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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Recombinant expression, purification and cross-reactivity of chenopod profilin: rChe a 2 as a good marker for profilin sensitization

Rodrigo Barderas1 / Mayte Villalba2 / Rosalía Rodríguez3

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Corresponding author e-mail:

Citation Information: Biological Chemistry. Volume 385, Issue 8, Pages 731–737, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2004.089, June 2005

Publication History

Received:
March 26, 2004
Accepted:
June 11, 2004
Published Online:
2005-06-01

Abstract

Chenopod pollen is one of the major sources of allergens in some locations in the US, southern Europe and desert countries, and pollen profilin (Che a 2) is a major allergen. Recombinant Che a 2 (rChe a 2) has been produced in Escherichia coli cells with a final yield of 25 mg/l of cell culture. The expressed protein was isolated and structurally characterized by means of mass spectrometry, Edman degradation and circular dichroism. rChe a 2 displayed a molecular mass of 13 959 Da, which agrees with that of the amino acid sequence. The N-terminal amino acid sequence indicated the correct processing of the recombinant product. The immunological analysis of rChe a 2 showed IgG- and IgE-binding capabilities equivalent to those of its natural counterpart, Che a 2, isolated from the pollen. Inhibition experiments showed high cross-reactivity degrees with different allergenic sources. Inhibition degrees of > 95% and > 80% were obtained for chenopod profilin and, respectively, latex and pollen extracts, whereas 10–95% of inhibition was observed for different plant-derived foods. Due to its close relation to other allergenic profilins from pollens, plant-derived foods and latex, rChe a 2 could be a useful tool in clinical trials to detect profilin-allergic patients and perhaps, depending on its clinical relevance, in specific immunotherapy of these hypersensitive individuals.

Keywords: Che a 2; Chenopodium album pollinosis; cross-reactivity; profilin; recombinant allergen

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