Molecular characterization of recombinant T1, a non-allergenic periwinkle (Catharanthus roseus) protein, with sequence similarity to the Bet v 1 plant allergen family
- 1 July 2003
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 373 (1), 261-269
- https://doi.org/10.1042/bj20030331
Abstract
More than 25% of the population suffer from Type I allergy, an IgE-mediated hypersensitivity disease. Allergens with homology to the major birch (Betula verrucosa) pollen allergen, Bet v 1, belong to the most potent elicitors of IgE-mediated allergies. T1, a cytokinin-inducible cytoplasmic periwinkle (Catharanthus roseus) protein, with significant sequence similarity to members of the Bet v 1 plant allergen family, was expressed in Escherichia coli. Recombinant T1 (rT1) did not react with IgE antibodies from allergic patients, and failed to induce basophil histamine release and immediate-type skin reactions in Bet v 1-allergic patients. Antibodies raised against purified rT1 could be used for in situ localization of natural T1 by immunogold electron microscopy, but did not cross-react with most of the Bet v 1-related allergens. CD analysis showed significant differences regarding secondary structure and thermal denaturation behaviour between rT1 and recombinant Bet v 1, suggesting that these structural differences are responsible for the different allergenicity of the proteins. T1 represents a non-allergenic member of the Bet v 1 family that may be used to study structural requirements of allergenicity and to engineer hypo-allergenic plants by replacing Bet v 1-related allergens for primary prevention of allergy.Keywords
This publication has 40 references indexed in Scilit:
- Will genetically modified foods be allergenic?Journal of Allergy and Clinical Immunology, 2001
- Protein secondary structure prediction based on position-specific scoring matrices 1 1Edited by G. Von HeijneJournal of Molecular Biology, 1999
- X-ray and NMR structure of Bet v 1, the origin of birch pollen allergyNature Structural & Molecular Biology, 1996
- Reduction of 14–16 kDa allergenic proteins in transgenic rice plants by antisense geneFEBS Letters, 1996
- Type I allergic reactions to plant-derived food: A consequence of primary sensitization to pollen allergens*Journal of Allergy and Clinical Immunology, 1996
- Cloning and Sequencing of Mal d 1, the Major Allergen from Apple (Malus domestica), and Its Immunological Relationship to Bet v 1, the Major Birch Pollen AllergenBiochemical and Biophysical Research Communications, 1995
- Purification, Characterization and N-Terminal Amino Acid Sequence of a New Major Allergen from European Chestnut Pollen - Cas s 1Biochemical and Biophysical Research Communications, 1993
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- The skin prick test in the diagnosis of atopic allergyJournal of the American Academy of Dermatology, 1989
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979