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Journal of Bacteriology, December 2004, p. 8137-8143, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8137-8143.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Vibrio cholerae Strains with Mutations in an Atypical Type I Secretion System Accumulate RTX Toxin Intracellularly

Bethany Kay Boardman and Karla J. Fullner Satchell*

Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois

Received 30 June 2004/ Accepted 25 August 2004

This study shows that the Vibrio cholerae RTX toxin is secreted by a four-component type I secretion system (TISS) encoded by rtxB, rtxD, rtxE, and tolC. ATP-binding site mutations in both RtxB and RtxE blocked secretion, demonstrating that this atypical TISS requires two transport ATPases that may function as a heterodimer.

* Corresponding author. Mailing address: Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Morton 6-626, 303 E. Chicago Ave., Chicago, IL 60611. Phone: (312) 503-2162. Fax: (312) 503-1339. E-mail: k-satchell{at}northwestern.edu.

Journal of Bacteriology, December 2004, p. 8137-8143, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8137-8143.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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