YELLOW JACKET VENOM ALLERGENS, HYALURONIDASE AND PHOSPHOLIPASE - SEQUENCE SIMILARITY AND ANTIGENIC CROSS-REACTIVITY WITH THEIR HORNET AND WASP HOMOLOGS AND POSSIBLE IMPLICATIONS FOR CLINICAL ALLERGY

Three known allergens of yellow jacket (Vespula vulgaris) venom are an tigen 5, hyaluronidase, and phospholipase. Yellow jacket antigen 5 has been previously cloned and expressed in bacteria; it contains 204 ami no acid residues, and it has 69% and 60% sequence identities with the homologous proteins of white-faced hornet (Dolichovespula maculata) an d wasp (Polistes annularis), respectively. These studies are now exten ded to yellow jacket hyaluronidase and phospholipase; they contain 331 and 300 amino acid residues, respectively, and they show 92% and 67% sequence identity with their homologs of white-faced hornet. Tests wit h the natural and the recombinant vespid allergens in mice indicate pa rtial antigenic cross-reactivity of their homologous proteins at both B- and T-cell levels. There is greater cross-reactivity among hornet a nd yellow jacket allergens than that among hornet or yellow jacket and wasp allergens. The order of cross-reaction of the three vespid aller gens is hyaluronidase > antigen 5 > phospholipase. The continuous (lin ear) B-cell epitopes of vespid allergens show greater cross-reactivity than their discontinuous epitopes do. The discontinuous B-cell epitop es are immunodominant for all vespid allergens. The low degree of cros s-reactivity of the immunodominant discontinuous B-cell epitopes of ve spid allergens should be taken into consideration in selection of veno ms for immunotherapy of patients with sensitivity to multiple vespids.