Open AccessEscherichia coliCdtB Mediates Cytolethal Distending Toxin Cell Cycle Arrest
Author(s) -
Cherilyn A. Elwell,
Kinlin Chao,
Kamlesh D. Patel,
Lawrence A. Dreyfus
Publication year - 2001
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.69.5.3418-3422.2001
Subject(s) - cytolethal distending toxin , biology , hela , cell cycle checkpoint , cell cycle , escherichia coli , microbiology and biotechnology , dna fragmentation , chromatin , apoptosis , fragmentation (computing) , dna damage , dna , cell , programmed cell death , biochemistry , ecology , gene
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 CdtB(H154A) 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.