TY - JOUR
T1 - Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: a comprehensive allergenomic approach
AU - Kamath, Sandip Dayanand
AU - Rahman, Anas M Abdel
AU - Voskamp, Astrid Lida
AU - Komoda, Toshikazu
AU - Rolland, Jennifer May
AU - O'Hehir, Robyn E
AU - Lopata, Andreas L
PY - 2014
Y1 - 2014
N2 - 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. ? 2014 WILEY-VCH Verlag GmbH Co. KGaA, Weinheim.
AB - 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. ? 2014 WILEY-VCH Verlag GmbH Co. KGaA, Weinheim.
UR - http://onlinelibrary.wiley.com/doi/10.1002/mnfr.201300584/epdf
U2 - 10.1002/mnfr.201300584
DO - 10.1002/mnfr.201300584
M3 - Article
VL - 58
SP - 1144
EP - 1155
JO - Molecular Nutrition & Food Research
JF - Molecular Nutrition & Food Research
SN - 1613-4125
IS - 5
ER -