CdtB is considered the active subunit of the CDT holotoxin. Microinjection of CdtB into susceptible cells without CdtA or CdtC results in the G2/M cell cycle arrest and cytoplasmic distension characteristic of CDT toxins. The structure of CdtB is well-conserved between different bacteria. The CdtB subunit is the most sequentially conserved between species. The molecular weight of CdtB ranges from 28 kDa to 29 kDa, depending on the species.
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Background
Cytolethal distending toxin (CDT) was first isolated from culture filtrate of Escherichia coli, and is a heat-labile bacterial genotoxin that breaks double-stranded DNA in mammalian cells. When the resulting DDR is extreme and irreversible, cell cycle arrest ensues, even cell death. Cells damaged by CDT might sometimes survive and proliferate, but this can cause host cells to be genomically unstable and risk carcinogenesis. Therefore, this toxin also exhibits certain carcinogenic properties.
CDT is mostly present in Gram-negative microaerophilic bacteria such as Helicobacter pylori, Campylobacter jejuni and Shigella dysenteriae that can all generate the toxin. CDT usually consists of three genes that are part of the same operon (CdtA, CdtB, and CdtC). When these three subunits combine, they form the trimeric holotoxin complex known as CDT. CDT is a member of the AB toxin family and in most Gram-negative bacteria it is a common AB2 type toxin (A means the active part of the toxin and B means binding parts). CdtB is the toxins' active subunit of CDT and CdtA and CdtC are binding subunits that facilitate binding of the toxin to cells.
CdtB shares functional and structural homology with type I deoxyribonuclease, enabling it to cleave DNA, ultimately leading to programmed cell death. Studies have shown that CdtB exhibits PI3,4,5P3 activity, which can result in cell cycle arrest and programmed cell death in certain cell types. Importantly, CdtB only demonstrates phosphatase activity in the presence of PI3,4,5P3. Mutations at sites related to CdtB's phosphatase activity significantly reduce its effectiveness. This suggests that phosphatase activity may be one of the toxic mechanisms of CdtB.
Figure 1. 3D structure of CdtB (Source: Pons BJ, et al. 2019)
Alternative Names
Anti Cytolethal distending toxin B polyclonal Antibody
References
1. Pons BJ, et al. Cytolethal Distending Toxin Subunit B: A Review of Structure-Function Relationship. Toxins (Basel). 2019 Oct 12;11(10):595.
2. Bezine E, et al. The cytolethal distending toxin effects on Mammalian cells: a DNA damage perspective. Cells. 2014 Jun 11;3(2):592-615.
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Figure 1. 3D structure of CdtB
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