IgE-binding proteins from pine (Pinus radiata D. Don) pollen: evidence for cross-reactivity with ryegrass (Lolium perenne)

Int Arch Allergy Appl Immunol. 1990;93(1):41-6. doi: 10.1159/000235277.

Abstract

A complex mixture of pine (Pinus radiata D. Don) pollen proteins are rapidly released into aqueous solutions. IgE-binding proteins have been identified in these extracts using combined SDS-PAGE immunoblotting techniques. These IgE-binding proteins were detected using atopic patient and commercial pooled human sera known to be high in ryegrass-specific IgE. Enzyme-immunoassay inhibition studies revealed that leached P. radiata pollen proteins could partially inhibit serum IgE binding to ryegrass RAST discs thus providing preliminary evidence for allergen cross-reactivity between these two unrelated species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Differentiation / metabolism*
  • Cross Reactions
  • Galectin 3
  • Humans
  • Immunoblotting
  • In Vitro Techniques
  • Molecular Weight
  • Plant Proteins / immunology
  • Pollen / immunology*
  • Secale / immunology
  • Trees*

Substances

  • Antigens, Differentiation
  • Galectin 3
  • Plant Proteins