Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization.

@article{Groulx2011SingleMF,
  title={Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization.},
  author={Nicolas Groulx and Hugo McGuire and Raynald Laprade and J. Schwartz and Rikard Blunck},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 49},
  pages={
          42274-82
        }
}
Pore-forming toxins constitute a class of potent virulence factors that attack their host membrane in a two- or three-step mechanism. After binding to the membrane, often aided by specific receptors, they form pores in the membrane. Pore formation either unfolds a cytolytic activity in itself or provides a pathway to introduce enzymes into the cells that act upon intracellular proteins. The elucidation of the pore-forming mechanism of many of these toxins represents a major research challenge… CONTINUE READING

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