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Infection and Immunity, May 2001, p. 3418-3422, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3418-3422.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Escherichia coli CdtB Mediates Cytolethal Distending Toxin Cell Cycle Arrest

Cherilyn Elwell, Kinlin Chao, Kamlesh Patel, and Lawrence Dreyfus*

Division of Cell Biology and Biophysics, University of Missouri---Kansas City, Kansas City, Missouri 64110

Received 26 September 2000/Returned for modification 18 December 2000/Accepted 19 February 2001

We previously reported that the CdtB polypeptide of Escherichia coli cytolethal distending toxin (CDT) shares significant pattern-specific homology with mammalian type I DNases. In addition, the DNase-related residues of CdtB are required for cellular toxicity. Here we demonstrate that purified CdtB converts supercoiled plasmid DNA to relaxed and linear forms and promotes cell cycle arrest when combined with an E. coli extract containing CdtA and CdtC. CdtB alone had no effect on HeLa cells, however; introduction of the polypeptide into HeLa cells by electroporation resulted in cellular distension, chromatin fragmentation, and cell cycle arrest, all of which are consequences of CDT action. In contrast to these findings, purified CdtBH154A lacked both DNA-nicking and cell cycle arrest activities. These results suggest a functional relationship between DNase-related residues in CdtB and CDT biological activity.

* Corresponding author. Mailing address: Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri---Kansas City, Kansas City, MO 64110. Phone: (816) 235-5245. Fax: (816) 235-1503. E-mail: dreyfusl{at}umkc.edu.

Infection and Immunity, May 2001, p. 3418-3422, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3418-3422.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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