1887

Abstract

produces an NAD-specific glutamate dehydrogenase (GDH), which converts -glutamate into α-ketoglutarate through an irreversible reaction. The enzyme GDH is detected in the stool samples of patients with ‐associated disease and serves as one of the diagnostic tools to detect infection (CDI). We demonstrate here that supernatant fluids of cultures contain GDH. To understand the role of GDH in the physiology of , an isogenic insertional mutant of was created in strain JIR8094. The mutant failed to produce and secrete GDH as shown by Western blot analysis. Various phenotypic assays were performed to understand the importance of GDH in physiology. In TY (tryptose yeast extract) medium, the mutant grew slower than the parent strain. Complementation of the mutant with the functional gene reversed the growth defect in TY medium. The presence of extracellular GDH may have a functional role in the pathogenesis of CDI. In support of this assumption we found higher sensitivity to HO in the mutant as compared to the parent strain. Complementation of the mutant with the functional gene reversed the HO sensitivity.

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2014-01-01
2019-12-13
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