Allergens in Hymenoptera venom XI. Isolation of protein allergens from Vespula maculifrons (yellow jacket) venom

Abstract

Pure Vespula maculifrons venom was demonstrated to contain five major allergenic proteins, which were all isolated from commercial venom sac extract. The five proteins: Vmacl, MW 97,000; hyaluronidase, MW 46,000; Vmac3, MW 39,000; phospholipase A and B, MW 34,000; and antigen 5, MW 22,000 were all demonstrated to be biochemically and immunologically distinct. All five proteins had significant allergenic activity, with phospholipase and hyaluronidase demonstrating the most IgE binding with 39 sera from allergic patients. Sera from honeybee-reactive patients, who had weak cross-reactions with yellow jacket venom, demonstrated strong IgE binding to purified V. maculifrons hyaluronidase and Vmacl. Dose-dependent inhibition of RAST was observed by use of honeybee hyaluronidase and high-molecular-weight fraction to inhibit the binding to the corresponding yellow jacket allergen.