Background: Seed storage proteins (SSP; Ara h 1, Ara h 2, Ara h 3) have been shown to be major peanut allergens, although recently, peanut lipid transfer protein has been reported to be an important allergen in the Mediterranean area. We sought to investigate the sensitization pattern to peanut SSP and vegetable pan-allergens in a group of peanut-allergic children compared with a peanut-tolerant group.
Methods: One hundred and twenty-three children who presented with food allergy were included in the study. Tolerance to peanut ingestion was assessed. Specific IgE was determined by ImmunoCAP, and microarray ISAC was performed. Sensitization frequencies and levels of specific IgE were compared between groups.
Results: Fifty-five of 123 children presented symptoms upon contact or ingestion. Frequency of sensitization to Ara h 1, Ara h 2, and Ara h 3 was 60.0%, 72.7%, and 43.6%, respectively, in the group of allergic children vs. 7.4%, 1.5%, and 7.4% in the group of tolerant children. Levels of specific IgE against Ara h 1, Ara h 2, and Ara h 3 were significantly higher in the allergic group (p < 0.001). The frequency of sensitization and the levels of specific IgE against Cor a 8 (36.4% vs. 16.2%) were significantly higher in the allergic children, whereas no significant differences were found for Pru p 3. No differences were seen for other pan-allergens. Patients sensitized to SSP, regardless of sensitization to nsLTP, were allergic rather than tolerant.
Conclusion: In our population, peanut-allergic children were mainly sensitive to SSP. A few patients were also sensitive to some nsLTPs. No differences were shown in other pan-allergens.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1111/j.1399-3038.2012.01337.x | DOI Listing |
Ecancermedicalscience
November 2024
Internal Medicine Service, Sanatorio Sagrado Corazón, Buenos Aires, CP 1039, Argentina.
Plasmacytoid blast dendritic cell neoplasm is a rare subtype of acute leukaemia that represents less than 1% of haematologic neoplasms. It is characterised by skin involvement and leukaemic dissemination in the rest of the body. The immunophenotype is represented by the expression of CD4, CD56 and CD123.
View Article and Find Full Text PDFJ Allergy Clin Immunol
January 2025
Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN; Department of Pharmacology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN.
Background: Studies of human IgE and its targeted epitopes on allergens have been very limited. We have an established method to immortalize IgE encoding B cells from allergic individuals.
Objective: To develop an unbiased and comprehensive panel of peanut-specific human IgE mAbs to characterize key immunodominant antigenic regions and epitopes on peanut allergens to map the molecular interactions responsible for inducing anaphylaxis.
Food Chem X
January 2025
Key Laboratory of Precision Nutrition and Food Quality, Department of Nutrition and Health, China Agricultural University, Beijing 100083, China.
Egg yolk phospholipids are commercially valuable products that are beneficial to human health. Previous research on phospholipids in egg yolk mainly focuses on phosphatidyl choline (PC), phosphatidyl ethanolamine (PE), and fatty acid compositions, and neglects the esterification position and other bioactive phospholipids. This study found a total of 19 classes of phospholipids and 275 subclasses using lipidomics.
View Article and Find Full Text PDFJ Allergy Clin Immunol
January 2025
Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN; Department of Pharmacology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN. Electronic address:
Background: Human monoclonal IgE antibodies recognizing peanut allergens have recently become available, but we lack a detailed understanding of how these IgEs target allergens.
Objective: To determine the molecular details of the antibody-allergen interaction for a panel of clinically important human IgE monoclonal antibodies and to develop strategies to disrupt disease causing antibody-allergen interactions.
Methods: We identified candidates from a panel of epitope binned human IgE monoclonals that recognize two important and homologous peanut allergens, Ara h 2 and Ara h 6.
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!