Structural and immunological aspects of Polybia scutellaris Antigen 5

Comparative proteomic analysis of two wasps venom, Vespa tropica and Vespa affinis

“…Native Ag 5-like protein (Vesp ma 5) with IgE-binding ability in Vespa wasps was purified and characterized . Sequence analysis indicated that the protein had a 72.5e90.3% similarity to the members of the vespid Ag-5 family with the known primary structure (Pirpignani et al, 2002). Ag 5 from these insects shows varied extents of cross reactivity when tested with mouse polyclonal antibodies by enzyme immunoassay (King, 1987).…”

Current Advances in Immunological Studies on the Vespidae Venom Antigen 5: Therapeutic and Prophylaxis to Hypersensitivity Responses

“…King et al (1978) identified a protein of approximately 23 kDa of Dolichovespula maculata venom, naming it Antigen 5 (Ag 5) [ 45 ]. Since then, Antigen 5 has been frequently reported to be the most allergenic venom component in different species of social wasps, such as those belonging to the genus Dolichovespula , Vespa , Vespula , Polistes and Polybia [ 46 , 47 , 48 , 49 , 50 , 51 ]. Interestingly, Ag 5 also exhibits sequence homology with other proteins from various tissues, such as ant venoms, tomato leaf tobacco, mammalian testis proteins and human brain tumor [ 52 ].…”

From Molecular Cloning to Vaccine Development for Allergic Diseases

“…Naturally occurring variants of insect allergens could be also useful for specific immunotherapy. For example, the sting of Polybia scutellaris, a South American wasp, does not cause allergic symptoms, however it has been proven that its venom contain Antigen 5 (Poly s 5), an analogue of the allergen Pol s 5 [126,127]. In mice, Poly s 5 induced IgG antibodies that cross react with Pol a 5, but induced only minimal amounts of IgE and was poor inducer of basophil-mediator release.…”