Tc Toxin Complexes: Assembly, Membrane Permeation, and Protein Translocation.


Journal

Annual review of microbiology
ISSN: 1545-3251
Titre abrégé: Annu Rev Microbiol
Pays: United States
ID NLM: 0372370

Informations de publication

Date de publication:
08 09 2019
Historique:
pubmed: 30 5 2019
medline: 6 5 2020
entrez: 30 5 2019
Statut: ppublish

Résumé

Tc toxin complexes are virulence factors of many bacteria, including insect and human pathogens. Tc toxins are composed of three subunits that act together to perforate the host membrane, similar to a syringe, and translocate toxic enzymes into the host cell. The reactions of the toxic enzymes lead to deterioration and ultimately death of the cell. We review recent high-resolution structural and functional data that explain the mechanism of action of this type of bacterial toxin at an unprecedented level of molecular detail. We focus on the steps that are necessary for toxin activation and membrane permeation. This is where the largest conformational transitions appear. Furthermore, we compare the architecture and function of Tc toxins with those of anthrax toxin and vertebrate teneurin.

Identifiants

pubmed: 31140906
doi: 10.1146/annurev-micro-102215-095531
doi:

Substances chimiques

Bacterial Toxins 0
Protein Subunits 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

247-265

Auteurs

Daniel Roderer (D)

Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany; email: daniel.roderer@mpi-dortmund.mpg.de, raunser@mpi-dortmund.mpg.de.

Stefan Raunser (S)

Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany; email: daniel.roderer@mpi-dortmund.mpg.de, raunser@mpi-dortmund.mpg.de.

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Classifications MeSH