Open AccessInteraction of Escherichia coli heat‐stable enterotoxin B with rat intestinal epithelial cells and membrane lipids
Author(s) -
Chao Kinlin L,
Dreyfus Lawrence A
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13455.x
Subject(s) - enterotoxin , heat stable enterotoxin , escherichia coli , microbiology and biotechnology , chemistry , membrane , enterobacteriaceae , biology , biochemistry , gene
The binding of 125 I‐labeled Escherichia coli heat‐stable enterotoxin B to rat intestinal epithelial cells was unsaturable and nonspecific, at concentrations well above that required to mediate biological events. Following its interaction with intestinal cells, ∼50–80% of heat‐stable enterotoxin B remained stably associated with the cells, implying that it was partitioned into the membrane and/or internalized by the cell. The toxin bound with different affinities to lipids isolated from intestinal epithelial cells, phospholipids, glycolipids, neutral lipids and to model membrane vesicles containing negatively charged lipids. These results indicate that heat‐stable enterotoxin B utilizes the membrane bilayer, rather than a surface protein or glycoprotein in modulating toxin‐induced enterotoxicity.