A Recombinant Sal k 1 Isoform as an Alternative to the Polymorphic Allergen from Salsola kali Pollen for Allergy Diagnosis

Mas, Salvador and Boissy, Patrice and Monsalve, Rafael I. and Cuesta Herranz, J. and Diaz Perales, Araceli and Fernández, Javier and Colás, Carlos and Rodríguez, Rosalía and Barderas, Rodrigo and Villalba, M. (2015). A Recombinant Sal k 1 Isoform as an Alternative to the Polymorphic Allergen from Salsola kali Pollen for Allergy Diagnosis. "International Archives of Allergy And Immunology", v. 167 (n. 2); pp. 83-93. ISSN 1018-2438. https://doi.org/10.1159/000434680.

Description

Title: A Recombinant Sal k 1 Isoform as an Alternative to the Polymorphic Allergen from Salsola kali Pollen for Allergy Diagnosis
Author/s:
  • Mas, Salvador
  • Boissy, Patrice
  • Monsalve, Rafael I.
  • Cuesta Herranz, J.
  • Diaz Perales, Araceli
  • Fernández, Javier
  • Colás, Carlos
  • Rodríguez, Rosalía
  • Barderas, Rodrigo
  • Villalba, M.
Item Type: Article
Título de Revista/Publicación: International Archives of Allergy And Immunology
Date: September 2015
ISSN: 1018-2438
Volume: 167
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

The incidence of Amaranthaceae pollen allergy has increased due to the desertification occurring in many countries. In some regions of Spain, Salsola kali is the main cause of pollinosis, at almost the same level as olive and grass pollen. Sal k 1 - the sensitization marker of S. kali pollinosis - is used in clinical diagnosis, but is purified at a low yield from pollen. We aimed to produce a recombinant (r)Sal k 1 able to span the structural and immunological properties of the natural isoforms from pollen, and validate its potential use for diagnosis. METHODS: Specific cDNA was amplified by PCR, cloned into the pET41b vector and used to transform BL21 (DE3) Escherichia coli cells. Immunoblotting, ELISA, basophil activation and skin-prick tests were used to validate the recombinant protein against Sal k 1 isolated from pollen. Sera and blood cells from S. kali pollen-sensitized patients and specific monoclonal and polyclonal antisera were used. RESULTS: rSal k 1 was produced in bacteria with a yield of 7.5 mg/l of cell culture. The protein was purified to homogeneity and structural and immunologically validated against the natural form. rSal k 1 exhibited a higher IgE cross-reactivity with plant-derived food extracts such as peanut, almond or tomato than with pollen sources such as Platanus acerifolia and Oleaceae members. CONCLUSIONS: rSal k 1 expressed in bacteria retains intact structural and immunological properties in comparison to the pollen-derived allergen. It spans the immunological properties of most of the isoforms found in pollen, and it might substitute natural Sal k 1 in clinical diagnosis.

More information

Item ID: 41287
DC Identifier: http://oa.upm.es/41287/
OAI Identifier: oai:oa.upm.es:41287
DOI: 10.1159/000434680
Official URL: http://content.karger.com/Article/Abstract/434680
Deposited by: Memoria Investigacion
Deposited on: 21 Jun 2016 15:30
Last Modified: 21 Jun 2016 15:30
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