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Food allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Ara h 3 is a glycinin seed storage protein (i.e., a globulin) with a molecular weight of 60 kDa and is highly homologous with Ara h 4 (now renamed to Ara h 3.02, an isoallergen of Ara h 3). Approximately 45% of patients with peanut allergy have specific IgE to this allergen [17]. Ara h 9 is a nonspecific lipid transfer protein (LTP) that is 9.8 kDa and is an α-helical folded protein. Ara h 9 is a major allergen in Mediterranean areas [39], whereas its relevance in other populations is likely minor. Ara h 5, a profilin, and Ara h 8 [40], a Bet v 1 homologue, are considered pan-allergens and cross-react with environmental allergens. These proteins can lead to pollen–food allergy syndrome upon ingestion but are easily digested and unlikely to cause systemic allergic symptoms. Altogether, 17 allergens are identified (Ara h 1 to Ara h 17) with Ara h 1, 2, 3, and 6 considered to be the most common allergens in most studies.
Lactic Acid Bacteria Application to Decrease Food Allergies
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Vanessa Biscola, Marcela Albuquerque Cavalcanti de Albuquerque, Tatiana Pacheco Nunes, Antonio Diogo Silva Vieira, Bernadette Dora Gombossy de Melo Franco
Regarding the implicated antigens, the pattern of sensitization to peanut proteins varies among populations in different geographical regions. The three main elicitors of allergic reactions in the U.S. are Ara h 1, Ara h 2, and Ara h 3. In Spain, Ara h 9 is the most antigenic protein, while for Swedish patients Ara h 8 has the highest sensitization rates (Vereda et al. 2011, Ballmer-Weber et al. 2015).
Allergic Diseases
Published in Stephan Strobel, Lewis Spitz, Stephen D. Marks, Great Ormond Street Handbook of Paediatrics, 2019
Adam Fox, George Du Toit, Stephan Strobel
These specialised diagnostic tests measure IgE responses to specific ‘components’ of the allergen: for example, peanut allergen components can be measured to Ara h1, Ara h2, Ara h3, Ara h8, Ara h9. Specific components may be associated with different clinical expressions and may be becoming helpful in certain clinical scenarios, such as distinguishing allergic sensitisation from clinical allergy and identifying food-allergic patients at risk of more severe reactions (e.g. Ara h2 in peanut allergy and ovomucoid in egg allergy have been associated with more severe reactions).
Current Trend in Immunotherapy for Peanut Allergy
Published in International Reviews of Immunology, 2018
Chong Joo Chan, Timmy Richardo, Renee Lay Hong Lim
A total of 17 peanut allergens has been identified and recognised by the WHO/IUIS Allergen Nomenclature Sub-committee. They were characterised based on their biological function and placed in protein superfamilies such as the Cupin, Prolamin, Bet v-1 like, Profilin Glycosyl transferase GT-C, Scorpion toxin-like knottin and the recently reported lipid transfer proteins as shown in Table 2.60 Among these allergens, Ara h 1, Ara h 2 and Ara h 3 are classified as the major peanut allergens due to their ability to recognise IgE in more than 50% of peanut-allergic patients.61 Ara h 6 was reported to exhibit similar allergenic potential and activity as Ara h 2.62