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Clostridium difficile  is a Gram positive, anaerobic bacterium that can form highly resistant endospores. The bacterium is the causative agent of  C. difficile  infection (CDI), for which the symptoms can range from a mild diarrhea to potentially fatal pseudomembranous colitis and toxic megacolon. Endospore formation in Firmicutes, including  C. difficile , is governed by the key regulator for sporulation, Spo0A. In  Bacillus subtilis , this transcription factor is also directly or indirectly involved in various other cellular processes. Here, we report that  C. difficile  Spo0A shows a high degree of similarity to the well characterized  B. subtilis  protein and recognizes a similar binding sequence. We find that the laboratory strain  C. difficile  630Δerm contains an 18bp-duplication near the DNA-binding domain compared to its ancestral strain 630.  In vitro  binding assays using purified C-terminal DNA binding domain of the  C. difficile  Spo0A protein demonstrate direct binding to DNA upstream of  spo0A  and  sigH , early sporulation genes and several other putative targets.  In vitro  binding assays suggest that the gene encoding the major clostridial toxin TcdB may be a direct target of Spo0A, but supernatant derived from a  spo0A  negative strain was no less toxic towards Vero cells than that obtained from a wild type strain, in contrast to previous reports. These results identify for the first time direct (putative) targets of the Spo0A protein in  C. difficile  and make a positive effect of Spo0A on production of the large clostridial toxins unlikely.

C. difficile 630Δerm Spo0A Regulates Sporulation, but Does Not Contribute to Toxin Production, by Direct High-Affinity Binding to Target DNA