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Titolo:
IgE binding capacity of synthetic and recombinant peptides of the major storage mite (Lepidoglyphus destructor) allergen, Lep d 2
Autore:
Elfman, LHM; Whitley, P; Schmidt, M; van Hage-Hamsten, M;
Indirizzi:
Karolinska Hosp, Dept Lab Med, Div Clin Immunol, S-17176 Stockholm, SwedenKarolinska Hosp Stockholm Sweden S-17176 unol, S-17176 Stockholm, Sweden Karolinska Inst, S-17176 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17176 Inst, S-17176 Stockholm, Sweden E Carolina Univ, Dept Phys, Greenville, NC 27858 USA E Carolina Univ Greenville NC USA 27858 pt Phys, Greenville, NC 27858 USA
Titolo Testata:
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY
fascicolo: 3, volume: 117, anno: 1998,
pagine: 167 - 173
SICI:
1018-2438(199811)117:3<167:IBCOSA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
BIRCH POLLEN ALLERGEN; HOUSE-DUST MITES; DER-P-I; DERMATOPHAGOIDES-PTERONYSSINUS; MONOCLONAL-ANTIBODIES; FARMING POPULATION; F-I; BET-V-1; EPITOPE; FARINAE;
Keywords:
allergen; B-cell epitope; IgE; Lepidoglyphus destructor; mite;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Elfman, LHM Karolinska Hosp, Dept Lab Med, Div Clin Immunol, S-17176 Stockholm, Sweden Karolinska Hosp Stockholm Sweden S-17176 6 Stockholm, Sweden
Citazione:
L.H.M. Elfman et al., "IgE binding capacity of synthetic and recombinant peptides of the major storage mite (Lepidoglyphus destructor) allergen, Lep d 2", INT A AL IM, 117(3), 1998, pp. 167-173

Abstract

Background: Lepidoglyphus destructor is an important non-pyroglyphid mite species in Europe and a dominant allergen in fanning environments. The major allergen of L. destructor, Lep d 2, is a protein of 13.2 kD that is recognised by about 90% of sera RAST positive to this mite species. Methods: ThecDNA of two isoallergens of the Lep d 2 has previously been sequenced and the protein expressed in different protein expression systems. In order to map the B-cell epitopes, the full length protein and the truncated forms ofthe protein have been expressed in Escherichia coli as glutathione-S-transferase (GST) fusion proteins. Recombinant Lep d 2 fragments and synthetic overlapping 15 mer peptides spanning Lep d 2 were probed with sera from patients allergic to storage mite. Results: The full-length (125 amino acids) GST fusion protein reacted strongly with patient IgE in Western blots and dot blots. Synthetic peptides failed to react with IgE antibodies from mite-allergic patients and the truncated fusion proteins displayed weak IgE-binding capacity. Conclusion: We conclude that there are no dominant linear IgE-binding epitopes in Lep d 2. Recombinant or synthetic Lep d 2 fragments may, however, be further evaluated as hypoallergenic candidate molecules for specific immunotherapy.

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Documento generato il 22/10/20 alle ore 03:31:20