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Mapping of IgE-binding epitopes on the recombinant major group I allergen of velvet grass pollen, rHol l 1.
- Source :
-
The Journal of allergy and clinical immunology [J Allergy Clin Immunol] 1997 Jun; Vol. 99 (6 Pt 1), pp. 781-7. - Publication Year :
- 1997
-
Abstract
- Background: New and more successful approaches to diagnosis and therapy of allergic diseases require a more subtle understanding of the structure and the epitopes on the allergen molecule.<br />Objective: This study was done to obtain more information on the structure and the IgE-binding epitopes of a major allergen of velvet grass pollen, Hol l 1.<br />Methods: We cloned Hol l 1 from a complementary DNA library and performed B-cell epitope mapping with 21 recombinant fragments expressed as fusion proteins in Escherichia coli. The fragments were analyzed by Western blotting with sera from 50 different patients.<br />Results: The patients' sera individually recognized at least four different IgE-binding regions (amino acids 1 to 27, 61 to 76, 84 to 105, and 158 to 240). According to their binding patterns with these epitopes, they were divided into five groups. Most sera (92%) bound to the C-terminal peptide (158 to 240), which consists of more than 80 amino acids, whereas there was virtually no binding to smaller fragments covering this region. In contrast to the C-terminal peptide, the IgE-binding peptides on the N terminus and on the middle region of the molecule were of a smaller size (15 to 30 amino acids).<br />Conclusions: The major group I allergen of velvet grass bears at least four different IgE-binding epitopes, which were individually recognized by sera from different patients. The C terminus represents the major IgE-binding region and contains at least one discontinuous IgE-binding epitope, whereas the N terminus and middle region of Hol l 1 seem to contain continuous IgE-binding epitopes.
- Subjects :
- Allergens biosynthesis
Allergens genetics
Amino Acid Sequence
Antigens, Plant
Base Sequence
DNA, Complementary isolation & purification
Epitopes, B-Lymphocyte chemistry
Glycoproteins biosynthesis
Glycoproteins genetics
Humans
Molecular Sequence Data
Peptide Fragments chemistry
Peptide Fragments genetics
Peptide Fragments immunology
Plant Proteins biosynthesis
Plant Proteins genetics
Poaceae chemistry
Poaceae immunology
Pollen immunology
Recombinant Proteins biosynthesis
Recombinant Proteins chemistry
Allergens chemistry
Binding Sites, Antibody
Epitope Mapping
Glycoproteins immunology
Immunoglobulin E metabolism
Plant Proteins immunology
Pollen chemistry
Recombinant Proteins immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0091-6749
- Volume :
- 99
- Issue :
- 6 Pt 1
- Database :
- MEDLINE
- Journal :
- The Journal of allergy and clinical immunology
- Publication Type :
- Academic Journal
- Accession number :
- 9215246
- Full Text :
- https://doi.org/10.1016/s0091-6749(97)80012-7