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Titolo:
Hypoallergenic variants of the Parietaria judaica major allergen Par j 1: A member of the non-specific lipid transfer protein plant family
Autore:
Bonura, A; Amoroso, S; Locorotondo, G; Di Felice, G; Tinghino, R; Geraci, D; Colombo, P;
Indirizzi:
CNR, Ist Biol Sviluppo, I-90146 Palermo, Italy CNR Palermo Italy I-90146CNR, Ist Biol Sviluppo, I-90146 Palermo, Italy Ist Super Sanita, I-00161 Rome, Italy Ist Super Sanita Rome Italy I-00161 st Super Sanita, I-00161 Rome, Italy Osped Civ, Unita Allergol, Palermo, Italy Osped Civ Palermo ItalyOsped Civ, Unita Allergol, Palermo, Italy
Titolo Testata:
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY
fascicolo: 1, volume: 126, anno: 2001,
pagine: 32 - 40
SICI:
1018-2438(200109)126:1<32:HVOTPJ>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
DUST-MITE ALLERGEN; SITE-DIRECTED MUTAGENESIS; GRASS-POLLEN ALLERGEN; IGE-BINDING; INTERLEUKIN-4 PRODUCTION; OFFICINALIS POLLEN; DISULFIDE BONDS; CDNA CLONING; BEE VENOM; T-CELLS;
Keywords:
Parietaria judaica; Par j 1 recombinant allergen; hypoallergenic recombinant Par j 1 mutants; skin prick test; immunoglobulin E; peripheral blood mononuclear cell proliferation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Colombo, P CNR, Ist Biol Sviluppo, Via Ugo La Malfa 153, I-90146 Palermo, Italy CNR Via Ugo La Malfa 153 Palermo Italy I-90146 Palermo, Italy
Citazione:
A. Bonura et al., "Hypoallergenic variants of the Parietaria judaica major allergen Par j 1: A member of the non-specific lipid transfer protein plant family", INT A AL IM, 126(1), 2001, pp. 32-40

Abstract

Background. Par j 1 represents a major allergenic component of Parietaria judaica (Pj) pollen, since it is able to induce an immunoglobulin E (IgE) response in 95% of Pj-allergic patients. It belongs to the non-specific lipid transfer protein family, sharing with them a common three-dimensional structure. Methods: Disulphide bond variants of the recombinant Par j 1 (rParj1) allergen were generated by site-directed mutagenesis, and the immunological activity of rPar j 1 and its conformational mutants was compared with the use of the skin prick test (SPT). The ability to bind IgE antibodies was evaluated by Western blot, ELISA and ELISA inhibition. T cell reactivity was measured by peripheral blood mononuclear cell proliferation assay. Results: The disruption of Cys14-Cys29 and Cys30-Cys75 bridging (PjA mutant) caused the loss of the majority of specific IgE-binding activity. Additional disruption of the Cys4-Cys52 bridge (PjC mutant) and the latter Cys50-Cys91bridge (PjD mutant) led to the abolition of IgE-binding activity. On the SPT, PjB (lacking the Cys4-Cys52 and Cys50-Cys91 bridges) was still capable of triggering a type 1 hypersensitive reaction in 9 out of 10 patients, andPjA in 3 out of 10 patients, while PjC and PjD did not show any SPT reactivity. All the mutants preserved their T cell reactivity. Conclusion: Recombinant hypoallergenic variants of the rPar j 1 allergen described herein mayrepresent a useful tool for improved immunotherapy. Copyright (C) 2001 S, Karger AG, Basel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 03:13:31