Toxins 2010, 2(5), 963-977; doi:10.3390/toxins2050963

Autoproteolytic Activation of Bacterial Toxins

Department of Pathology, Stanford School of Medicine, 300 Pasteur Drive, Stanford, California 94305, USA
Received: 31 March 2010; in revised form: 28 April 2010 / Accepted: 5 May 2010 / Published: 6 May 2010
(This article belongs to the Special Issue Protein Toxins as Proteases)
PDF Full-text Download PDF Full-Text [342 KB, uploaded 6 May 2010 10:17 CEST]
Abstract: 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.
Keywords: cysteine protease domain (CPD); MARTX toxin; glucosylating toxin (GT); inositol hexakisphosphate (InsP6); glucosyltransferase (Glc); structure activity relationship (SAR)

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

MDPI and ACS Style

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

AMA Style

Shen A. Autoproteolytic Activation of Bacterial Toxins. Toxins. 2010; 2(5):963-977.

Chicago/Turabian Style

Shen, Aimee. 2010. "Autoproteolytic Activation of Bacterial Toxins." Toxins 2, no. 5: 963-977.

Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert