Affiliation:
1. Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9048
Abstract
ABSTRACT
The cytolethal distending toxin (CDT) of
Haemophilus ducreyi
is comprised of the CdtA, CdtB, and CdtC proteins, with the CdtB protein having demonstrated enzymatic (i.e., DNase) activity. Using a single recombinant
Escherichia coli
strain with two plasmids individually containing the
H. ducreyi cdtA
and
cdtC
genes, we purified a noncovalent CdtA-CdtC complex. Incubation of this CdtA-CdtC complex with HeLa cells blocked killing of these cells by CDT holotoxin. Furthermore, the addition of purified recombinant CdtB to HeLa cells preincubated with the CdtA-CdtC complex resulted in the killing of these human epithelial cells.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
32 articles.
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