In:
eLife, eLife Sciences Publications, Ltd, Vol. 4 ( 2015-10-29)
Abstract:
Cholera is a serious diarrheal disease that can be deadly if left untreated. It is caused by eating food, or drinking water, contaminated by the bacterium Vibrio cholerae. This bacterium can survive passage through the acidic conditions of the stomach. Inside the small intestine, V. cholerae attaches to the intestinal wall and starts producing cholera toxin. The toxin enters intestinal cells, causing them to release water and ions, including sodium and chloride ions. The salt-water environment created inside the intestine can, by osmosis, draw up to a further six liters of water into the intestine each day. This results in the copious production of watery diarrhea and severe dehydration. Cholera toxin is composed of six protein subunits, including five copies of cholera toxin subunit B (CTB). CTB subunits help the uptake of the toxin by intestinal cells, and it has long been reported that CTB subunits attach to intestinal cells by binding to a cell surface molecule called GM1. CTB subunits have a high affinity for GM1, yet recent work suggests CTB may not bind exclusively to GM1; one or more additional cell surface molecules may be directly involved in cholera toxin uptake. Wands et al. now reveal that numerous cell surface molecules are recognized by CTB, and that these molecules can assist cholera toxin uptake by host cells. Glycoproteins, proteins that are marked with sugar molecules, were shown to be the primary CTB binding sites on human colon cells, and it was the glycoprotein’s sugar component, not the protein itself, that interacted with CTB. Wands et al. discovered that in particular glycoproteins containing a sugar called fucose were largely responsible for CTB binding and toxin uptake. Together these findings reveal a previously unrecognized mechanism for cholera toxin entry into host cells, and suggest that fucose-containing or fucose-mimicking molecules could be developed as new treatments for cholera.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.09545.001
DOI:
10.7554/eLife.09545.002
DOI:
10.7554/eLife.09545.003
DOI:
10.7554/eLife.09545.004
DOI:
10.7554/eLife.09545.005
DOI:
10.7554/eLife.09545.006
DOI:
10.7554/eLife.09545.007
DOI:
10.7554/eLife.09545.008
DOI:
10.7554/eLife.09545.009
DOI:
10.7554/eLife.09545.010
DOI:
10.7554/eLife.09545.011
DOI:
10.7554/eLife.09545.012
DOI:
10.7554/eLife.09545.013
DOI:
10.7554/eLife.09545.014
DOI:
10.7554/eLife.09545.015
DOI:
10.7554/eLife.09545.016
DOI:
10.7554/eLife.09545.017
DOI:
10.7554/eLife.09545.018
DOI:
10.7554/eLife.09545.019
DOI:
10.7554/eLife.09545.020
DOI:
10.7554/eLife.09545.021
DOI:
10.7554/eLife.09545.022
DOI:
10.7554/eLife.09545.023
DOI:
10.7554/eLife.09545.024
DOI:
10.7554/eLife.09545.025
DOI:
10.7554/eLife.09545.026
DOI:
10.7554/eLife.09545.027
DOI:
10.7554/eLife.09545.028
DOI:
10.7554/eLife.09545.029
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2015
detail.hit.zdb_id:
2687154-3
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