Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis.

Title:

Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis.

Dataset

identifier:	1468288
description:	epitope description:E46 antigen name:Bet v 1 host organism:Mus musculus BALB/c antibody name:BV16
aggregation:	instance of dataset
availability:	available
primaryPublications:	12960334

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1005425
landingPage:	http://www.iedb.org/assay/1468288

Publication

type:	Literature
publicationVenue:	J Immunol
dates:	2003

Dimension

study type:	b cell assays
subject species:	Betula pendula

Person

fullName:	Michael D Spangfort Osman Mirza Henrik Ipsen R J Joost Van Neerven Michael Gajhede Jø rgen N Larsen

Data Type

method:	antigen inhibition

Study

name:	Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis.
description:	The authors conclude that Glu45 on Bet v 1 is a critical amino acid for mAb BV16 binding because a Bet v 1 mutant carrying a Glu to Ser mutation at position 45 did not inhibit the binding of Bet v 1.2801 to mAb BV16. Mutants carrying substitutions at positions 8, 32, 60, 77, or 108 were able to block binding. The crystal structure of Bet v 1 in complex with the Fab' fragment of mAb BV16, showed that the antibody recognized a conformational epitope including residues 42-52. The electron density map showed that the Glu45 to Ser mutant did not significantly affect the overall structure of the molecule. Glu45 is also a critical residue in a major human IgE-binding epitope.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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