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Titolo:
Structural and immunological characteristics of a 28-kilodalton cruzipain-like cysteine protease of Paragonimus westermani expressed in the definitive host stage
Autore:
Yun, DH; Chung, JY; Chung, YB; Bahk, YY; Kang, SY; Kong, Y; Cho, SY;
Indirizzi:
Sung Kyun Kwan Univ, Sch Med, Sect Mol Parasitol, Dept Mol Cell Biol, Suwon 440746, South Korea Sung Kyun Kwan Univ Suwon South Korea 440746 , Suwon 440746, South Korea Chung Ang Univ, Coll Med, Dept Parasitol, Seoul 156756, South Korea Chung Ang Univ Seoul South Korea 156756 sitol, Seoul 156756, South Korea
Titolo Testata:
CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY
fascicolo: 6, volume: 7, anno: 2000,
pagine: 932 - 939
SICI:
1071-412X(200011)7:6<932:SAICOA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUTRAL THIOL PROTEASE; CATHEPSIN-L; SCHISTOSOMA-MANSONI; ANTIBODY-RESPONSES; FASCIOLA-HEPATICA; IMMUNOGLOBULIN-G; PROTEINASES; SEQUENCE; CLONING; TREMATODE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Kong, Y Sung Kyun Kwan Univ, Sch Med, Sect Mol Parasitol, Dept Mol Cell Biol, Suwon 440746, South Korea Sung Kyun Kwan Univ Suwon South Korea 440746 440746, South Korea
Citazione:
D.H. Yun et al., "Structural and immunological characteristics of a 28-kilodalton cruzipain-like cysteine protease of Paragonimus westermani expressed in the definitive host stage", CL DIAG LAB, 7(6), 2000, pp. 932-939

Abstract

A complete cDNA sequence encoding a 28-kDa cruzipain-like cysteine protease of adult Paragonimus westermani, termed Pw28CCP, was isolated from an adult cDNA library, The cDNA contained a single open reading frame of 975 bp encoding 325 amino acids, which exhibited the structural motif and domain organization characteristic of cysteine proteases of non-cathepsin Bs including a hydrophobic signal sequence, an ERFNIN motif, and essential cysteine residues as well as active sites in the mature catalytic region, Analysis ofits phylogenetic position revealed that this novel enzyme belonged to the cruzipain-like cysteine proteases. The sequence of the first 13 amino acidspredicted from the mature domain of Pw28CCP was in accord with that determined from the native 28-kDa enzyme purified from the adult worm. Expressionof Pw28CCP was observed specifically in juvenile and adult worms, with a location in the intestinal epithelium, suggesting that this enzyme could be secreted and involved in nutrient uptake and immune modulation. The recombinant protein expressed in Escherichia coli was used to assess antigenicity by immunoblotting with sera from patients with active paragonimiasis and from those with other parasitic infections. The resulting sensitivity of 86.2% (56 of 65 samples) and specificity of 98% (147 of 150 samples) suggest its potential as an antigen for use in immunodiagnosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 09:56:30