Attenuated endocytosis and toxicity of a mutant cholera toxin with decreased ability to cluster ganglioside GM1 molecules.

@article{Wolf2008AttenuatedEA,
  title={Attenuated endocytosis and toxicity of a mutant cholera toxin with decreased ability to cluster ganglioside GM1 molecules.},
  author={Anne A. Wolf and Michael G. Jobling and David E. Saslowsky and Eli Kern and Kimberly R. Drake and Anne K. Kenworthy and Randall K. Holmes and Wayne I Lencer},
  journal={Infection and immunity},
  year={2008},
  volume={76 4},
  pages={1476-84}
}
Cholera toxin (CT) moves from the plasma membrane (PM) of host cells to the endoplasmic reticulum (ER) by binding to the lipid raft ganglioside GM(1). The homopentomeric B-subunit of the toxin can bind up to five GM(1) molecules at once. Here, we examined the role of polyvalent binding of GM(1) in CT action by producing chimeric CTs that had B-subunits with only one or two normal binding pockets for GM(1). The chimeric toxins had attenuated affinity for binding to host cell PM, as expected… CONTINUE READING