NDLI: Crystal Structure of a Dimerized Cockroach Allergen Bla g 2 Complexed with a Monoclonal Antibody

Content Provider	Journal of Biological Chemistry (JBC)
Author	Li, Mi Gustchina, Alla Alexandratos, Jerry Wlodawer, Alexander Wünschmann, Sabina Kepley, Christopher L. Chapman, Martin D. Pomés, Anna
Abstract	The crystal structure of a 1:1 complex between the German cockroach allergen Bla g 2 and the Fab′ fragment of a monoclonal antibody 7C11 was solved at 2.8-Å resolution. Bla g 2 binds to the antibody through four loops that include residues 60-70, 83-86, 98-100, and 129-132. Cation-π interactions exist between Lys-65, Arg-83, and Lys-132 in Bla g 2 and several tyrosines in 7C11. In the complex with Fab′, Bla g 2 forms a dimer, which is stabilized by a quasi-four-helix bundle comprised of an α-helix and a helical turn from each allergen monomer, exhibiting a novel dimerization mode for an aspartic protease. A disulfide bridge between C51a and C113, unique to the aspartic protease family, connects the two helical elements within each Bla g 2 monomer, thus facilitating formation of the bundle. Mutation of these cysteines, as well as the residues Asn-52, Gln-110, and Ile-114, involved in hydrophobic interactions within the bundle, resulted in a protein that did not dimerize. The mutant proteins induced less β-hexosaminidase release from mast cells than the wild-type Bla g 2, suggesting a functional role of dimerization in allergenicity. Because 7C11 shares a binding epitope with IgE, the information gained by analysis of the crystal structure of its complex provided guidance for site-directed mutagenesis of the allergen epitope. We have now identified key residues involved in IgE antibody binding; this information will be useful for the design of vaccines for immunotherapy.
Related Links	http://www.jbc.org/content/283/33/22806.abstract
Ending Page	22814
Starting Page	22806
Page Count	9
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	33
Volume Number	283
DOI	10.1074/jbc.M800937200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2008-08-15
Access Restriction	Open
Subject Keyword	Protein Structure and Folding
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Crystal Structure of a Dimerized Cockroach Allergen Bla g 2 Complexed with a Monoclonal Antibody*

Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody.

Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody (2011)

Mechanisms of allergen-antibody interaction of cockroach allergen bla g 2 with monoclonal antibodies that inhibit ige antibody binding.

Mechanisms of Allergen-Antibody Interaction of Cockroach Allergen Bla g 2 with Monoclonal Antibodies That Inhibit IgE Antibody Binding

Molecular Cloning of a Major Cockroach (Blattella germanica) Allergen, Bla g 2 SEQUENCE HOMOLOGY TO THE ASPARTIC PROTEASES

Mechanisms of Allergen-Antibody Interaction of Cockroach Allergen Bla g 2 with Monoclonal Antibodies That Inhibit IgE Antibody Binding

Antigenic Determinants of the Bilobal Cockroach Allergen Bla g 2

Carbohydrates Contribute to the Interactions between Cockroach Allergen Bla g 2 and a Monoclonal Antibody

Crystal Structure of a Dimerized Cockroach Allergen Bla g 2 Complexed with a Monoclonal Antibody

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Crystal Structure of a Dimerized Cockroach Allergen Bla g 2 Complexed with a Monoclonal Antibody*

Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody.

Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody (2011)

Mechanisms of allergen-antibody interaction of cockroach allergen bla g 2 with monoclonal antibodies that inhibit ige antibody binding.

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