtained via a prokaryotic expression system, was used as an immunogen to generate antibodies in a mouse model. Polyclonal IgE antibodies against Ara h 5 were purified from the antiserum by affinity chromatography. Using these Ara h 5 IgE antibodies as the target, three rounds of biopanning were performed against the phage display heptapeptide library. Positive phage clones were isolated and sequenced. Three mimotope sequences, FHWWYLK, WETIYSR, and GPLWNVN, were identified. These mimotopes provide an important foundation for the development of blocking antibodies or epitope-specific immunotherapy for peanut allergy.

Food allergies are increasingly prevalent worldwide, yet the underlying immunometabolic mechanisms remain incompletely elucidated. Lactylation, as an emerging post-translational modification, has recently been identified as a critical regulator of immunometabolic reprogramming and inflammatory responses in allergic diseases. This review synthesizes current evidence on the role of lactylation in modulating immune cell dynamics, including macrophage polarization, dendritic cell antigen presentation, T-cell differentiation, mast cell activation, and neutrophil function. By systematically integrating lactate metabolism with lactylation-mediated epigenetic regulation, this review highlights their central role in shaping allergic inflammation, thereby linking metabolism to immune regulation in food allergies. Despite the research progress, challenges remain in understanding the transient nature of lactylation and tissue-specific dynamics. Future research should combine spatial omics, lactylation-specific imaging, and physiologically relevant models to clarify its spatiotemporal regulation. Meanwhile, dietary strategies, microbiota-based interventions, and pharmacological regulation may provide practical approaches for modulating lactate metabolism and lactylation.

In recent years, the incidence of food allergy has continued to rise globally. Food allergy has become a global food safety and public health problem. Currently, avoiding allergens is the best way to deal with food allergy, and food allergen labeling plays an important role in protecting allergic consumers. This paper reviews recent progress in food allergen risk assessment from the perspectives of the establishment of the food allergens list, the soring-out and utilization of national nutrition and diet survey results, and the population threshold for food allergens. Furthermore, the problems existing in China’s food allergen management are discussed. It is expected that this review will provide information for scientific research and a theoretical reference to strengthen the management of food allergens.

Diarrhea has become the leading cause of illness and death among infants and young children in developing countries. Clinically, patients with diarrhea showed damaged intestinal epithelial villi, usually accompanied by lactase def iciency. In this study, we evaluated the therapeutic effects of lactose-free milk powder on rats and children with diarrhea. Antibiotic-associated diarrhea (AAD) model was established by gavage with antibiotic mixture in SD rats, followed by administration of milk powder containing lactose or not. The results showed that lactose-free milk powder ameliorated AAD-related diarrhea symptoms, and accelerated the recovery from diarrhea. And 16S sequencing results indicated lactose-free milk powder contributed to increase the α- and β-diversity of intestinal f lora, and restore the intestinal microbiota disorder. In conclusion, our data demonstrate that lactose-free milk powder could alleviate diarrhea by restoring gut microbiota and intestinal barrier function.

The precise mechanism underlying the effects of anti-CD4 antibody and calcium ions (Ca²⁺) in peanut allergy remains unknown. C3H/HeJ mice sensitized with peanut protein extract (PPE) were injected with anti-CD4 antibodies for 4 weeks. Stimulation with PPE increased the specific immunoglobulin (IgE), cytokine, histamine, and mMcp-1 levels, upregulated decorin (Dcn) expression, induced Ca²⁺ inflow in the spleen, and augmented the expression of the transcription factors GATA-3 and Foxp3, which resulted in Th2 and Treg cell activation. Notably, the Ca²⁺ levels were positively correlated with the histamine, interleukin (IL)-4, IL-5, and IL-13 levels, and negatively correlated with IL-10 levels. However, administration of anti-CD4 antibodies markedly alleviated allergic symptoms, activated T cells, and reduced Ca²⁺ inflow, cytokine, histamine, mMcp-1, and the IgHG3, CXCL12, MMP2 and FABP4 gene. Our results indicated that anti-CD4 antibodies can ameliorate PPE-induced allergy, which is probably related to the suppression of Ca²⁺ inflow, and inhibiting histamine, cytokine and IgHG3, CXCL12, MMP2, and FABP4, thus exerting a protective effect against PPE-sensitized food allergy.

Quail egg ovomucoid can inhibit activation of basophils and eosinophils, while hen egg ovomucoid has been shown to be a major allergen, named Gal d 1. At present, the differences in structure and function between two ovomucoid are unclear. We found the homology of ovomucoid in quail eggs and hen eggs reached 77%. Compared with hen egg ovomucoid, the distribution of secondary structure was different in AA52−53, AA57−58, AA66−68, AA71−72, AA131−133, AA139−140, AA157−159 and AA184−185. Among 9 epitopes of egg ovomucoid, there were different amino acids from quail egg ovomucoid in 8 epitopes. Recombination quail egg ovomucoid had trypsin inhibition activity and quail egg ovomucoid didn't specifically bind to serum of eggs allergic patients. Quail egg ovomucoid can significantly inhibit RBL-2H3 cells degranulation and protect cells morphology to a certain extent, indicating quail egg ovomucoid can inhibit cells activation and have potential anti-allergic effects, which is related to trypsin inhibitory activity. The difference in sensitization compare to hen egg ovomucoid may be due to amino acids differences affecting protein structure by changing antigenic epitopes.