α-Gal present on both glycolipids and glycoproteins contributes to immune response in meat-allergic patients
Abstract
BACKGROUND: The α-Gal syndrome is associated with the presence of IgE directed to the carbohydrate galactose-α-1,3-galactose (α-Gal) and is characterized by a delayed allergic reaction occurring 2 to 6 hours after ingestion of mammalian meat. On the basis of their slow digestion and processing kinetics, α-Gal-carrying glycolipids have been proposed as the main trigger of the delayed reaction. OBJECTIVE: We analyzed and compared the in vitro allergenicity of α-Gal-carrying glycoproteins and glycolipids from natural food sources. METHODS: Proteins and lipids were extracted from pork kidney (PK), beef, and chicken. Glycolipids were purified from rabbit erythrocytes. The presence of α-Gal and IgE binding of α-Gal-allergic patient sera (n = 39) was assessed by thin-layer chromatography as well as by direct and inhibition enzyme-linked immunosorbent assay. The in vitro allergenicity of glycoproteins and glycolipids from different meat extracts was determined by basophil activation test. Glycoprotein stability was evaluated by simulated gastric and intestinal digestion assays. RESULTS: α-Gal was detected on glycolipids of PK and beef. Patient IgE antibodies recognized α-Gal bound to glycoproteins and glycolipids, although binding to glycoproteins was more potent. Rabbit glycolipids were able to strongly activate patient basophils, whereas lipid extracts from PK and beef were also found to trigger basophil activation, but at a lower capacity compared to the respective protein extracts. Simulated gastric digestion assays of PK showed a high stability of α-Gal-carrying proteins in PK. CONCLUSION: Both α-Gal-carrying glycoproteins and glycolipids are able to strongly activate patient basophils. In PK and beef, α-Gal epitopes seem to be less abundant on glycolipids than on glycoproteins, suggesting a major role of glycoproteins in delayed anaphylaxis upon consumption of these food sources.
Related
- Quantitative Model of the Ocular Immune Response during Seasonal Allergic Conjunctivitis
- Cross-allergenicity of peanut and lupine: The risk of lupine allergy in patients allergic to peanuts
- Cell heterogeneity contributes to the variable response of HIV-1 to latency-reversing agents
- Cooperation between Adh and OR5M11 contributes to the lung pathogenicity of Actinobacillus pleuropneumoniae by facilitating the NLRP3-mediated inflammatory response
- Association of Score for Allergic Rhinitis with Serum Total IgE and Clinical Characteristics in Patients with Allergic Rhinitis
BibTeX
@article{chakrapani2026αgal,
title = {{α-Gal present on both glycolipids and glycoproteins contributes to immune response in meat-allergic patients}},
author = {Neera Chakrapani and Jörg Fischer and Kyra Swiontek and Françoise Codreanu-Morel and Farah Hannachi and Martine Morisset and Clément Mugemana and Dmitry Bulaev and Simon Blank and Carsten Bindslev-Jensen and Tilo Biedermann and Markus Ollert and Christiane Hilger},
journal = {Journal of Allergy and Clinical Immunology},
year = {2026},
month = oct,
doi = {10.1016/j.jaci.2022.02.030},
url = {https://hal.science/hal-05779957v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - α-Gal present on both glycolipids and glycoproteins contributes to immune response in meat-allergic patients
AU - Neera Chakrapani
AU - Jörg Fischer
AU - Kyra Swiontek
AU - Françoise Codreanu-Morel
AU - Farah Hannachi
AU - Martine Morisset
AU - Clément Mugemana
AU - Dmitry Bulaev
AU - Simon Blank
AU - Carsten Bindslev-Jensen
AU - Tilo Biedermann
AU - Markus Ollert
AU - Christiane Hilger
PY - 2026
DA - 2026/10/06
JO - Journal of Allergy and Clinical Immunology
DO - 10.1016/j.jaci.2022.02.030
UR - https://hal.science/hal-05779957v1
AB - BACKGROUND: The α-Gal syndrome is associated with the presence of IgE directed to the carbohydrate galactose-α-1,3-galactose (α-Gal) and is characterized by a delayed allergic reaction occurring 2 to 6 hours after ingestion of mammalian meat. On the basis of their slow digestion and processing kinetics, α-Gal-carrying glycolipids have been proposed as the main trigger of the delayed reaction. OBJECTIVE: We analyzed and compared the in vitro allergenicity of α-Gal-carrying glycoproteins and glycolipids from natural food sources. METHODS: Proteins and lipids were extracted from pork kidney (PK), beef, and chicken. Glycolipids were purified from rabbit erythrocytes. The presence of α-Gal and IgE binding of α-Gal-allergic patient sera (n = 39) was assessed by thin-layer chromatography as well as by direct and inhibition enzyme-linked immunosorbent assay. The in vitro allergenicity of glycoproteins and glycolipids from different meat extracts was determined by basophil activation test. Glycoprotein stability was evaluated by simulated gastric and intestinal digestion assays. RESULTS: α-Gal was detected on glycolipids of PK and beef. Patient IgE antibodies recognized α-Gal bound to glycoproteins and glycolipids, although binding to glycoproteins was more potent. Rabbit glycolipids were able to strongly activate patient basophils, whereas lipid extracts from PK and beef were also found to trigger basophil activation, but at a lower capacity compared to the respective protein extracts. Simulated gastric digestion assays of PK showed a high stability of α-Gal-carrying proteins in PK. CONCLUSION: Both α-Gal-carrying glycoproteins and glycolipids are able to strongly activate patient basophils. In PK and beef, α-Gal epitopes seem to be less abundant on glycolipids than on glycoproteins, suggesting a major role of glycoproteins in delayed anaphylaxis upon consumption of these food sources.
SN - 0091-6749
ER -