Modified par j I allergen from P judaica pollen and its rate of absorption in rats

Immunol Lett. 1994 Apr;40(1):31-6. doi: 10.1016/0165-2478(94)90202-x.

Abstract

Polymerized allergens (allergoids) have been introduced in the immunotherapy of allergic disease in order to reduce the risk of side effects. However, their high molecular weight can be a limit, particularly when they are administered by a route involving passage through the mucosal barrier. We describe a simple procedure aimed at developing an original modified allergen with significantly less allergenic potential (intended as human IgE-binding capacity) but preserving the monomeric nature of the molecule. Par j I, the major allergen of Parietaria judaica pollen, was purified by a combination of monoclonal antibodies and affinity chromatography. Par j I allergen was then modified by reaction with potassium cyanate (KCNO), and compared with the native allergen to evaluate its allergenic potency (RAST-inhibition) and molecular weight (SDS-PAGE). Modified allergen showed significantly lower allergenic potency but kept its original molecular weight, making it particularly suitable for buccal (sublingual) administration. To study the adsorption profile, modified Par j I was radiolabeled and administered intravenously and sublingually to normal rats. The prospects for clinical application of the modified allergen are discussed.

Publication types

  • Comparative Study

MeSH terms

  • Absorption
  • Administration, Sublingual
  • Allergens / isolation & purification
  • Allergens / metabolism*
  • Animals
  • Antibodies, Monoclonal
  • Chromatography, Affinity
  • Glycoproteins / isolation & purification
  • Glycoproteins / metabolism*
  • Immunoglobulin E / immunology
  • Injections, Intravenous
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Plant Proteins*
  • Pollen / metabolism*
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Allergens
  • Antibodies, Monoclonal
  • Glycoproteins
  • Par j I protein, Parietaria judaica
  • Plant Proteins
  • Immunoglobulin E