Structure-function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G-proteins.

@article{Littler2017StructurefunctionAO,
  title={Structure-function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G-proteins.},
  author={Dene R. Littler and Sheng Ang and Danilo Gomes Moriel and Martina Kocan and Oded Kleifeld and Matthew D. Johnson and Mai T. Tran and Adrienne W Paton and James C Paton and Roger J Summers and Mark A Schembri and Jamie Rossjohn and Travis Beddoe},
  journal={The Journal of biological chemistry},
  year={2017},
  volume={292 36},
  pages={15143-15158}
}
Pertussis-like toxins are secreted by several bacterial pathogens during infection. They belong to the AB5 virulence factors, which bind to glycans on host cell membranes for internalization. Host cell recognition and internalization are mediated by toxin B subunits sharing a unique pentameric ring-like assembly. Although the role of pertussis toxin in whooping cough is well-established, pertussis-like toxins produced by other bacteria are less studied, and their mechanisms of action are… CONTINUE READING