cholera/protease

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Interaction of the histone-like nucleoid structuring protein and the general stress response regulator RpoS at Vibrio cholerae promoters that regulate motility and hemagglutinin/protease expression.

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The bacterium Vibrio cholerae colonizes the human small intestine and secretes cholera toxin (CT) to cause the rice-watery diarrhea characteristic of this illness. The ability of this pathogen to colonize the small bowel, express CT, and return to the aquatic environment is controlled by a complex

Purification and characterization of an Aeromonas caviae metalloprotease that is related to the Vibrio cholerae hemagglutinin/protease.

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A zinc metalloprotease (AP34) from Aeromonas caviae was purified by ammonium sulfate precipitation and subsequent gel filtration through Sephadex G-100 and Sephadex G-50 Superfine. The molecular mass was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be 34 kDa. The

Expression of foreign proteins in a Vibrio cholerae vaccine strain using the stationary phase hemagglutinin/protease promoter.

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The use of the hemagglutinin(HA)/protease promoter and secretion signals to drive expression and secretion of a foreign antigen in a live genetically attenuated cholera vaccine candidate is demonstrated. A Vibrio cholerae vaccine strain, containing a HA/protease-tetanus toxin C fragment (TCF)

Characterization of two forms of hemagglutinin/protease produced by Vibrio cholerae non-O1.

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Two forms (34 kDa and 32 kDa) of hemagglutinin/protease produced by Vibrio cholerae non-O1 were characterized. The hemagglutinin/protease purified by immunoaffinity column chromatography using a monoclonal antibody was essentially a 34-kDa form. By incubation of the purified 34-kDa form at 37

Detection of virulence associated genes, haemolysin and protease amongst Vibrio cholerae isolated in Malaysia.

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Eighty-four strains of Vibrio cholerae O1, O139 and non-O1/non-O139 from clinical and environmental sources were investigated for the presence of the toxin co-regulated pilus gene, tcpA, the virulence cassette genes ctxA, zot, ace and cep and also for their ability to elaborate haemolysin and

Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation.

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The beta-domain of the Neisseria IgA protease precursor (Iga) provides the essential transport function for the protease across the outer membrane. To investigate the secretion function of the beta-domain (Iga beta), we engineered hybrid proteins between Iga beta and the non-toxic 12 kd cholera

[Membrane-bound proteases of ompT+ and ompT- Vibrio cholerae strains].

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OBJECTIVE Detection ofproteases in outer membranes (OM) of ompT+ and ompT- Vibrio cholerae strains of O1 and O139 serogroups. METHODS Specific sterile preparations of OM were obtained by lysis of live V. cholerae cells by 4.5 M urea solution with subsequent differential centrifugation and treatment

The effect on enterotoxicity of protease purified from Vibrio cholerae O1.

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The effect on enterotoxicity of protease purified from Vibrio cholerae O1 was investigated by the inoculation of live vibrio cells into protease-treated loops of the ileal loop model. Fluid accumulation ratios in the protease-treated loops were elevated in a dose-dependent manner by challenge with

Comparison of the Vibrio cholerae hemagglutinin/protease and the Pseudomonas aeruginosa elastase.

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The soluble hemagglutinin/protease (HA/protease) produced by Vibrio cholerae and the elastase of Pseudomonas aeruginosa are both zinc/calcium-dependent proteases. In the present study the two enzymes are compared immunologically and functionally. The N-terminal amino acid sequences of the proteins

Production of monoclonal antibodies against a hemagglutinin/protease of Vibrio cholerae non-01.

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Two hybridoma cell lines producing monoclonal antibodies (MAbs) against a hemagglutinin/protease (HA/P) from Vibrio cholerae non-01 were produced and characterized. The two MAbs contained the kappa light chain and were IgG1 type. They similarly neutralized HA/P protease activity derived from both V.

Cloning and nucleotide sequence of the Vibrio cholerae hemagglutinin/protease (HA/protease) gene and construction of an HA/protease-negative strain.

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The structural gene hap for the extracellular hemagglutinin/protease (HA/protease) of Vibrio cholerae was cloned and sequenced. The cloned DNA fragment contained a 1,827-bp open reading frame potentially encoding a 609-amino-acid polypeptide. The deduced protein contains a putative signal sequence

Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1.

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Haemaglutinin/protease (HA/P) is one of the virulence factors of Vibrio cholerae O1 and pathogenic strains of V. cholerae non-O1. In this study, we examined protease activity of a new serogroup of Vibrio cholerae recently designated as O139 synonym Bengal. The protease activity was produced by all

Isolation and characterization of protease-deficient mutants of vibrio cholerae.

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Mutants of Vibrio cholerae that were deficient in protease production were isolated by picking clones form gelatin or casein plates which showed reduced zones of proteolysis. All mutants showed reduced ability to degrade complex proteins (casein and gelatin), and those tested were deficient in

Effect of extracellular protease production on bacteriophage sensitivity of Vibrio cholerae.

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The effect of varying levels of extracellular protease production on the bacteriophage type of Vibrio cholerae 1621 serotype 01, biotype E1 Tor, has been investigated. It has been shown that the production of high levels of exoprotease can alter the apparent type of the strain by rendering it

Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain.

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Vibrio cholerae RTX is a large multifunctional bacterial toxin that causes actin crosslinking. Due to its size, it was predicted to undergo proteolytic cleavage during translocation into host cells to deliver activity domains to the cytosol. In this study, we identified a domain within the RTX toxin

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