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Characterization of the major allergens purified from the venom of the paper wasp Polistes gallicus.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2003 Oct 13; Vol. 1623 (2-3), pp. 72-81. - Publication Year :
- 2003
-
Abstract
- Allergic reactions to vespid stings are one of the major causes of IgE-mediated anaphylaxis. Vespa and Vespula venoms are closely related; Polistes venom is more distantly related and its allergens are less well studied. There is limited cross-reactivity between Polistes and the other vespid venoms because of differences in the epitopes on the allergen molecules. In this study, the major allergens of Polistes gallicus are isolated and characterized. P. gallicus venom contains four major allergens: phospholipase, antigen 5 (Ag5), hyaluronidase and protease that were characterized by mass spectrometry and specific binding to IgE. The complete amino acid sequence of Ag5 and the sequence of the N-terminal region of phospholipase were also determined. The alignment of Ag5 from P. gallicus (European species) and Polistes annularis (American species) shows an 85% identity that increases to 98% within the same subgenus. This could suggest the presence of specific epitopes on Ag5 molecule being the variations on the superficial loops. The features of the P. gallicus allergens could explain the partial cross-reactivity found between the American and European Polistes venoms, and suggest that the use of European Polistes venoms would improve the diagnostic specificity and the therapy of European patients and of North American patients sensitized by European Polistes.
- Subjects :
- Allergens genetics
Allergens isolation & purification
Amino Acid Sequence
Anaphylaxis etiology
Animals
Cross Reactions
Humans
Hypersensitivity, Immediate diagnosis
Hypersensitivity, Immediate etiology
Models, Molecular
Molecular Sequence Data
Phylogeny
Protein Conformation
Species Specificity
Wasp Venoms genetics
Wasp Venoms isolation & purification
Wasps genetics
Wasps immunology
Allergens chemistry
Wasp Venoms immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1623
- Issue :
- 2-3
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 14572904
- Full Text :
- https://doi.org/10.1016/j.bbagen.2003.07.001