Three-way regulation of cholera toxin production
نویسندگان
چکیده
منابع مشابه
production of pentameric cholera toxin b subunit in escherichia coli
cholera toxin b subunit (ctb) has been extensively studied as an immunogen, adjuvant, and inducer of oral tolerance in many investigations. production of ctb has been carried out in the bacterial, plant, insect and yeast expression systems. in this study the expression of the ctb containing a 6xhis-tagged was performed by escherichia coli (e.coli) m15. the yield of purified pentameric recombina...
متن کاملCholera Toxin
Vibrio cholerae, the causative agent of cholera, requires two coordinately regulated factors for full virulence: cholera toxin (CT), a potent enterotoxin, and toxin-coregulated pili (TCP), surface organelles required for intestinal colonization. The structural genes for CT are shown here to be encoded by a filamentous bacteriophage (designated CTXCP), which is related to coliphage Ml 3. The CTX...
متن کاملProduction and characterization of monoclonal antibodies to cholera toxin.
Monoclonal antibodies against cholera toxin were produced to obtain highly specific antisera to cholera toxin. Fifteen hybridoma cell lines producing monoclonal antibodies specific for the determinants of cholera toxin were derived from the fusion of mouse myeloma cells and spleen cells from mice immunized with cholera toxin. The cell lines were stabilized, examined for specific antibody produc...
متن کاملProduction of Pentameric Cholera Toxin B Subunit in Escherichia coli
Cholera toxin B subunit (CTB) has been extensively studied as an immunogen, adjuvant, and inducer of oral tolerance in many investigations. Production of CTB has been carried out in the bacterial, plant, insect and yeast expression systems. In this study the expression of the CTB containing a 6XHis-tagged was performed by Escherichia coli (E.coli) M15. The yield of purified pentameric recombina...
متن کاملThe three-dimensional crystal structure of cholera toxin.
The clinical manifestations of cholera are largely attributable to the actions of a secreted hexameric AB5 enterotoxin (choleragen). We have independently solved and refined the three-dimensional structure of choleragen at 2.5 A resolution. The structure of the crystalline toxin closely resembles that described for the heat-labile enterotoxin from Escherichia coli (LT) with which it shares 80% ...
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ژورنال
عنوان ژورنال: Genome Biology
سال: 2002
ISSN: 1474-760X
DOI: 10.1186/gb-2002-3-10-reports0056