Structural and immunological aspects of Polybia scutellaris Antigen 5
2002 (English)In: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 407, no 2, 224-230 p.Article in journal (Refereed) Published
Vespid venoms contain Antigen 5, an important allergen whose primary structure and immunological behavior have been extensively studied from venoms of vespids of the Northern Hemisphere. We report herein structural and immunological aspects of Antigen 5 from Polybia scutellaris subspecies rioplatensis (vulgar name: camoati) found in South America. Mast cell degranulation, histamine release, and IgE induction experiments performed in mice allow us to suggest that P. scutellaris Antigen 5 is a variant with reduced IgE response and anaphylactic activity. Sequence data indicate that the protein has a 72.5-90.3% similarity to that of members of the vespid Antigen 5 family with an already known primary structure. Moreover, results suggest that the protein-a new member of an extracellular protein superfamily-could be a good candidate for immunotherapy related to vespid allergy.
Place, publisher, year, edition, pages
2002. Vol. 407, no 2, 224-230 p.
Allergens/*chemistry/*immunology, Amino Acid Sequence, Animals, Antigens/*chemistry/*immunology, Cell Degranulation, Cysteine/metabolism, Glycosylation, Histamine Release, Immunoglobulin E/biosynthesis, Male, Mast Cells/immunology, Mice, Mice; Inbred BALB C, Molecular Sequence Data, Oxidation-Reduction, Protein Structure; Secondary, Rats, Rats; Sprague-Dawley, Sequence Alignment, Wasp Venoms/*chemistry/*immunology, Wasps/*immunology
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-10402DOI: 10.1016/S0003-9861(02)00554-4PubMedID: 12413495OAI: oai:DiVA.org:uu-10402DiVA: diva2:38170