Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa)

Muñoz García, Esther and Luengo Sánchez, Olga and Haroun Díaz, Elisa and Sanz Maroto, Aroa and Palacín Gómez, Aranzazu and Díaz Perales, Araceli and Heras Gozalo, Manuel de las and Labrador Horrillo, Moises and Vivanco, Fernando and Cuesta-Herranz, Javier and Pastor Vargas, Carlos (2013). Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa). "Molecular Nutrition & Food Research", v. 57 (n. 12); pp. 2245-2252. ISSN 1613-4125. https://doi.org/10.1002/mnfr.201300139.

Description

Title: Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa)
Author/s:
  • Muñoz García, Esther
  • Luengo Sánchez, Olga
  • Haroun Díaz, Elisa
  • Sanz Maroto, Aroa
  • Palacín Gómez, Aranzazu
  • Díaz Perales, Araceli
  • Heras Gozalo, Manuel de las
  • Labrador Horrillo, Moises
  • Vivanco, Fernando
  • Cuesta-Herranz, Javier
  • Pastor Vargas, Carlos
Item Type: Article
Título de Revista/Publicación: Molecular Nutrition & Food Research
Date: 2013
ISSN: 1613-4125
Volume: 57
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Scope: 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. Methods and results: Sera from 42 Spanish lettuce-allergic patients were obtained from pa-tients 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. Conclusion: 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.

More information

Item ID: 26291
DC Identifier: http://oa.upm.es/26291/
OAI Identifier: oai:oa.upm.es:26291
DOI: 10.1002/mnfr.201300139
Deposited by: Memoria Investigacion
Deposited on: 24 Sep 2014 17:45
Last Modified: 24 Sep 2014 17:45
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