Identification of thaumatin‐like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa). Issue 12 (25th August 2013)
- Record Type:
- Journal Article
- Title:
- Identification of thaumatin‐like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa). Issue 12 (25th August 2013)
- Main Title:
- Identification of thaumatin‐like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa)
- Authors:
- Muñoz‐García, Esther
Luengo‐Sánchez, Olga
Haroun‐Díaz, Elisa
Maroto, Aroa Sanz
Palacín, Arancha
Díaz –Perales, Araceli
de, Manuel
Labrador‐Horrillo, Moisés
Vivanco, Fernando
Cuesta‐Herranz, Javier
Pastor‐Vargas, Carlos - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="mnfr2057-sec-0010" sec-type="section"> <title>Scope</title> <p>Today, about 2–8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic reactions. To date, however, only one lipid transfer protein has been described in allergic reaction to lettuce. The aim of this study was to identify potential new allergens involved in lettuce allergy.</p> </sec> <sec id="mnfr2057-sec-0020" sec-type="section"> <title>Methods and results</title> <p>Sera from 42 Spanish lettuce‐allergic patients were obtained from patients recruited at the outpatient clinic. IgE‐binding proteins were detected by SDS‐PAGE and immunoblotting. Molecular characterization of IgE‐binding bands was performed by MS. Thaumatin was purified using the Agilent 3100 OFFGEL system. The IgE‐binding bands recognized in the sera of more than 50% of patients were identified as lipid transfer protein (9 kDa), a thaumatin‐like protein (26 kDa), and an aspartyl protease (35 and 45 kDa). ELISA inhibition studies were performed to confirm the IgE reactivity of the purified allergen.</p> </sec> <sec id="mnfr2057-sec-0030" sec-type="section"> <title>Conclusion</title> <p>Two new major lettuce allergens—a thaumatin‐like protein and<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="mnfr2057-sec-0010" sec-type="section"> <title>Scope</title> <p>Today, about 2–8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic reactions. To date, however, only one lipid transfer protein has been described in allergic reaction to lettuce. The aim of this study was to identify potential new allergens involved in lettuce allergy.</p> </sec> <sec id="mnfr2057-sec-0020" sec-type="section"> <title>Methods and results</title> <p>Sera from 42 Spanish lettuce‐allergic patients were obtained from patients recruited at the outpatient clinic. IgE‐binding proteins were detected by SDS‐PAGE and immunoblotting. Molecular characterization of IgE‐binding bands was performed by MS. Thaumatin was purified using the Agilent 3100 OFFGEL system. The IgE‐binding bands recognized in the sera of more than 50% of patients were identified as lipid transfer protein (9 kDa), a thaumatin‐like protein (26 kDa), and an aspartyl protease (35 and 45 kDa). ELISA inhibition studies were performed to confirm the IgE reactivity of the purified allergen.</p> </sec> <sec id="mnfr2057-sec-0030" sec-type="section"> <title>Conclusion</title> <p>Two new major lettuce allergens—a thaumatin‐like protein and an aspartyl protease—have been identified and characterized. These allergens may be used to improve both diagnosis and treatment of lettuce‐allergic patients.</p> </sec> </abstract> … (more)
- Is Part Of:
- Molecular nutrition & food research. Volume 57:Issue 12(2013:Dec.)
- Journal:
- Molecular nutrition & food research
- Issue:
- Volume 57:Issue 12(2013:Dec.)
- Issue Display:
- Volume 57, Issue 12 (2013)
- Year:
- 2013
- Volume:
- 57
- Issue:
- 12
- Issue Sort Value:
- 2013-0057-0012-0000
- Page Start:
- 2245
- Page End:
- 2252
- Publication Date:
- 2013-08-25
- 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 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/mnfr.201300139 ↗
- Languages:
- English
- ISSNs:
- 1613-4125
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817992
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3256.xml