Pore Forming Toxins: Protein Expression, Biotechnology and Interactions with the Membrane

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: closed (14 July 2023) | Viewed by 410

Special Issue Editor


E-Mail Website
Guest Editor
College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK
Interests: pore-forming toxins; cutting-edge structural; biophysical; molecular cell biology approaches; Clostridium perfringens epsilon toxin (Etx); host cell membrane; diagnostics; therapeutics; vaccines; bacterial infections

Special Issue Information

Dear Colleagues,

Secreted bacterial pore-forming toxins (PFTs) are key mediators of bacterial pathogenicity. The binding of toxins to host cell receptors is critical to the action of the toxin and the progression of disease; thus, understanding this key interaction is central to the production of new diagnostics, therapeutics, and vaccines. Development of these interventions is crucial and timely given the increasing incidence of antibiotic resistance in bacteria infecting humans and animals. β-pore-forming toxins (β-PFTs) are the largest group of cytotoxic proteins produced by bacteria. Many, including the toxins produced by a broad range of clostridial species, play important roles in human and animal bacterial infections worldwide. In some cases, such as for epsilon toxin (Etx), produced by Clostridium perfringens, the role of the toxin in disease is so pivotal that toxoid vaccines are sufficient to protect against disease. Dissecting the molecular basis for Etx interaction with the host cell membrane will thus enable improved vaccine design and future engineering of toxin derivatives for therapeutic cellular targeting. Understanding Etx will also allow us to better understand a wide range of bacterial toxins, with significant long-term implications for developing new approaches to controlling bacterial infections.

Dr. Monika Bokori-Brown
Guest Editor

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Keywords

  • membrane biophysics
  • aerolysin family
  • plasma membrane
  • Clostridium perfringens epsilon toxin
  • myelin and lymphocyte protein

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Published Papers

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