Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins

Martina Egerer, Karla J. F. Satchell

Research output: Contribution to journalReview article

36 Citations (Scopus)

Abstract

Large bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Grampositive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms for effector translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is activated for autoprocessing by binding inositol hexakisphosphate (InsP6), a molecule found exclusively in eukaryotic cells. Thus, InsP6-induced autoprocessing represents a unique mechanism for toxin effector delivery specifically within the target cell. This review summarizes recent studies of the structural and molecular events for activation of autoprocessing for both CGT and MARTX toxins, demonstrating both similar and potentially distinct aspects of autoprocessing among the toxins that utilize this method of activation and effector delivery.

Original languageEnglish (US)
Article numbere1000942
Pages (from-to)1-8
Number of pages8
JournalPLoS Pathogens
Volume6
Issue number7
DOIs
StatePublished - Jul 1 2010

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Bacterial Toxins
Phytic Acid
Bacterial Proteins
Eukaryotic Cells
Cysteine Proteases
Gram-Negative Bacteria
Cytosol
Bacteria
stichoposide

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Molecular Biology
  • Genetics
  • Virology

Cite this

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Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. / Egerer, Martina; Satchell, Karla J. F.

In: PLoS Pathogens, Vol. 6, No. 7, e1000942, 01.07.2010, p. 1-8.

Research output: Contribution to journalReview article

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