Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1, 3‐galactose‐containing allergens. Issue 10 (28th July 2014)
- Record Type:
- Journal Article
- Title:
- Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1, 3‐galactose‐containing allergens. Issue 10 (28th July 2014)
- Main Title:
- Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1, 3‐galactose‐containing allergens
- Authors:
- Apostolovic, D.
Tran, T. A. T.
Hamsten, C.
Starkhammar, M.
Cirkovic Velickovic, T.
van Hage, M. - Abstract:
- <abstract abstract-type="main" id="all12462-abs-0001"> <title>Abstract</title> <sec id="all12462-sec-0001" sec-type="section"> <title>Background</title> <p>Red meat allergy presents a novel form of food allergy with severe delayed allergic reactions where IgE antibodies are directed against the carbohydrate α‐Gal epitope. Food preparation and processing can influence the allergenicity of proteins. The aim of this study was to characterize the proteomic profile of different beef preparations and to investigate their α‐Gal reactivity and potential allergenicity.</p> </sec> <sec id="all12462-sec-0002" sec-type="section"> <title>Methods</title> <p>Extracts from raw, boiled, fried, and medium rare prepared beef were assessed by 2D PAGE for the comparison of protein profiles. IgE‐binding proteins were identified using immunoblot‐coupled proteomic analysis using sera from red meat‐allergic patients. Presence of the α‐Gal epitope was verified using anti‐α‐Gal antibody and IgE inhibition immunoblot with α‐Gal.</p> </sec> <sec id="all12462-sec-0003" sec-type="section"> <title>Results</title> <p>Multiple IgE‐binding proteins were detected in the different beef preparations, many of which were also recognized by the anti‐α‐Gal antibody. Protein spots reacting with IgE in patient sera were analyzed by MS/MS, resulting in identification of 18 proteins with high identification scores. Seven of the 18 beef allergens identified using meat‐allergic patient sera were also recognized by the<abstract abstract-type="main" id="all12462-abs-0001"> <title>Abstract</title> <sec id="all12462-sec-0001" sec-type="section"> <title>Background</title> <p>Red meat allergy presents a novel form of food allergy with severe delayed allergic reactions where IgE antibodies are directed against the carbohydrate α‐Gal epitope. Food preparation and processing can influence the allergenicity of proteins. The aim of this study was to characterize the proteomic profile of different beef preparations and to investigate their α‐Gal reactivity and potential allergenicity.</p> </sec> <sec id="all12462-sec-0002" sec-type="section"> <title>Methods</title> <p>Extracts from raw, boiled, fried, and medium rare prepared beef were assessed by 2D PAGE for the comparison of protein profiles. IgE‐binding proteins were identified using immunoblot‐coupled proteomic analysis using sera from red meat‐allergic patients. Presence of the α‐Gal epitope was verified using anti‐α‐Gal antibody and IgE inhibition immunoblot with α‐Gal.</p> </sec> <sec id="all12462-sec-0003" sec-type="section"> <title>Results</title> <p>Multiple IgE‐binding proteins were detected in the different beef preparations, many of which were also recognized by the anti‐α‐Gal antibody. Protein spots reacting with IgE in patient sera were analyzed by MS/MS, resulting in identification of 18 proteins with high identification scores. Seven of the 18 beef allergens identified using meat‐allergic patient sera were also recognized by the anti‐α‐Gal monoclonal antibody, and four of them were stabile to thermal treatment. Furthermore, a dose‐dependent inhibition of red meat‐allergic patients' IgE to beef by α‐Gal was demonstrated.</p> </sec> <sec id="all12462-sec-0004" sec-type="section"> <title>Conclusions</title> <p>We show that the α‐Gal epitope is commonly present in IgE‐reactive beef proteins recognized by meat‐allergic patients. Seven novel α‐Gal‐containing IgE‐binding proteins were identified, of which four were stable to heat treatment. Thus, the allergenicity of red meat proteins is preserved even upon different thermal cooking.</p> </sec> </abstract> … (more)
- Is Part Of:
- Allergy. Volume 69:Issue 10(2014:Oct.)
- Journal:
- Allergy
- Issue:
- Volume 69:Issue 10(2014:Oct.)
- Issue Display:
- Volume 69, Issue 10 (2014)
- Year:
- 2014
- Volume:
- 69
- Issue:
- 10
- Issue Sort Value:
- 2014-0069-0010-0000
- Page Start:
- 1308
- Page End:
- 1315
- Publication Date:
- 2014-07-28
- Subjects:
- Allergy -- Periodicals
616.97 - Journal URLs:
- http://estar.bl.uk/cgi-bin/sciserv.pl?collection=journals&journal=01054538 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1398-9995 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/all.12462 ↗
- Languages:
- English
- ISSNs:
- 0105-4538
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0790.945000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4181.xml