SCOPE: Prawn allergy is one of the leading causes of IgE-mediated hypersensitivity to food. Alterations of IgE-antibody reactivity to prawn allergens due to thermal processing are not fully understood. The aim of this study was to analyze the impact of heating on prawn allergens using a comprehensive allergenomic approach. METHODS AND RESULTS: Proteins from raw and heat-processed black tiger prawn (Penaeus monodon) extracts as well as recombinant tropomyosin (rPen m1) were analyzed by SDS-PAGE and immunoblotting using sera from 16 shellfish allergic patients. IgE antibody binding proteins were identified by advanced mass spectroscopy, characterized by molecular structure analysis and their IgE reactivity compared among the prepared black tiger prawn extracts. Heat processing enhanced the overall patient IgE binding to prawn extracts and increased recognition of a number of allergen variants and fragments of prawn allergens. Allergens identified were tropomyosin, myosin light chain, sarcoplasmic calcium binding protein, and putative novel allergens including triose phosphate isomerase, aldolase, and titin. CONCLUSION: Seven allergenic proteins are present in prawns, which are mostly heat-stable and form dimers or oligomers. Thermal treatment enhanced antibody reactivity to prawn allergens as well as fragments and should be considered in the diagnosis of prawn allergy and detection of crustacean allergens in processed food.
SCOPE: Prawn allergy is one of the leading causes of IgE-mediated hypersensitivity to food. Alterations of IgE-antibody reactivity to prawn allergens due to thermal processing are not fully understood. The aim of this study was to analyze the impact of heating on prawn allergens using a comprehensive allergenomic approach. METHODS AND RESULTS: Proteins from raw and heat-processed black tiger prawn (Penaeus monodon) extracts as well as recombinant tropomyosin (rPen m1) were analyzed by SDS-PAGE and immunoblotting using sera from 16 shellfish allergicpatients. IgE antibody binding proteins were identified by advanced mass spectroscopy, characterized by molecular structure analysis and their IgE reactivity compared among the prepared black tiger prawn extracts. Heat processing enhanced the overall patient IgE binding to prawn extracts and increased recognition of a number of allergen variants and fragments of prawn allergens. Allergens identified were tropomyosin, myosin light chain, sarcoplasmic calcium binding protein, and putative novel allergens including triose phosphate isomerase, aldolase, and titin. CONCLUSION: Seven allergenic proteins are present in prawns, which are mostly heat-stable and form dimers or oligomers. Thermal treatment enhanced antibody reactivity to prawn allergens as well as fragments and should be considered in the diagnosis of prawn allergy and detection of crustacean allergens in processed food.
Authors: Nagib Ahsan; R Shyama Prasad Rao; Philip A Gruppuso; Bharat Ramratnam; Arthur R Salomon Journal: J Proteomics Date: 2016-04-22 Impact factor: 4.044
Authors: Joana Costa; Caterina Villa; Kitty Verhoeckx; Tanja Cirkovic-Velickovic; Denise Schrama; Paola Roncada; Pedro M Rodrigues; Cristian Piras; Laura Martín-Pedraza; Linda Monaci; Elena Molina; Gabriel Mazzucchelli; Isabel Mafra; Roberta Lupi; Daniel Lozano-Ojalvo; Colette Larré; Julia Klueber; Eva Gelencser; Cristina Bueno-Diaz; Araceli Diaz-Perales; Sara Benedé; Simona Lucia Bavaro; Annette Kuehn; Karin Hoffmann-Sommergruber; Thomas Holzhauser Journal: Clin Rev Allergy Immunol Date: 2021-01-07 Impact factor: 8.667
Authors: Jennifer M Rolland; Nirupama P Varese; Jodie B Abramovitch; Jessica Anania; Roni Nugraha; Sandip Kamath; Anita Hazard; Andreas L Lopata; Robyn E O'Hehir Journal: Mol Nutr Food Res Date: 2018-05-14 Impact factor: 5.914