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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. Since both cholera toxin and GM1 species can be tagged with a fluorescent tags, the mechanism of retrograde traffic can be monitored.
During infection, V. cholerae secretes cholera toxin (CT), a protein that causes profuse, watery diarrhea (known as "rice-water stool"). [33] [5] This cholera toxin contains 5 B subunits that plays a role in attaching to the intestinal epithelial cells and 1 A subunit that plays a role in toxin activity.
This toxin has the ability to disrupt electrolyte balance in intestinal epithelial cells which can lead to issues including severe diarrhea, which is known to be a common symptom of this toxin. [15] In addition to the cholera toxin, there are other virulence factors such as surface adhesins, which are essential in helping the bacteria to adhere ...
After their B subunit binds to receptors on the cell surface, the toxin is enveloped by the cell and transported inside either through clathrin-dependent endocytosis or clathrin-independent endocytosis. [21] The mechanism pathways for the four AB5 toxins: cholera toxin, pertussis toxin, shiga toxin, and subtilase cytotoxin.
V. cholerae is the most common pathogen that causes cholera. The gold standard for detecting cholera is through cultures of stool samples or rectal swabs. Identification is then done through microscopy or by agglutination of antibodies. [25] Cultures are done in thiosulfate citrate bile-salts sucrose agar. V cholerae will form yellow colonies. [26]
The cholera toxin (CTX or CT) is an oligomeric complex made up of six protein subunits: a single copy of the A subunit (part A), and five copies of the B subunit (part B), connected by a disulfide bond. The five B subunits form a five-membered ring that binds to GM1 gangliosides on the surface of the
In addition to its effects on chloride secretion, which involve the same steps as the effects of cholera toxin, Elt binds additional substrates: lipopolysaccharide on the surface of E. coli cells and A-type blood antigens. [2] The importance of these binding events is not yet known.
CTXφ is generally present and integrated into the genome of the V. cholerae bacterium, and more rarely in a virion from outside the bacterium. While integrated into the bacterial genome, CTX prophages are found on each of the two chromosomes (in the O1 serogroup of V. cholerae) or arranged in tandem on the larger chromosome (in the El Tor biotype of V. cholerae). [2]