Distribution of allergen activity and identification of the main IgE-binding glycopeptide of Parietaria judaica pollen

Int Arch Allergy Appl Immunol. 1985;76(2):156-61. doi: 10.1159/000233683.

Abstract

Parietaria judaica pollen extract was separated by preparative isoelectric focusing and showed two allergenic components (A1 and A2) heterogeneously distributed within the pH gradient (pH 3-10). By fused-rocket immunoelectrophoresis, A1 was detected from pH 3 to 10, whereas A2 was only found at pH values below 8. Both components, A1 and A2, showed IgE-binding ability throughout their pH ranges, as determined by crossed-radio immunoelectrophoresis. In addition, all the preparative isoelectric focusing fractions contained the main allergenic polypeptide of P. judaica (Pj10) when analyzed by SDS-PAGE. This polypeptide was shown to be a glycopeptide or to be bound to a glycoprotein with alpha-D-mannopyranoside or alpha-D-glycopyranoside residues. Implication of charged sugar residues in the wide distribution of P. judaica allergens in a pH gradient is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / analysis*
  • Binding Sites, Antibody
  • Chemistry Techniques, Analytical
  • Concanavalin A / immunology
  • Glycopeptides / analysis*
  • Immunoglobulin E / immunology*
  • Isoelectric Focusing
  • Plant Extracts / immunology*

Substances

  • Allergens
  • Glycopeptides
  • Plant Extracts
  • Concanavalin A
  • Immunoglobulin E