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. 2014 Jul 22;6(7):2162–2176. doi: 10.3390/toxins6072162

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© 2014 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

PMC Copyright notice

The CROPs of TcdA protect from premature autoproteolytic toxin inactivation. (A) Autocatalytic processing of TcdA, TcdB and the chimeras, TcdA^1–1874-TcdB CROPs and TcdB^1–1852-TcdA CROPs, respectively. Cleavage was induced by the addition of IP₆ and DTT at pH 7.0. Specific antibody directed against the glucosyltransferase domain (GTD) of TcdA (indicated by the arrow) was applied in the case of TcdA and TcdA^1–1874-TcdB CROPs (α-TcdA 542) and against the homologous domain of TcdB in the case of TcdB and TcdB^1–1852-TcdA CROPs (α-TcdB 543); (B) The bar chart shows the densitometrical evaluation of the cleaved glucosyltransferase domain. The cleavage efficacy of TcdA differs significantly from that of chimera TcdA^1–1874-TcdB CROPs (*** p < 0.0001) and TcdB (* p = 0.017), respectively; ns = not significant.