Allergens in Hymenoptera venom XIV: IgE binding activities of venom proteins from three species of vespids

J Allergy Clin Immunol. 1985 May;75(5):606-10. doi: 10.1016/0091-6749(85)90037-5.


RAST disks were prepared with purified proteins from the venoms of Vespula squamosa, Dolichovespula maculata, and Polistes exclamans and tested against a panel of sera obtained from patients allergic to each of the venoms. By the use of several criteria, IgE binding was strongest to antigen 5 of V. squamosa and phospholipase of P. exclamans. Hyaluronidase from Polistes had little IgE binding activity. All five proteins tested from D. maculata bound IgE antibodies strongly. Linear correlation analysis suggested that all of the proteins were distinct allergens in each of the venoms. A variety of patterns of response were observed for individual sera with each of the venoms.

MeSH terms

  • Allergens / immunology
  • Animals
  • Antibody Specificity
  • Bee Venoms / immunology*
  • Humans
  • Hyaluronoglucosaminidase / immunology
  • Immunoglobulin E / immunology
  • Molecular Weight
  • Phospholipases / immunology
  • Radioallergosorbent Test
  • Wasp Venoms / immunology*


  • Allergens
  • Bee Venoms
  • Wasp Venoms
  • Immunoglobulin E
  • Phospholipases
  • Hyaluronoglucosaminidase