Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine beta-lactoglobulin allergen

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):25-8. doi: 10.1107/S174430910706160X. Epub 2007 Dec 20.

Abstract

A D1 Fab fragment containing the allergen-binding variable domains of the IgE antibody was characterized by ESI FT-ICR mass spectrometry and crystallized with bovine beta-lactoglobulin (BLG) using the hanging-drop vapour-diffusion method at 293 K. X-ray data suitable for structure determination were collected to 2.8 A resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 A. The three-dimensional structure of the D1 Fab fragment-BLG complex will provide the first insight into IgE antibody-allergen interactions at the molecular level.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / immunology
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Child
  • Crystallography, X-Ray
  • Food Hypersensitivity / immunology
  • Humans
  • Hypersensitivity / immunology
  • Immunoglobulin E / chemistry*
  • Immunoglobulin Fab Fragments / chemistry*
  • Immunoglobulin Fab Fragments / isolation & purification
  • Immunoglobulin Heavy Chains / chemistry
  • Immunoglobulin Light Chains / chemistry
  • Lactoglobulins / chemistry*
  • Lactoglobulins / immunology*
  • Lymphocytes / immunology
  • Molecular Sequence Data
  • Spectrum Analysis

Substances

  • Allergens
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Heavy Chains
  • Immunoglobulin Light Chains
  • Lactoglobulins
  • Immunoglobulin E