Next Article in Journal / Special Issue
The Zinc-Dependent Protease Activity of the Botulinum Neurotoxins
Previous Article in Journal
The Role of Lymphostatin/EHEC Factor for Adherence-1 in the Pathogenesis of Gram Negative Infection
Previous Article in Special Issue
Proteases as Insecticidal Agents
Open AccessReview

Autoproteolytic Activation of Bacterial Toxins

Department of Pathology, Stanford School of Medicine, 300 Pasteur Drive, Stanford, California 94305, USA
Toxins 2010, 2(5), 963-977; https://doi.org/10.3390/toxins2050963
Received: 31 March 2010 / Revised: 28 April 2010 / Accepted: 5 May 2010 / Published: 6 May 2010
(This article belongs to the Special Issue Protein Toxins as Proteases)
Protease domains within toxins typically act as the primary effector domain within target cells. By contrast, the primary function of the cysteine protease domain (CPD) in Multifunctional Autoprocessing RTX-like (MARTX) and Clostridium sp. glucosylating toxin families is to proteolytically cleave the toxin and release its cognate effector domains. The CPD becomes activated upon binding to the eukaryotic-specific small molecule, inositol hexakisphosphate (InsP6), which is found abundantly in the eukaryotic cytosol. This property allows the CPD to spatially and temporally regulate toxin activation, making it a prime candidate for developing anti-toxin therapeutics. In this review, we summarize recent findings related to defining the regulation of toxin function by the CPD and the development of inhibitors to prevent CPD-mediated activation of bacterial toxins. View Full-Text
Keywords: cysteine protease domain (CPD); MARTX toxin; glucosylating toxin (GT); inositol hexakisphosphate (InsP6); glucosyltransferase (Glc); structure activity relationship (SAR) cysteine protease domain (CPD); MARTX toxin; glucosylating toxin (GT); inositol hexakisphosphate (InsP6); glucosyltransferase (Glc); structure activity relationship (SAR)
Show Figures

Figure 1

MDPI and ACS Style

Shen, A. Autoproteolytic Activation of Bacterial Toxins. Toxins 2010, 2, 963-977.

Show more citation formats Show less citations formats

Article Access Map

1
Only visits after 24 November 2015 are recorded.
Back to TopTop