3 research outputs found
Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa
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, Mol. 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 to the 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
neither chitinolytic 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)
Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa
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, Mol. 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 to the 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
neither chitinolytic 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)