Mutant Escherichia coli heat-labile toxin B subunit that separates toxoid-mediated signaling and immunomodulatory action from trafficking and delivery functions.

@article{Fraser2003MutantEC,
  title={Mutant Escherichia coli heat-labile toxin B subunit that separates toxoid-mediated signaling and immunomodulatory action from trafficking and delivery functions.},
  author={Sylvia A. Fraser and Lolke de Haan and Arron R. Hearn and Heather K. Bone and Robert J Salmond and A. Jennifer Rivett and Neil A. Williams and Timothy R. Hirst},
  journal={Infection and immunity},
  year={2003},
  volume={71 3},
  pages={1527-37}
}
The homopentameric B-subunit components of Escherichia coli heat-labile enterotoxin (EtxB) and cholera toxin (CtxB) possess the capacity to enter mammalian cells and to activate cell-signaling events in leukocytes that modulate immune cell function. Both properties have been attributed to the ability of the B subunits to bind to GM1-ganglioside receptors, a ubiquitous glycosphingolipid found in the plasma membrane. Here we describe the properties of EtxB(H57S), a mutant B subunit with a His… CONTINUE READING
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