Modifications of cholera toxin subunit B binding to human large intestinal epithelium: an immunohistochemical study
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Modifications of cholera toxin subunit B binding to human large intestinal epithelium : an immunohistochemical study. / Kirkeby, Svend; Pedersen, Anne Marie Lynge.
In: Microbial Pathogenesis, Vol. 124, 2018, p. 332-336.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Modifications of cholera toxin subunit B binding to human large intestinal epithelium
T2 - an immunohistochemical study
AU - Kirkeby, Svend
AU - Pedersen, Anne Marie Lynge
N1 - Copyright © 2018. Published by Elsevier Ltd.
PY - 2018
Y1 - 2018
N2 - Binding of cholera toxin subunit B (CTB) to its receptor and toxin transport into the intestinal epithelial cells are the causative events for the potentially lethal disease cholera. The five sugar mono-sialo ganglioside GM1 is the cell surface receptor for cholera toxin B-subunit. CTB binding was determined by use of immobilized GM1 to microtiter plates and by immunohistochemistry. Sections from the human colon and the human soft palate were incubated with FITC-conjugated CTB and with anti-MUC2. Both the luminal surface of the intestine and the secretory goblet cells exhibited strong binding. Addition of simple carbohydrates and milk to the incubation medium showed that a combination of lactose and non-fat dry milk was potent inhibitors of toxin- and mucin binding. Both CTB and ant-MUC2 stained to the cytoplasm (mucin granules) in the goblet cells from the human soft palate. In the colon CTB stained the entire cytoplasm of the goblet cells while anti-MUC2 detected only the supranuclear region of some cells, suggesting carbohydrate heterogeneity between goblet cell mucin granules in different regions of the human body. Both CTB- and MUC2 binding were inhibited when GM1 was added to the incubation medium. It is proposed that the human colonic goblet cells play a role in the secretory diarrhea in patients with cholera and that milk might have a prophylactic or therapeutic application in the management of cholera.
AB - Binding of cholera toxin subunit B (CTB) to its receptor and toxin transport into the intestinal epithelial cells are the causative events for the potentially lethal disease cholera. The five sugar mono-sialo ganglioside GM1 is the cell surface receptor for cholera toxin B-subunit. CTB binding was determined by use of immobilized GM1 to microtiter plates and by immunohistochemistry. Sections from the human colon and the human soft palate were incubated with FITC-conjugated CTB and with anti-MUC2. Both the luminal surface of the intestine and the secretory goblet cells exhibited strong binding. Addition of simple carbohydrates and milk to the incubation medium showed that a combination of lactose and non-fat dry milk was potent inhibitors of toxin- and mucin binding. Both CTB and ant-MUC2 stained to the cytoplasm (mucin granules) in the goblet cells from the human soft palate. In the colon CTB stained the entire cytoplasm of the goblet cells while anti-MUC2 detected only the supranuclear region of some cells, suggesting carbohydrate heterogeneity between goblet cell mucin granules in different regions of the human body. Both CTB- and MUC2 binding were inhibited when GM1 was added to the incubation medium. It is proposed that the human colonic goblet cells play a role in the secretory diarrhea in patients with cholera and that milk might have a prophylactic or therapeutic application in the management of cholera.
U2 - 10.1016/j.micpath.2018.08.047
DO - 10.1016/j.micpath.2018.08.047
M3 - Journal article
C2 - 30145256
VL - 124
SP - 332
EP - 336
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
SN - 0882-4010
ER -
ID: 201807812