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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 385, Issue 8 (Aug 2004)

Issues

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

Rodrigo Barderas
  • Depto. Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, E-28040 Madrid, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Mayte Villalba
  • Depto. Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, E-28040 Madrid, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Rosalía Rodríguez
  • Depto. Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, E-28040 Madrid, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.089

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

About the article

Corresponding author e-mail:


Received: March 26, 2004

Accepted: June 11, 2004

Published Online: 2005-06-01

Published in Print: 2004-08-01


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.089.

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