Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab′ fragment

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 55; no. 12; pp. 2035 - 2036
• Main Authors: Spangfort, Michael D., Mirza, Osman, Svensson, L. Anders, Larsen, Jørgen N., Gajhede, Michael, Ipsen, Henrik
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.12.1999
• Subjects: allergen-Fab′ complexes; Allergens - chemistry; Allergens - isolation & purification; Animals; Antibodies, Monoclonal - chemistry; Antigen-Antibody Reactions; Antigens, Plant; Bet v 1; birch pollen; Crystallization; Crystallography, X-Ray; Humans; Immunoglobulin Fab Fragments - chemistry; Immunoglobulin G - chemistry; Mice; monoclonal antibodies; Plant Proteins - chemistry; Plant Proteins - isolation & purification; Pollen - chemistry; Pollen - immunology; Rhinitis, Allergic, Seasonal - immunology; serum IgE
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444999011804

The human type I allergic response is characterized by the presence of allergen‐specific serum immunoglobulin E (IgE). Allergen‐mediated cross‐linking of receptor‐bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen–antibody interaction, a complex between the major birch‐pollen allergen Bet v 1 and a Fab′ fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit‐cell parameters a = 91.65, b = 99.14, c = 108.90 Å, α = 105.7, β = 98.32, γ = 97.62°, and diffract to 2.9 Å resolution when analyzed at 100 K using synchrotron‐generated X‐­rays.