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Infection and Immunity, January 2001, p. 599-601, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.599-601.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Cytosolic Delivery and Characterization of the TcdB Glucosylating Domain by Using a Heterologous Protein Fusion

Lea M. Spyres,1 Maen Qa'Dan,1 Amy Meader,1 James J. Tomasek,2 Eric W. Howard,2 and Jimmy D. Ballard1,*

The Department of Cell Biology, The University of Oklahoma Health Sciences Center, Oklahoma City,2 and The Department of Botany and Microbiology, University of Oklahoma, Norman,1 Oklahoma

Received 14 August 2000/Returned for modification 22 September 2000/Accepted 16 October 2000

TcdB from Clostridium difficile glucosylates small GTPases (Rho, Rac, and Cdc42) and is an important virulence factor in the human disease pseudomembranous colitis. In these experiments, in-frame genetic fusions between the genes for the 255 amino-terminal residues of anthrax toxin lethal factor (LFn) and the TcdB1-556 coding region were constructed, expressed, and purified from Escherichia coli. LFnTcdB1-556 was enzymatically active and glucosylated recombinant RhoA, Rac, Cdc42, and substrates from cell extracts. LFnTcdB1-556 plus anthrax toxin protective antigen intoxicated cultured mammalian cells and caused actin reorganization and mouse lethality, all similar to those caused by wild-type TcdB.

* Corresponding author. Mailing address: The Department of Botany and Microbiology, University of Oklahoma, 770 Van Vleet Oval, GLCH 516, Norman, OK 73019-0245. Phone: (405) 325-5133. Fax: (405) 325-7619. E-mail: jballard{at}ou.edu.

Infection and Immunity, January 2001, p. 599-601, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.599-601.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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