Ability of Blood Group A-active Glycosphingolipids to Act as Escherichia coli Heat-Labile Enterotoxin Receptors in HT-29 Cells

We examined the ability of blood group A-active glycoconjugates to act as receptors for Escherichia coli heatlabile type I enterotoxin (LT-I) in HT-29 cells. These cells contained ∼4 times more specific binding sites for LT-I than for cholera toxin (CT). Binding of LT-I could not be blocked by the B...

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Bibliographic Details
Published in:The Journal of infectious diseases 2004-05, Vol.189 (9), p.1556-1564
Main Authors: Galván, Estela M., Diema, Claudio D., Roth, German A., Monferran, Clara G.
Format: Article
Language:English
Subjects:
ABO Blood-Group System - chemistry
Bacteria
Bacterial Toxins - metabolism
Bacteriology
Biological and medical sciences
Blood groups
Cell membranes
Cholera
Cyclic AMP - metabolism
Enterotoxins
Enterotoxins - metabolism
Escherichia coli
Escherichia coli - metabolism
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
Glycolipids
Glycosphingolipids
Glycosphingolipids - metabolism
Guanylate Cyclase - metabolism
HT29 Cells
Humans
Infectious diseases
Ligands
Medical sciences
Meperidine - analogs & derivatives
Meperidine - pharmacology
Microbiology
Miscellaneous
Receptors
Receptors, Enterotoxin
Receptors, Guanylate Cyclase-Coupled
Receptors, Peptide - metabolism
Signal Transduction
Toxins
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Summary:We examined the ability of blood group A-active glycoconjugates to act as receptors for Escherichia coli heatlabile type I enterotoxin (LT-I) in HT-29 cells. These cells contained ∼4 times more specific binding sites for LT-I than for cholera toxin (CT). Binding of LT-I could not be blocked by the B subunit of CT (CT-B), indicating the existence of LT-I receptors in addition to the glycosphingolipid GM1. LT-I was able to increase levels of cyclic adenosine monophosphate (AMP), even in the presence of CT-B. Helix pomatia and anti-blood group A antibody caused a dose-dependent inhibition of binding of LT-I to cells and production of cyclic AMP. LT-I recognized several complex blood group A-active glycosphingolipids from cells, and this interaction was also interfered with by H. pomatia. Treatment of cells with D,L-threo-1-phenyl-2-hexadecanoylamino-3-morpholino-1-propanol diminished surface expression of blood group A-active glycosphingolipids and binding of LT-I to non-GM1 receptors. These observations suggest that blood group A-active glycosphingolipids can function as alternative receptors for LT-I in HT-29 cells.
ISSN:0022-1899
1537-6613
DOI:10.1086/383349