Immunochemical characterization of a high molecular weight basic allergen (HMBA) of rye grass (Lolium perenne) pollen

Mol Immunol. 1983 Apr;20(4):465-73. doi: 10.1016/0161-5890(83)90027-5.

Abstract

A high molecular weight basic allergen (HMBA) was isolated from the mixture of non-dialysable components of the aqueous extract of defatted rye grass pollen by a combination of gel filtration and isoelectrofocusing, HMBA, a glycoprotein of mol. wt 56,800 (17% carbohydrate) contained all naturally occurring amino acids. A hyperimmune rabbit anti-HMBA serum gave only a single precipitin band with the crude extract of the rye grass pollen in crossed immunoelectrophoresis. Thus, it was concluded that HMBA was a unique and highly purified antigen. The allergenicity of HMBA was revealed by its ability to elicit immediate skin reactions in grass allergic patients. Moreover, all patients' sera tested had IgE antibodies to HMBA detectable by direct RAST with HMBA allergosorbent discs. These observations indicated that HMBA was a major allergenic constituent of rye grass pollen. Treatment of HMBA by 6 M guanidine HCl led to a significant reduction in its ability to combine with human IgE antibodies. The treatment also resulted in the complete loss of allergenicity (i.e. inability to elicit PCA reactions with a murine reaginic antiserum to HMBA) and antigenicity (inability to form precipitins with rabbit anti-HMBA); hence, it would appear that the allergenic and antigenic determinants of HMBA are 'conformational'.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Antibodies / immunology
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • Guanidine
  • Guanidines / pharmacology
  • Immunoelectrophoresis, Two-Dimensional
  • Immunoglobulin E / immunology
  • Molecular Weight
  • Poaceae / immunology
  • Pollen / immunology*
  • Radioallergosorbent Test

Substances

  • Amino Acids
  • Antibodies
  • Guanidines
  • Immunoglobulin E
  • Guanidine