Cholera toxin is AB5 multimeric protein complex secreted by the bacterium Vibrio cholerae.
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Cholera toxin is AB5 multimeric protein complex secreted by the bacterium Vibrio cholerae.
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Cholera toxin was discovered in 1959 by Indian microbiologist Sambhu Nath De.
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Complete Cholera toxin is a hexamer made up of a single copy of the A subunit, and five copies of the B subunit, denoted as AB5.
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Once bound, the entire toxin complex is endocytosed by the cell and the cholera toxin A1 chain is released by the reduction of a disulfide bridge.
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Pertussis Cholera toxin produced by Bordetella pertussis acts in a similar manner with the exception that it ADP-ribosylates the Gai subunit, rendering it unable to inhibit cAMP production.
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Gene encoding the cholera toxin is introduced into V cholerae by horizontal gene transfer.
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Treatment of cultured rodent neural stem cells with cholera toxin induces changes in the localization of the transcription factor Hes3 and increases their numbers.
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Since cholera toxin has been shown to preferentially bind to GM1 gangliosides, this characteristic can be utilized for membrane studies.
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Cholera toxin has been shown to enter cells via endocytosis in multiple pathways.
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One of the most important aspects of cholera toxin is the retrograde traffic mechanism that transports the toxin from the cell membrane back to the trans-Golgi network and the endoplasmic reticulum.
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