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Determination of Tolerable Fatty Acids and Cholera Toxin Concentrations Using Human Intestinal Epithelial Cells and BALB/c Mouse Macrophages
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Cell type and receptor identity regulate cholera toxin subunit B (CTB) internalization.

Anirudh Sethi1, Amberlyn M Wands1, Marcel Mettlen2

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Interface Focus
|March 8, 2019
PubMed
Summary

Cholera toxin (CT) internalization depends on cell type and receptor identity. Fucosylated glycoconjugates contribute to CTB binding and uptake, even with ganglioside GM1 present.

Keywords:
GM1choleraexotoxinfucoseglycosylation

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Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity
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Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Cholera toxin (CT) is a bacterial toxin that intoxicates mammalian cells.
  • The CT B subunit (CTB) mediates cell surface receptor binding.
  • Ganglioside GM1 is the historically recognized CT receptor, but fucosylated glycoconjugates also bind CTB.

Purpose of the Study:

  • To investigate the contribution of gangliosides and fucosylated glycoconjugates to CTB internalization.
  • To determine how receptor type and cell context influence CTB uptake.

Main Methods:

  • Utilized colonic and respiratory epithelial cell lines.
  • Examined CTB binding and internalization mechanisms.
  • Compared the roles of gangliosides and fucosylated glycoconjugates in CTB uptake.

Main Results:

  • Fucosylated glycoconjugates significantly contribute to CTB binding and internalization, irrespective of GM1 presence.
  • The relative importance of gangliosides and fucosylated glycoconjugates varies by cell type.
  • In cells expressing both receptor types, gangliosides primarily regulate CTB internalization efficiency.

Conclusions:

  • Fucosylated glycoconjugates play a functional role in CTB internalization.
  • CT internalization is a complex process influenced by both receptor identity and host cell type.