Application | Comment | Organism |
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medicine | Peptoclostridium difficile toxins A and B are S-nitrosylated by the infected host and S-nitrosylation attenuates virulence by inhibiting toxin self-cleavage and cell entry. InsP(6)- and inositol diphosphate InsP(7)-induced conformational changes in the toxin enable host S-nitrosothiols to transnitrosylate the toxin catalytic cysteine, which forms part of a structurally conserved nitrosylation motif. Treatment with exogenous InsP(6) enhances the therapeutic actions of oral S-nitrosothiols in mouse models of Peptoclostridium difficile infection | Clostridioides difficile |
Organism | UniProt | Comment | Textmining |
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Clostridioides difficile | - |
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