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| Subject Categories:
Proteins
| Microbiology & Pathogens
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The EMBO Journal
(2007) 26, 2552–2561, doi:10.1038/sj.emboj.7601700 Published online 26 April 2007
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| Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain |
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Kerri-Lynn Sheahan1, Christina L Cordero and Karla J Fullner Satchell
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Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA
To whom correspondence should be addressed
Karla J Fullner Satchell, Department of Microbiology-Immunology, Northwestern University, 303 E. Chicago Avenue, Tarry 3-713, Chicago, IL 60611, USA. Tel.: +1 312 503 2162; Fax: +1 312 503 1339; E-mail: k-satchell@northwestern.edu
1 Present address: Department of Microbiology, Tufts University, 136 Harrison Avenue, Boston, MA 02111, USA
Received 30 June 2006; Accepted 30 March 2007; Published online 26 April 2007.
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| Abstract |
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| Vibrio cholerae RTX is a large multifunctional bacterial toxin that causes actin crosslinking. Due to its size, it was predicted to undergo proteolytic cleavage during translocation into host cells to deliver activity domains to the cytosol. In this study, we identified a domain within the RTX toxin that is conserved in large clostridial glucosylating toxins TcdB, TcdA, TcnA, and TcsL; putative toxins from V. vulnificus, Yersinia sp., Photorhabdus sp., and Xenorhabdus sp.; and a filamentous/hemagglutinin-like protein FhaL from Bordetella sp. In vivo transfection studies and in vitro characterization of purified recombinant protein revealed that this domain from the V. cholerae RTX toxin is an autoprocessing cysteine protease whose activity is stimulated by the intracellular environment. A cysteine point mutation within the RTX holotoxin attenuated actin crosslinking activity suggesting that processing of the toxin is an important step in toxin translocation. Overall, we have uncovered a new mechanism by which large bacterial toxins and proteins deliver catalytic activities to the eukaryotic cell cytosol by autoprocessing after translocation. |
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| Keywords: Clostridium difficile Toxin B, cysteine protease, GTP, HCV NS2, V. cholerae RTX toxin |
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