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Titolo:
Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa
Autore:
Folders, J; Tommassen, J; van Loon, LC; Bitter, W;
Indirizzi:
Univ Utrecht, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3584 CH 3584 CH Utrecht, Netherlands Univ Utrecht, Inst Biomembranes, NL-3584 CH Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3584 CH 3584 CH Utrecht, Netherlands Univ Utrecht, Dept Plant Ecol & Evolut Biol, NL-3584 CH Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3584 CH 3584 CH Utrecht, Netherlands
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 5, volume: 182, anno: 2000,
pagine: 1257 - 1263
SICI:
0021-9193(200003)182:5<1257:IOACPS>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
GRAM-NEGATIVE BACTERIA; ESCHERICHIA-COLI; BORDETELLA-PERTUSSIS; ANTIFUNGAL ACTIVITY; OUTER-MEMBRANE; LASA PROTEASE; ELASTASE; GENE; PROPEPTIDE; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Bitter, W Univ Utrecht, Dept Mol Microbiol, Padualaan 8, NL-3584 CH Utrecht, Netherlands Univ Utrecht Padualaan 8 Utrecht Netherlands NL-3584 CH erlands
Citazione:
J. Folders et al., "Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa", J BACT, 182(5), 2000, pp. 1257-1263

Abstract

One of the major proteins secreted by Pseudomonas aeruginosa is a 43-kDa protein, which is cleaved by elastase into smaller fragments, including a 30-kDa and a 23-kDa fragment. The N-terminal 23-kDa fragment was previously suggested as corresponding to a staphylolytic protease and was designated LasD (S. Park and D. R. Galloway, Mel. Microbiol. 16:263-270, 1995). However,the sequence of the gene encoding this 43-kDa protein revealed that the N-terminal half of the protein is homologous to the chitin-binding proteins CHB1 of Streptomyces olivaceoviridis and CBP21 of Serratia marcescens and tothe cellulose-binding protein p40 of Streptomyces halstedii, Furthermore, a short C-terminal fragment shows homology to a part of chitinase A of Vibrio harveyi. The full-length 43-kDa protein could bind chitin and was thereby protected against the proteolytic activity of elastase, whereas the degradation products did not bind chitin, The purified 43-kDa chitin-binding protein had no staphylolytic activity, and comparison of the enzymatic activities in the extracellular medium of a wild-type strain and a chitin-binding protein-deficient mutant indicated that the 43-kDa protein supports neitherchitinolytic nor staphylolytic activity. We conclude that the 43-kDa protein, which was found to be produced by many clinical isolates of P. aeruginosa, is a chitin-binding protein, and we propose to name it CbpD (chitin-binding protein D).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 19:56:07