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Significance Clostridioides difficile (formerlyClostridium difficile ) is the leading cause of hospital-acquired diarrhea in the United States. The pathology resulting fromC. difficile infection has been attributed to the activity of up to three secreted toxins known as toxin A (TcdA), toxin B (TcdB), and theC. difficile transferase toxin (CDT). Reported here is the near-atomic resolution structure of CDT, a bipartite toxin that is made up of two components called CDTa and CDTb. Our structure highlights a unique mode of toxin assembly that is distinct from the previously characterized anthrax toxin. The orientation we observe appears to prime CDT for delivery into the host by placing the N-terminal domain of CDTa at the entrance to the pore.

Structural elucidation of the Clostridioides difficile transferase toxin reveals a single-site binding mode for the enzyme