1llt: Difference between revisions
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{{STRUCTURE_1llt| PDB=1llt | SCENE= }} | |||
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'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S''' | '''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S''' | ||
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[[Category: Neerven, R J.Van.]] | [[Category: Neerven, R J.Van.]] | ||
[[Category: Spangfort, M D.]] | [[Category: Spangfort, M D.]] | ||
[[Category: | [[Category: Allergen]] | ||
[[Category: | [[Category: Pathogenesis related protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:02:47 2008'' | |||
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Revision as of 21:02, 2 May 2008
BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S
Overview
Specific allergy vaccination is an efficient treatment for allergic disease; however, the development of safer vaccines would enable a more general use of the treatment. Determination of molecular structures of allergens and allergen-Ab complexes facilitates epitope mapping and enables a rational approach to the engineering of allergen molecules with reduced IgE binding. In this study, we describe the identification and modification of a human IgE-binding epitope based on the crystal structure of Bet v 1 in complex with the BV16 Fab' fragment. The epitope occupies approximately 10% of the molecular surface area of Bet v 1 and is clearly conformational. A synthetic peptide representing a sequential motif in the epitope (11 of 16 residues) did not inhibit the binding of mAb BV16 to Bet v 1, illustrating limitations in the use of peptides for B cell epitope characterization. The single amino acid substitution, Glu(45)-Ser, was introduced in the epitope and completely abolished the binding of mAb BV16 to the Bet v 1 mutant within a concentration range 1000-fold higher than wild type. The mutant also showed up to 50% reduction in the binding of human polyclonal IgE, demonstrating that glutamic acid 45 is a critical amino acid also in a major human IgE-binding epitope. By solving the three-dimensional crystal structure of the Bet v 1 Glu(45)-Ser mutant, it was shown that the change in immunochemical activity is directly related to the Glu(45)-Ser substitution and not to long-range structural alterations or collapse of the Bet v 1 mutant tertiary structure.
About this Structure
1LLT is a Single protein structure of sequence from Betula pendula. Full crystallographic information is available from OCA.
Reference
Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis., Spangfort MD, Mirza O, Ipsen H, Van Neerven RJ, Gajhede M, Larsen JN, J Immunol. 2003 Sep 15;171(6):3084-90. PMID:12960334 Page seeded by OCA on Sat May 3 00:02:47 2008
