Immunochemical studies of stinging insect venom allergens

• Published in: Toxicon (Oxford) Vol. 34; no. 11; pp. 1455 - 1458
• Main Author: King, T.P.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Oxford Elsevier Ltd 01.11.1996; Elsevier Science
• Subjects: Allergens - chemistry; Allergens - immunology; Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Animals; Arthropod Venoms - chemistry; Arthropod Venoms - immunology; Biological and medical sciences; Humans; Hymenoptera - chemistry; Hymenoptera - immunology; Immunochemistry; Insect Bites and Stings - immunology; Insect Bites and Stings - metabolism; Medical sciences; Mice; Molecular Sequence Data; Toxicology; Toxicity; Insecta; Sting; Apidae; Formicoidea; Structure activity relation; Apoidea; Cross reaction; Aminoacid sequence; Vespa; Aculeata; Immunopathology; Apis; Rodentia; Animal origin; Vertebrata; Mammalia; Immunogenicity; Mouse; Arthropoda; Animal; Venom; Vespidae; Hymenoptera; Invertebrata; Comparative study; Allergen; Structural analysis
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/S0041-0101(96)00088-8

Several major venom allergens from different insects of the Hymenoptera order have been cloned and sequenced by different laboratories. These insects include fire ants, honey bees, hornets, yellowjackets and wasps. These venom allergens have different biochemical functions, but have one feature in common, their varying extents of sequence identity with other proteins in our environment. Our studies in mice suggest that recombinant fragments containing regions of sequence identity of venom allergen(s) and host protein(s) show antigenic cross-reactivity. These studies lead to the hypothesis that cross-reactivity of venom allergens with host proteins promotes the immunogenicity of venom allergens in susceptible people.