Characterization of IgE-binding epitopes of peanut (Arachis hypogaea) PNA lectin allergen cross-reacting with other structurally related legume lectins.

Sera from peanut allergic patients contain IgE that specifically interact with the peanut lectin PNA and other closely related legume lectins like LcA from lentil, PsA from pea and PHA from kidney bean. The IgE-binding activity of PNA and legume lectins was assessed by immunoblotting, surface plasmon resonance (SPR) and ELISA measurements, using sera from peanut allergic patients as a IgE source. This IgE-binding cross-reactivity most probably depends on the occurrence of structurally related epitopes that have been identified on the molecular surface of PNA and other legume lectins. These epitopes definitely differ from those responsible for the allergenicity of the major allergens Ara h 1, Ara h 2 and Ara h 3, also recognized by the IgE-containing sera of peanut allergic patients. Peanut lectin PNA and other legume lectins have been characterized as potential allergens for patients allergic to edible legume seeds. However, the clinical significance of the lectin-IgE interaction has to be addressed.

[1]  C. Abergel,et al.  X-ray crystal structure determination and refinement at 1.9 A resolution of isolectin I from the seeds of Lathyrus ochrus. , 1990, Journal of molecular biology.

[2]  W. Becker,et al.  Influence of the maillard reaction on the allergenicity of rAra h 2, a recombinant major allergen from peanut (Arachis hypogaea), its major epitopes, and peanut agglutinin. , 2005, Journal of agricultural and food chemistry.

[3]  P. Rougé,et al.  Localisation of amino acid sequence stretches containing a continuous epitope on the surface of the two Lathyrus ochrus isolectins. , 1990, Immunology letters.

[4]  G. Mitchell,et al.  Allergenicity of concanavalin A in mice. , 1979, International archives of allergy and applied immunology.

[5]  P. Rougé,et al.  Isolation and partial characterization of two isolectins from Lathyrus ochrus (L.) DC. seeds , 1984 .

[6]  H. Sampson,et al.  Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family. , 2005, The Journal of allergy and clinical immunology.

[7]  R. Helm,et al.  Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. , 1994, International archives of allergy and immunology.

[8]  F. L. Suddath,et al.  Design, expression, and crystallization of recombinant lectin from the garden pea (Pisum sativum). , 1990, The Journal of biological chemistry.

[9]  M Vijayan,et al.  Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex. , 1996, Journal of molecular biology.

[10]  P. Rougé,et al.  Plant Lectins: A Composite of Several Distinct Families of Structurally and Evolutionary Related Proteins with Diverse Biological Roles , 1998 .

[11]  E. Champagne,et al.  Allergenicity of Maillard reaction products from peanut proteins. , 1999, Journal of agricultural and food chemistry.

[12]  V. Zavázal,et al.  Lectin-binding ability of immunoglobulin E and its partipication in triggering of mast cells , 2008, Folia Microbiologica.

[13]  K. Sharp,et al.  Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.

[14]  P. Shewry,et al.  Seed storage proteins: structures and biosynthesis. , 1995, The Plant cell.

[15]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[16]  J. Risler,et al.  Amino acid substitutions in structurally related proteins. A pattern recognition approach. Determination of a new and efficient scoring matrix. , 1988, Journal of molecular biology.

[17]  A. Burks,et al.  Molecular cloning and epitope analysis of the peanut allergen Ara h 3. , 1999, The Journal of clinical investigation.

[18]  S. Isoyama,et al.  Interaction of lectins with human IgE: IgE-binding property and histamine-releasing activity of twelve plant lectins. , 1992, International archives of allergy and immunology.

[19]  S. N. Pramod,et al.  Effect of horse gram lectin (Dolichos biflorus agglutinin) on degranulation of mast cells and basophils of atopic subjects: identification as an allergen. , 2006, International immunopharmacology.

[20]  M. Schlaak,et al.  Dietary lectins can induce in vitro release of IL‐4 and IL‐13 from human basophils , 1999, European journal of immunology.

[21]  D. Barnett,et al.  Multiplicity of allergens in peanuts. , 1983, The Journal of allergy and clinical immunology.

[22]  R. Siraganian,et al.  Mechanism of Action of Concanvalin A on Human Basophils , 1975, The Journal of Immunology.

[23]  I. Glaspole,et al.  Immunological analysis of allergenic cross‐reactivity between peanut and tree nuts , 2003, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

[24]  L. Wyns,et al.  Structural analysis of two crystal forms of lentil lectin at 1.8 Å resolution , 1994, Proteins.

[25]  J. Thompson,et al.  The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. , 1997, Nucleic acids research.

[26]  G. Boons,et al.  Comprehensive glycoscience : from chemistry to systems biology , 2007 .

[27]  B. Honig,et al.  Calculation of electrostatic potentials in an enzyme active site , 1987, Nature.

[28]  V. Rotari,et al.  Calcium ions make phytohemagglutinin resistant to trypsin proteolysis. , 2008, Journal of agricultural and food chemistry.

[29]  Hugh A Sampson,et al.  Update on food allergy. , 2004, The Journal of allergy and clinical immunology.

[30]  P. Restani,et al.  Two-dimensional electrophoresis and western-blotting analyses with anti Ara h 3 basic subunit IgG evidence the cross-reacting polypeptides of Arachis hypogaea, Glycine max, and Lupinus albus seed proteomes. , 2005, Journal of agricultural and food chemistry.

[31]  R. Frank.  Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support , 1992 .

[32]  C. Radauer,et al.  Type I allergy to elderberry (Sambucus nigra) is elicited by a 33.2 kDa allergen with significant homology to ribosomal inactivating proteins , 2003, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

[33]  P. Rougé,et al.  The identification of two peptide sequences of light subunits of the Lathyrus ochrus isolectins containing a sequential epitope. , 1988, Immunology letters.

[34]  R. Helm,et al.  Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. , 1991, The Journal of allergy and clinical immunology.

[35]  R. Helm,et al.  Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. , 1992, The Journal of allergy and clinical immunology.

[36]  A. Treves,et al.  Effect of Concanavalin A on Lymphocyte-mediated Cytotoxicity , 1971, Nature.

[37]  B. Whisman,et al.  Cross-reactivity among edible nuts: double immunodiffusion, crossed immunoelectrophoresis, and human specific igE serologic surveys. , 2005, Annals of Allergy, Asthma & Immunology.

[38]  P. Rougé,et al.  The major elderberry (Sambucus nigra) fruit protein is a lectin derived from a truncated type 2 ribosome-inactivating protein. , 1997, The Plant journal : for cell and molecular biology.

[39]  M. Haine,et al.  Van Damme A. , 1986 .

[40]  A. Neuberger,et al.  A simple method for the preparation of an affinity absorbent for soybean agglutinin using galactosamine and CH-Sepharose. , 1975 .

[41]  P. Rougé,et al.  Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes. , 2008, Molecular immunology.

[42]  D. Laune,et al.  Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding. , 2002, Journal of immunological methods.

[43]  K. Roux,et al.  Ana o 2, a Major Cashew (Anacardium occidentale L.) Nut Allergen of the Legumin Family , 2003, International Archives of Allergy and Immunology.