1qmr
From Proteopedia
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'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G''' | '''BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G''' | ||
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[[Category: Holm, J O.]] | [[Category: Holm, J O.]] | ||
[[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 06:27:39 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:27, 3 May 2008
BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G
Overview
Human type 1 immediate allergic response symptoms are caused by mediator release from basophils and mast cells. This event is triggered by allergens aggregating preformed IgE Abs bound to the high-affinity receptor (FcepsilonRI) on these cells. Thus, the allergen/IgE interaction is crucial for the cascade leading to the allergic and anaphylactic response. Two genetically engineered forms of the white birch pollen major allergen Bet v 1 with point mutations directed at molecular surfaces have been characterized. Four and nine point mutations led to a significant reduction of the binding to human serum IgE, suggesting a mutation-induced distortion of IgE-binding B cell epitopes. In addition, the mutated allergens showed a decrease in anaphylactic potential, because histamine release from human basophils was significantly reduced. Retained alpha-carbon backbone folding pattern of the mutated allergens was indicated by x-ray diffraction analysis and circular dichroism spectroscopy. The rBet v 1 mutants were able to induce proliferation of T cell lines derived from birch pollen allergic patients. The stimulation indices were similar to the indices of nonmutated rBet v 1 and natural Bet v 1 purified from birch pollen. The ability of anti-rBet v 1 mutant specific mouse IgG serum to block binding of human serum IgE to rBet v 1 demonstrates that the engineered rBet v 1 mutants are able to induce Abs reactive with nonmodified Bet v 1. rBet v 1 mutants may constitute vaccine candidates with improved efficacy/safety profiles for safer allergy vaccination.
About this Structure
1QMR is a Single protein structure of sequence from Betula pendula. Full crystallographic information is available from OCA.
Reference
Allergy vaccine engineering: epitope modulation of recombinant Bet v 1 reduces IgE binding but retains protein folding pattern for induction of protective blocking-antibody responses., Holm J, Gajhede M, Ferreras M, Henriksen A, Ipsen H, Larsen JN, Lund L, Jacobi H, Millner A, Wurtzen PA, Spangfort MD, J Immunol. 2004 Oct 15;173(8):5258-67. PMID:15470071 Page seeded by OCA on Sat May 3 06:27:39 2008
