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Titolo:
Unlocking the allergenic structure of the major house dust mite allergen Der f 2 by elimination of key intramolecular interactions
Autore:
Takai, T; Ichikawa, S; Yokota, T; Hatanaka, H; Inagaki, F; Okumura, Y;
Indirizzi:
Asahi Breweries Ltd, Biosci Res & Dev Lab, Ibaraki, Osaka 3020106, Japan Asahi Breweries Ltd Ibaraki Osaka Japan 3020106 aki, Osaka 3020106, Japan Tokyo Metropolitan Inst Med Sci, Dept Mol Physiol, Bunkyo Ku, Tokyo 1138613, Japan Tokyo Metropolitan Inst Med Sci Tokyo Japan 1138613 Tokyo 1138613, Japan Japan Womens Univ, Fac Sci, Dept Biol & Mat Sci, Bunkyo Ku, Tokyo 1128681,Japan Japan Womens Univ Tokyo Japan 1128681 ci, Bunkyo Ku, Tokyo 1128681,Japan Hokkaido Univ, Grad Sch Pharmaceut Sci, Div Struct Biol, Kita Ku, Sapporo,Hokkaido 0600812, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600812 poro,Hokkaido 0600812, Japan
Titolo Testata:
FEBS LETTERS
fascicolo: 2, volume: 484, anno: 2000,
pagine: 102 - 107
SICI:
0014-5793(20001103)484:2<102:UTASOT>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
BIRCH POLLEN ALLERGEN; DERMATOPHAGOIDES-FARINAE; RECOMBINANT ALLERGENS; IMMUNOGLOBULIN-E; IGE REACTIVITY; POTENTIAL USE; IMMUNOTHERAPY; DER-F-2; BET-V-1; EPITOPE;
Keywords:
allergen engineering; major house dust mite allergen; site-directed mutagenesis; conformational change; IgE-binding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Takai, T Asahi Breweries Ltd, Biosci Res & Dev Lab, 1-21,Midori 1 Chome, Ibaraki, Osaka 3020106, Japan Asahi Breweries Ltd 1-21,Midori 1 Chome Ibaraki Osaka Japan 3020106
Citazione:
T. Takai et al., "Unlocking the allergenic structure of the major house dust mite allergen Der f 2 by elimination of key intramolecular interactions", FEBS LETTER, 484(2), 2000, pp. 102-107

Abstract

We report on the structural background of the remarkable reduction of allergenicity in engineering of the major house dust mite allergen Der f 2, Disruption of intramolecular disulfide bonds in Der f 2 caused extensive conformational change that was monitored by circular dichroism and gelfiltrationanalysis. The degree of conformational change correlated tr ell with the degree of reductions in the capacity to bind IgE and to induce histamine release from basophils in mite-allergic patients, Loosening the rigid tertiarystructure by elimination of key intramolecular interactions is an effective strategy to reduce the number of high affinity IgE epitopes of allergen vaccine, (C) 2000 Federation of European Biochemical Societies. Published byElsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 11:21:58