Search citation statements
Paper Sections
Citation Types
Year Published
Publication Types
Relationship
Authors
Journals
As an intestinal human pathogen,Clostridioides difficileis the main cause of antibiotic-associated diarrhoea. Endospores of this gram-positive bacterium enter the intestinal tract via faecal-oral transmission, germinate into vegetative and toxin-producing cells and can trigger aClostridioides difficileinfection. The microaerophilic conditions (0.1 to 0.4 % O2) of the large intestine represent a challenge for the strictly anaerobic organism, which protects itself by a variety of oxidative stress proteins. Four of these are encoded in an operon that is assumed to be involved in the detoxification of H2O2and O2●-. This operon encodes a rubrerythrin (rbr), its own transcriptional repressor PerR (perR), a desulfoferrodoxin (rbo) and a putative glutamate dehydrogenase (CD630_08280) with an N-terminal rubredoxin domain, which is only expressed under high oxidative stress conditions. In this study, the enzyme activity of Rbr, Rbo and CD630_08280 was testedin-vitro. Recombinant proteins were overexpressed inC. difficileand purified anaerobically by affinity chromatography. A H2O2reduction potential was demonstrated for Rbr, Rbo and glutamate dehydrogenase. Rbr and glutamate dehydrogenase proved to synergistically detoxify H2O2very efficiently. Furthermore, Rbo was verified as a O2●-reductase and its activity compared to the superoxide dismutase ofE. coli. The investigated gene locus codes for an oxidative stress operon whose members are able to completely neutralize O2●-and H2O2to water and could thus be vital forC. difficileto establish an infection in the host.
As an intestinal human pathogen,Clostridioides difficileis the main cause of antibiotic-associated diarrhoea. Endospores of this gram-positive bacterium enter the intestinal tract via faecal-oral transmission, germinate into vegetative and toxin-producing cells and can trigger aClostridioides difficileinfection. The microaerophilic conditions (0.1 to 0.4 % O2) of the large intestine represent a challenge for the strictly anaerobic organism, which protects itself by a variety of oxidative stress proteins. Four of these are encoded in an operon that is assumed to be involved in the detoxification of H2O2and O2●-. This operon encodes a rubrerythrin (rbr), its own transcriptional repressor PerR (perR), a desulfoferrodoxin (rbo) and a putative glutamate dehydrogenase (CD630_08280) with an N-terminal rubredoxin domain, which is only expressed under high oxidative stress conditions. In this study, the enzyme activity of Rbr, Rbo and CD630_08280 was testedin-vitro. Recombinant proteins were overexpressed inC. difficileand purified anaerobically by affinity chromatography. A H2O2reduction potential was demonstrated for Rbr, Rbo and glutamate dehydrogenase. Rbr and glutamate dehydrogenase proved to synergistically detoxify H2O2very efficiently. Furthermore, Rbo was verified as a O2●-reductase and its activity compared to the superoxide dismutase ofE. coli. The investigated gene locus codes for an oxidative stress operon whose members are able to completely neutralize O2●-and H2O2to water and could thus be vital forC. difficileto establish an infection in the host.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.