1h2o
From Proteopedia
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'''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1 MUTANT E45W''' | '''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1 MUTANT E45W''' | ||
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[[Category: Sticht, H.]] | [[Category: Sticht, H.]] | ||
[[Category: Vieths, S.]] | [[Category: Vieths, S.]] | ||
| - | [[Category: | + | [[Category: Heteronuclear nmr]] |
| - | [[Category: | + | [[Category: Major cherry allergen]] |
| - | [[Category: | + | [[Category: Pathogenesis-related protein]] |
| - | [[Category: | + | [[Category: Plant defense]] |
| - | [[Category: | + | [[Category: Structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:20:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:20, 2 May 2008
SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1 MUTANT E45W
Overview
Birch pollinosis is often accompanied by adverse reactions to food due to pollen-allergen specific IgE cross-reacting with homologous food allergens. The tertiary structure of Pru av 1, the major cherry (Prunus avium) allergen, for example, is nearly identical with Bet v 1, the major birch (Betula verrucosa) pollen allergen. In order to define cross-reactive IgE epitopes, we generated and analysed mutants of Pru av 1 and Api g 1.0101, the major celery (Apium graveolens) allergen, by immunoblotting, EAST (enzyme allergosorbent test), CD and NMR spectroscopy. The mutation of Glu45 to Trp45 in the P-loop region, a known IgE epitope of Bet v 1, significantly reduced IgE binding to Pru av 1 in a subgroup of cherry-allergic patients. The backbone conformation of Pru av 1 wild-type is conserved in the three-dimensional structure of Pru av 1 Trp45, demonstrating that the side chain of Glu45 is involved in a cross-reactive IgE epitope. Accordingly, for a subgroup of celery-allergic patients, IgE binding to the homologous celery allergen Api g 1.0101 was enhanced by the mutation of Lys44 to Glu. The almost complete loss of IgE reactivity to the Pru av 1 Pro112 mutant is due to disruption of its tertiary structure. Neither the mutation Ala112 nor deletion of the C-terminal residues 155-159 influenced IgE binding to Pru av 1. In conclusion, the structure of the P-loop partially explains the cross-reactivity pattern, and modulation of IgE-binding by site-directed mutagenesis is a promising approach to develop hypo-allergenic variants for patient-tailored specific immunotherapy.
About this Structure
1H2O is a Single protein structure of sequence from Prunus avium. Full crystallographic information is available from OCA.
Reference
Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure., Neudecker P, Lehmann K, Nerkamp J, Haase T, Wangorsch A, Fotisch K, Hoffmann S, Rosch P, Vieths S, Scheurer S, Biochem J. 2003 Nov 15;376(Pt 1):97-107. PMID:12943529 Page seeded by OCA on Fri May 2 18:20:58 2008
