? lectin purified from Vibrio cholerae 01

Sasmal, D.

doi:10.1016/0378-1097(92)90159-l

Cited by 7 publications

(8 citation statements)

References 5 publications

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“…The filamentous hemagglutinin of B. pertussis and pertussis toxin contain carbohydrate recognition domains critical for binding to glycoconjugates on cell membranes (41,49). One of the hemagglutinins of V. cholerae has been reported to be specific for N-acetyl-Dglucosamine, the monomeric subunit of chitin, and mediates binding of the bacterial cells to rabbit intestinal epithelial cells (44). Furthermore, it has been shown that Klebsiella pneumoniae is internalized efficiently by cultured human epithelial cells, presumably via an N-glycosylated receptor containing N-acetyl-glucosamine residues (13).…”

Section: Discussionmentioning

confidence: 99%

Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa

Folders

Tommassen²,

Loon

et al. 2000

J Bacteriol

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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).The opportunistic pathogen Pseudomonas aeruginosa is able to secrete many proteins, including the exoenzymes S, T, and U, exotoxin A, lipase, phospholipase C, the proteases alkaline protease and elastase (LasB), and the staphylolytic proteases LasA and LasD, into the extracellular medium. Most of these proteins contribute to the virulence of the bacteria, as they are associated with epithelial cell and tissue damage or disfunctioning of infected host cells. These proteins are secreted across the bacterial cell envelope by three entirely different mechanisms. Exoenzymes S, T, and U are secreted by a type III secretion system and are actually injected directly into eukaryotic target cells (12,51). Alkaline protease is secreted by a type I secretion machinery (8). The other proteolytic enzymes mentioned above and exotoxin A are secreted via the type II secretion pathway, encoded by the xcp genes (for a review, see reference 11). The major proteolytic enzyme, elastase, is synthesized as a preproenzyme in the cytosol. During or directly after translocation across the cytoplasmic membrane, the signal sequence is removed, and the proenzyme is folded in a process that requires the propeptide as an intramolecular chaperone (5, 35). After autoproteolytic processing, the propeptide remains noncovalently associated with the mature enzyme and inhibits enzymatic activity in the periplasm (27, 34). The propeptide dissociates from the enzyme only after translocation across the outer membrane (6). LasA, a staphylolytic protease, is synthesized as a preproenzyme of 42 kDa and is processed into a 21-kDa mature protein ...

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Section: Discussionmentioning

confidence: 99%

Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa

Folders

Tommassen²,

Loon

et al. 2000

J Bacteriol

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“…Adhesive OMPs were shown to occur in Vibrio cholerae, 106 Aeromonas hydrophila, 107,108 Campylobacter jejuni, 109 Bartonella henselae, 110 Rickettsia rickettsii, 111 Salmonella typhimurium, 112 in enteroaggregative strains of Escherichia coli, 113 and in members of the Pasteurellaceae family. 114 By using the two-dimensional PAGE technique, De Mot and Vanderleyden 115 showed that a 33-kDa major outer membrane protein Critical Reviews in Microbiology Downloaded from informahealthcare.com by University of Memphis on 10/14/12…”

Section: Possible Involvement Of Outer Membrane Proteins (Omps) mentioning

confidence: 99%

Surface Characteristics ofAzospirillum brasilensein Relation to Cell Aggregation and Attachment to Plant Roots

Burdman

Okon

Jurkevitch

2000

Critical Reviews in Microbiology

116

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The free-living bacteria of the genus Azospirillum live in close association with plant roots and represent one of the best-characterized plant growth promoting rhizobacteria (PGPR). The attachment of Azospirillum to the roots is essential for the establishment of an efficient association with the host plant. Azospirillum cells are able to aggregate under certain environmental conditions, leading to the formation of bacterial flocs. The bacterial surface plays an important role in the establishment of the bacteria-plant association as well as in the bacterial aggregation and data suggesting the involvement of extracellular polysaccharides and proteins in these phenomena have been published. This review summarizes the current knowledge on the involvement of surface components in the adhesion processes of Azospirillum. Emphasis is placed on A. brasilense, the species that has been the subject of most studies in the Azospirillum genus.

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“…In both cases, these MOMPs were proposed to play a role in attachment and colonization of plant roots by the producing bacteria. Adhesive OMPs (generally porins) occur in Vibrio cholerae (Sasmal et al, 1992), Aeromonas hydrophila (Quinn & Flower, 1995;Lee et al, 1997) and in an enteroaggregative strain of Escherichia coli (Debroy et al, 1995). Porins were shown to be involved in the invasion of epithelial cells by Salmonella typhimurium (Dorman et al, 1989) and Shigella flexneri (Bernardini et al, 1993).…”

Section: Involvement Of Omps In Aggregationmentioning

confidence: 99%

Involvement of outer-membrane proteins in the aggregation of Azospirillum brasilense

et al. 1999

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A bioassay was developed t o investigate biological factors involved in the aggregation of Azospirillum brasilense strain Cd. Cells were grown for 24 h under aggregation-inducing and non-aggregation-inducing conditions (high and low C:N, respectively) and sonicated for 20 s. The cells were washed by centrifugation and resuspended in potassium phosphate buffer containing the two types of sonication extract. A greater extent of aggregation and higher flocculation were observed after 2-3 h incubation in the presence of sonicates from cells grown a t high C:N (H-cells) compared to cells grown at low C:N. Flocculation did not occur after incubation of these cells in phosphate buffer. Boiled or proteinase K-treated sonicates originating from H-cells had lower aggregation-inducing capacity. After fractionation of the crude sonicate, both the outer-membrane protein (OMP) and the total membrane (mostly OMP) fractions possessed relatively high aggregation specific activities. The aggregation-inducing capacity of the OMP fraction strongly correlated with its protein concentration in the bioassay. Treatment of this fraction with proteinase K also decreased its aggregation-inducing activity. These findings suggest that OMPs are involved in the aggregation process of cells of A. brasilense.1

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? lectin purified from Vibrio cholerae 01

Cited by 7 publications

References 5 publications

Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa

Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa

Surface Characteristics ofAzospirillum brasilensein Relation to Cell Aggregation and Attachment to Plant Roots

Involvement of outer-membrane proteins in the aggregation of Azospirillum brasilense

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