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Titolo:
Identification and characterisation of two allergens from the dust mite Acarus siro, homologous with fatty acid-binding proteins
Autore:
Eriksson, TLJ; Whitley, P; Johansson, E; van Hage-Hamsten, M; Gafvelin, G;
Indirizzi:
Karolinska Hosp & Inst, Dept Clin Immunol, Stockholm, Sweden Karolinska Hosp & Inst Stockholm Sweden Clin Immunol, Stockholm, Sweden
Titolo Testata:
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY
fascicolo: 4, volume: 119, anno: 1999,
pagine: 275 - 281
SICI:
1018-2438(199908)119:4<275:IACOTA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLOMIA-TROPICALIS ALLERGEN; STORAGE MITES; HOUSE-DUST; DERMATOPHAGOIDES-PTERONYSSINUS; TYROPHAGUS-PUTRESCENTIAE; LEPIDOGLYPHUS-DESTRUCTOR; SENSITIZATION; REACTIVITY; SEQUENCE; WORKERS;
Keywords:
mite; allergen; Acarus siro; Aca s 13; cDNA cloning; protein expression; fatty acid-binding-protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Eriksson, TLJ Karolinska Hosp, Div Clin Immunol, S-17176 Stockholm, SwedenKarolinska Hosp Stockholm Sweden S-17176 Stockholm, Sweden
Citazione:
T.L.J. Eriksson et al., "Identification and characterisation of two allergens from the dust mite Acarus siro, homologous with fatty acid-binding proteins", INT A AL IM, 119(4), 1999, pp. 275-281

Abstract

Background: Dust mites are a major cause of allergic disease worldwide. The dust mite Acarus sire is an inducer of occupational allergy among farmers, but sensitisation has also been found in non-farming populations. Methods: A degenerate primer was designed to the N-terminal amino acid sequence ofa 15-kD IgE-binding protein in A. siro extract. The cDNA sequence was obtained by using reverse transcriptase polymerase chain reaction, standard cloning and sequencing techniques. The protein was expressed in Escherichia coli with a 6-histidine tag at its C-terminus. Immunoblotting of the recombinant protein and whole extract was performed using patient sera. Results andconclusion: 15 and 17-kD allergens were identified in a fraction of A, sire extract. The cDNA of the 15-kD allergen was isolated, cloned and sequenced and the allergen was expressed as a recombinant protein. The calculated molecular weight of the cDNA-encoded protein is 14.2 kD. The predicted aminoacid sequence has one potential N-glycosylation site at position 4-6 and acytosolic fatty acid-binding protein signature at position 5-22. The protein has 64% sequence identity with Blo t 13, an allergen from the dust mite Blomia tropicalis, as well as homology with several other fatty acid-binding proteins (FABPs) from different organisms. The allergen was named Aca s 13 and was recognised strongly by 3 of 13 (23%) of the subjects investigated. The amino acid sequence of the 17-kD protein was partly determined and italso showed high sequence homology with Blo t 13 and FABPs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:36:03