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Titolo:
Hev b 9, an enolase and a new cross-reactive allergen from Hevea latex andmolds - Purification, characterization, cloning and expression
Autore:
Wagner, S; Breiteneder, H; Simon-Nobbe, B; Susani, M; Krebitz, M; Niggemann, B; Brehler, R; Scheiner, O; Hoffmann-Sommergruber, K;
Indirizzi:
Univ Vienna, Dept Pathophysiol, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 t Pathophysiol, A-1090 Vienna, Austria Salzburg Univ, Dept Genet & Gen Biol, A-5020 Salzburg, Austria Salzburg Univ Salzburg Austria A-5020 Gen Biol, A-5020 Salzburg, Austria Adv Biosyst, Salzburg, Austria Adv Biosyst Salzburg AustriaAdv Biosyst, Salzburg, Austria Univ Childrens Hosp Charite, Virchow Clin, Berlin, Germany Univ Childrens Hosp Charite Berlin Germany irchow Clin, Berlin, Germany Univ Munster, Dept Dermatol & Venerol, Munster, Germany Univ Munster Munster Germany Dept Dermatol & Venerol, Munster, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 24, volume: 267, anno: 2000,
pagine: 7006 - 7014
SICI:
0014-2956(200012)267:24<7006:HB9AEA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST PICHIA-PASTORIS; NATURAL-RUBBER LATEX; CLASS-I CHITINASES; SACCHAROMYCES-CEREVISIAE; ASPERGILLUS-FUMIGATUS; CANDIDA-ALBICANS; SPINA-BIFIDA; IGE-BINDING; IDENTIFICATION; AVOCADO;
Keywords:
cross-reactivity; enolase; Hevea latex allergy; mold allergy; recombinant Hev b 9;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Hoffmann-Sommergruber, K Univ Vienna, Dept Pathophysiol, Waehringer Guertel 18-20,AKH EBO 3Q, A-1090 Vienna, Austria Univ Vienna Waehringer Guertel 18-20,AKH EBO 3Q Vienna Austria A-1090
Citazione:
S. Wagner et al., "Hev b 9, an enolase and a new cross-reactive allergen from Hevea latex andmolds - Purification, characterization, cloning and expression", EUR J BIOCH, 267(24), 2000, pp. 7006-7014

Abstract

Natural rubber latex allergy is an IgE-mediated disease that is caused by proteins that elute from commercial latex products. A complementary DNA (cDNA) coding for Hev b 9, an enolase (2-phospho-D-glycerate hydrolyase) and allergen from latex of the rubber tree Hevea brasiliensis, was amplified by PCR. The PCR primers were designed according to conserved regions of enolases from plants. The obtained cDNA amplification product consisted of 1651 bp and encoded a protein of 445 amino-acid residues with a calculated molecular mass of 47.6 kDa. Sequence comparisons revealed high similarities of the Hevea latex enolase to mold enolases that have been identified as important allergens. In addition, the crucial amino-acid residues that participatein the formation of the catalytic site and the Mg2+ binding site of enolases were also conserved. Hevea latex enolase was produced as a recombinant protein in Escherichia coli with an N-terminal hexahistidyl tag, and purified by affinity chromatography. The yield amounted to 110 mg of purified Hev b 9 per litre of bacterial culture. The recombinant allergen bound IgE fromlatex, as well as mold-allergic patients, in immunoblot and ELISA experiments. The natural enolase was isolated from Hevea latex by (NH4)(2)SO4 precipitation and ion exchange chromatography. The natural and the recombinant (r)Hev b 9 showed equivalent enzymatic activity. Patients' IgE-antibodies preincubated with rHev b 9 lost their ability to bind to natural (n) Hev b 9,indicating the identity of the B-cell epitopes on both molecules. Cross-reactivity with two enolases from Cladosporium herbarum and Alternaria alternata was determined by inhibition of IgE-binding to these enolases by rHev b9. Therefore, enolases may represent another class of highly conserved enzymes with allergenic potentials.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/07/18 alle ore 13:20:39