Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies

J Allergy Clin Immunol. 1996 Nov;98(5 Pt 1):969-78. doi: 10.1016/s0091-6749(96)80014-5.

Abstract

Background: Soybean and peanut are members of the legume family and share several common antigenic fractions. Patients allergic to one of these foods have serum IgE antibodies that immunologically cross-react with other legumes. Nevertheless, ingestion of other legumes generally does not induce an allergic reaction, suggesting that cross-reacting antibodies are not clinically relevant.

Objective: This study was designed to identify unique peanut or soybean antigenic fractions, with sera adsorbed to remove cross-reacting antibodies, thus resulting in sera with IgE antibodies unique to either soy or peanut.

Methods: Cross-reacting antibodies to soy were removed from the sera of two patients allergic to peanut and soy and three patients allergic to peanut by soy-affinity chromatography. Cross-reacting antibodies to peanut were adsorbed from the sera of a patient allergic to peanut and soy and a patient allergic to peanut by peanut-affinity chromatography. Adequate removal of cross-reacting antibodies was verified by ELISA after each adsorption step. Unadsorbed sera and sera adsorbed to remove cross-reacting antibodies (either to soy or to peanut) were assayed for specific IgE binding to peanut or soy immunoblots.

Results: Unique peanut-specific IgE antibodies (i.e., soy antibody-adsorbed) were found to bind to peanut fractions at 46, 29, 25, 19, 17, 14, and 5 kd on immunoblots of whole peanut protein. Similarly, unique soy-specific IgE (i.e., peanut antibody-adsorbed) were found to bind a fraction at 46 kd, and to a lesser extent, to a fraction at 21 kd on immunoblots of whole soy protein. The 73% reduction of IgE antibody binding to peanut by ELISA after adsorption of cross-reacting antibodies indicates extensive cross-reactivity between soy and peanut antigens.

Conclusions: Antigen-affinity chromatography is an effective method for removal of cross-reacting antibodies. We identified IgE antibody binding (with sera where cross-reacting antibodies were removed) to several unique antigenic fractions of peanut and soy. Further studies will determine the clinical significance of these fractions in IgE-mediated food hypersensitivity reactions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adsorption
  • Allergens / immunology
  • Allergens / isolation & purification*
  • Arachis / immunology*
  • Chromatography, Affinity
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Fabaceae / immunology
  • Food Hypersensitivity / blood
  • Food Hypersensitivity / immunology*
  • Glycine max / immunology*
  • Humans
  • Immune Sera / immunology*
  • Immunoglobulin E / blood
  • Immunoglobulin E / immunology
  • Immunoglobulin E / isolation & purification*
  • Plant Extracts / immunology
  • Plant Proteins / blood
  • Plant Proteins / immunology
  • Plant Proteins / isolation & purification*
  • Plants, Medicinal

Substances

  • Allergens
  • Immune Sera
  • Plant Extracts
  • Plant Proteins
  • Immunoglobulin E