XI, a new major grass pollen allergen, is a member of a family of soybean trypsin inhibitor-related proteins
| Autor: | W.A. van Leeuwen, V. Brodard, D. R. Hoffman, R. C. Aalberse, W. Van Dijk, M. Grande, K. Mahieu, Carolien A. M. Koeleman, R. van Ree |
|---|---|
| Přispěvatelé: | Other departments |
| Rok vydání: | 1995 |
| Předmět: |
Molecular Sequence Data
Immunology medicine.disease_cause Allergen immune system diseases Lolium otorhinolaryngologic diseases medicine Humans Immunology and Allergy Amino Acid Sequence Polyacrylamide gel electrophoresis Peptide sequence Glycoproteins Plant Proteins Gel electrophoresis Binding Sites Sequence Homology Amino Acid Edman degradation Molecular mass biology Kunitz STI protease inhibitor Chemistry Monosaccharides food and beverages Allergens Antigens Plant Immunoglobulin E Proteinase K respiratory tract diseases Biochemistry biology.protein Pollen Trypsin Inhibitor Kunitz Soybean Sequence Analysis |
| Zdroj: | Journal of allergy and clinical immunology, 95(5 Part 1), 970-978. Mosby Inc. |
| ISSN: | 0091-6749 |
| Popis: | Background: Monoclonal antibodies were obtained against an unknown allergen from Lolium perenne grass pollen. The allergen had an apparent molecular mass of 18 kd on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Earlier immunoblotting studies had shown that carbohydrate-specific IgG antibodies recognize an antigen of similar size. Objective: We sought to characterize the allergen biochemically and immunologically. Methods: The amino acid sequence of the allergen was determined by automated Edman degradation, and its monosaccharide composition was determined by gas chromatographic analysis. A panel of 270 grass pollen-positive sera was assessed in a RAST with the purified allergen. Protease digestion (proteinase K) and chemical deglycosylation (trifluoromethane sulfonic acid) were used to distinguish between carbohydrate and peptide epitopes for IgE antibodies. Results: The allergen was shown to be a glycoprotein with a molecular mass of 16 kd, of which 8% is carbohydrate. Its amino acid sequence shares 32% homology with soybean trypsin inhibitor (Kunitz) but lacks its active site. No homology was found with known grass pollen allergens, hence it was designated Lol p XI. A high degree of homology (44%) was found with a tree pollen allergen, Ole e I, the major allergen of olive pollen. More than 65% of grass pollen-positive sera had IgE against Lol p XI. IgE reactivity was demonstrated both with the carbohydrate moiety and the peptide backbone. Conclusions: Lol p XI is a new major grass pollen allergen carrying an IgE-binding carbohydrate determinant. Lol p XI is structurally related to the major allergen from olive pollen. (J ALLERGY CLIN IMMUNOL 1995;95:970-8.) |
| Databáze: | OpenAIRE |
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