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Titolo:
MAPPING OF IGE-BINDING EPITOPES ON THE RECOMBINANT MAJOR GROUP-I ALLERGEN OF VELVET GRASS-POLLEN, RHOL-I-1
Autore:
SCHRAMM G; BUFE A; PETERSEN A; HAAS H; SCHLAAK M; BECKER WM;
Indirizzi:
FORSCHUNGSZENTRUM BORSTEL,DIV ALLERGOL,PK ALLEE 22 D-23845 BORSTEL GERMANY
Titolo Testata:
Journal of allergy and clinical immunology
fascicolo: 6, volume: 99, anno: 1997,
parte:, 1
pagine: 781 - 787
SICI:
0091-6749(1997)99:6<781:MOIEOT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOL-P-I; V ALLERGENS; RYE GRASS; EXPRESSION; PROTEINS; CLONING; NITROCELLULOSE; GENE; DNA;
Keywords:
GROUP I ALLERGENS; VELVET GRASS POLLEN; RECOMBINANT ALLERGENS; B-CELL EPITOPE MAPPING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
G. Schramm et al., "MAPPING OF IGE-BINDING EPITOPES ON THE RECOMBINANT MAJOR GROUP-I ALLERGEN OF VELVET GRASS-POLLEN, RHOL-I-1", Journal of allergy and clinical immunology, 99(6), 1997, pp. 781-787

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. 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 I 1.Methods: We cloned Hot I 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. 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 (158to 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). 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 I 1 seem to contain continuous IgE-binding epitopes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 08:11:51