Immunoglobulin-E reactivity and structural analysis of wheat low-molecular-weight glutenin subunits and their repetitive and nonrepetitive halves.

The IgE reactivity of the recombinant glutenin subunits P73 and B16, and of their repetitive N-terminal and nonrepetitive C-terminal halves, was analyzed using dot-blot with sera from patients diagnosed with baker's asthma, wheat-dependent exercise-induced anaphylaxis, or allergy to hydrolyzed wheat proteins. The linear epitopes of B16 were identified using the Pepscan method. Except for one common epitope, the IgE binding domains of glutenins differ from those of ω5-gliadins. Secondary structure content of the proteins was determined using synchrotron radiation circular dichroism (SRCD): while α structures were predominant in all glutenin subunits, fragments, or chimeras, a high IgE reactivity was associated with proteins rich in β structures. Mixing B16 halves induced conformational interaction, as evidenced by dynamic light scattering and SRCD. IgE reactivity was correlatively increased, as when the halves were associated in the B16-P73 chimera. These results suggest that structural interaction between N- and C-terminal halves may promote epitope presentation.

[1]  B. Bakan,et al.  Immunoglobulin‐E‐binding epitopes of wheat allergens in patients with food allergy to wheat and in mice experimentally sensitized to wheat proteins , 2011, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

[2]  D. Pozzo,et al.  Structural analysis of protein complexes with sodium alkyl sulfates by small-angle scattering and polyacrylamide gel electrophoresis. , 2011, Langmuir : the ACS journal of surfaces and colloids.

[3]  Dominique Tessier,et al.  A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures , 2010, Molecular Immunology.

[4]  D. Choudat,et al.  Immunoblotting analysis of wheat allergens: control of side reactions through wheat polypeptides naturally present in dried cow milk , 2010 .

[5]  N. Raison-Peyron,et al.  High molecular weight entities in industrial wheat protein hydrolysates are immunoreactive with IgE from allergic patients. , 2010, Journal of agricultural and food chemistry.

[6]  G. Branlard,et al.  Low Molecular Weight Glutenins in Wheat-Dependant, Exercise-Induced Anaphylaxis: Allergenicity and Antigenic Relationships with Omega 5-Gliadins , 2010, International Archives of Allergy and Immunology.

[7]  Haifeng Zhao,et al.  Effect of acetic acid deamidation-induced modification on functional and nutritional properties and conformation of wheat gluten. , 2010, Journal of the science of food and agriculture.

[8]  R. J. Green,et al.  Characterisation of an s-type low molecular weight glutenin subunit of wheat and its proline and glutamine-rich repetitive domain. , 2010 .

[9]  I. Lauer,et al.  Relevance of IgE binding to short peptides for the allergenic activity of food allergens. , 2009, The Journal of allergy and clinical immunology.

[10]  S. Denery-Papini,et al.  Evaluation of an in vitro Mast Cell Degranulation Test in the Context of Food Allergy to Wheat , 2008, International Archives of Allergy and Immunology.

[11]  T. Chardot,et al.  Recombinant proteins and peptides as tools for studying IgE reactivity with low-molecular-weight glutenin subunits in some wheat allergies. , 2007, Journal of agricultural and food chemistry.

[12]  Andrew J. Miles,et al.  A reference database for circular dichroism spectroscopy covering fold and secondary structure space , 2006, Bioinform..

[13]  N. Raison-Peyron,et al.  Hydrolysed wheat proteins present in cosmetics can induce immediate hypersensitivities , 2006, Contact dermatitis.

[14]  F. Pineau,et al.  Identification of IgE‐binding epitopes on gliadins for patients with food allergy to wheat , 2005, Allergy.

[15]  Alan R Davidson,et al.  The structure of “unstructured” regions in peptides and proteins: Role of the polyproline II helix in protein folding and recognition * , 2005, Biopolymers.

[16]  S. Vieths,et al.  Immunoglobulin E-reactivity of wheat-allergic subjects (baker's asthma, food allergy, wheat-dependent, exercise-induced anaphylaxis) to wheat protein fractions with different solubility and digestibility. , 2004, Molecular nutrition & food research.

[17]  Jonathan G. Lees,et al.  CDtool-an integrated software package for circular dichroism spectroscopic data processing, analysis, and archiving. , 2004, Analytical biochemistry.

[18]  Lee Whitmore,et al.  DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data , 2004, Nucleic Acids Res..

[19]  S. Masci,et al.  The low-molecular-weight glutenin subunits of wheat gluten , 2004 .

[20]  A. Tatham,et al.  Identification of the IgE-binding Epitope in ω-5 Gliadin, a Major Allergen in Wheat-dependent Exercise-induced Anaphylaxis* , 2004, Journal of Biological Chemistry.

[21]  S. Denery-Papini,et al.  Food allergy to wheat: identification of immunogloglin E and immunoglobulin G‐binding proteins with sequential extracts and purified proteins from wheat flour , 2003, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

[22]  K. Palosuo.  Update on wheat hypersensitivity , 2003, Current opinion in allergy and clinical immunology.

[23]  T. Reunala,et al.  Wheat ω-5 gliadin is a major allergen in children with immediate allergy to ingested wheat☆☆☆ , 2001 .

[24]  P. Shewry,et al.  High-level expression of a wheat LMW glutenin subunit using a baculovirus system , 1994 .

[25]  P. Song,et al.  Protein structures in SDS micelle-protein complexes. , 1992, Biophysical journal.

[26]  P. Shewry,et al.  Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[27]  I. V. van Stokkum,et al.  Estimation of protein secondary structure and error analysis from circular dichroism spectra. , 1990, Analytical biochemistry.

[28]  P. Shewry,et al.  The conformations of wheat gluten proteins, II, aggregated gliadins and low molecular weight subunits of glutenin , 1987 .