Structural and immunological aspects of Polybia scutellaris Antigen 5

• 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.

Keyword

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

Publication and Content Type

ref (subject category)

art (subject category)