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The natural profilin from R ussian thistle ( S alsola kali ) contains a low I g E ‐binding ability isoform – molecular and immunological characterization
Author(s) -
Mas Salvador,
Barderas Rodrigo,
Colás Carlos,
Quiralte Joaquín,
Rodríguez Rosalía,
Villalba Mayte
Publication year - 2012
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12024
Subject(s) - profilin , gene isoform , epitope , hypoallergenic , biology , melittin , allergen , biochemistry , immunoglobulin e , recombinant dna , antigenicity , molecular mass , chemistry , microbiology and biotechnology , allergy , genetics , antigen , immunology , antibody , gene , peptide , enzyme , actin cytoskeleton , cytoskeleton , cell
Chenopodiaceae pollens such as those from S alsola kali and C henopodium album are important causes of allergy in M editerranean areas because of the progress of desertification in European countries. Among the various allergenic protein families, profilins constitute a group of pan‐allergens that are involved in polysensitization and pollen‐food allergy syndrome. Two‐dimensional electrophoresis analysis of S . kali profilin highlighted a polymorphic pattern, with several isoforms that have different molecular features (isoelectric point and molecular mass) and immunological features. Two isoforms have been cloned and sequenced. Sal k 4.02 and S al k 4.03 displayed non‐conservative amino acid changes in critical positions of the I g E epitopes. Both isoforms were produced in E scherichia coli and structurally and spectroscopically characterized. Changes in the electrophoretic mobility and in their I g G and I g E immunological behavior were observed in comparison with C he a 2, their counterpart from C . album . The IgE‐binding ability of S al k 4.03 is similar to that of C he a 2, whereas S al k 4.02 showed a 35% reduction in IgE binding in 86% of patients, suggesting a hypoallergenic character. Three‐dimensional modeling allowed us to propose which amino acid residues are involved in those immunological changes based on epitope mapping studies previously performed in other profilins. These profilin isoforms constitute suitable candidates for specific immunotherapy with recombinant allergens.