Wheat and barley allergens associated with baker's asthma. Glycosylated subunits of the alpha-amylase-inhibitor family have enhanced IgE-binding capacity

Biochem J. 1992 Jan 15;281 ( Pt 2)(Pt 2):401-5. doi: 10.1042/bj2810401.

Abstract

A 16 kDa protein, designated CM16*, which strongly binds IgE from baker's-asthma patients has been identified as a glycosylated form of the previously reported WTAI-CM16, which is a subunit of the wheat tetrameric alpha-amylase inhibitor. A glycosylated form (CMb*) of BTAI-CMb, the equivalent inhibitor subunit from barley, has been also found to have significantly enhanced IgE-binding capacity. In all, 14 purified members of the alpha-amylase/trypsin-inhibitor family showed very different IgE-binding capacities when tested by a dot-blot assay. The glycosylated components CM16*, CMb* and the previously described non-glycosylated 14.5 kDa allergen from barley (renamed BMAI-1) were found to be the strongest allergens.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / immunology*
  • Amino Acid Sequence
  • Asthma / immunology*
  • Electrophoresis, Polyacrylamide Gel
  • Glycosylation
  • Hordeum / immunology*
  • Immunoglobulin E / metabolism*
  • Molecular Sequence Data
  • Occupational Diseases / immunology*
  • Plant Proteins / immunology
  • Triticum / immunology*
  • alpha-Amylases / antagonists & inhibitors*

Substances

  • Allergens
  • Plant Proteins
  • Immunoglobulin E
  • alpha-Amylases