Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: A comprehensive allergenomic approach. Issue 5 (13th January 2014)

• Record Type: Journal Article
• Authors: Kamath, Sandip D.; Rahman, Anas M. Abdel; Voskamp, Astrid; Komoda, Toshikazu; Rolland, Jennifer M.; O'Hehir, Robyn E.; Lopata, Andreas L.
• Is Part Of: Molecular nutrition & food research. Volume 58:Issue 5(2014:May)
• Page Start: 1144
• Page End: 1155
• Publication Date: 2014-01-13
• Subjects: Food -- Biotechnology -- Periodicals; Food -- Microbiology -- Periodicals; Nutrition -- Periodicals; Food -- Toxicology -- Periodicals; Nutrition -- Periodicals; Food Microbiology -- Periodicals; Food Technology -- Periodicals; Molecular Biology -- Periodicals; 664.0705
• DOI: 10.1002/mnfr.201300584
• Languages: English
• ISSNs: 1613-4125

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="mnfr2153-sec-0010" sec-type="section"> <title>Scope</title> <p>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.</p> </sec> <sec id="mnfr2153-sec-0020" sec-type="section"> <title>Methods and results</title> <p>Proteins from raw and heat‐processed black tiger prawn (<italic>Penaeus monodon</italic>) 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.</p> </sec> <sec id="mnfr2153-sec-0030" sec-type="section"> <title>Conclusion</title> <p>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.</p> </sec> </abstract>