ArticleMicrobiology (Reading, England)2014
Clostridium difficile glutamate dehydrogenase is a secreted enzyme that confers resistance to H2O2.
Article in Microbiology (Reading, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Defense arsenal of the strict anaerobemBio · 2025Article
- Article
- Shaping microbiology for 75 years: highlights of research published inMicrobiology (Reading, England) · 2023Article
- Bacterial crystalline cellulose secretion via a supramolecular BcsHD scaffold.Science advances · 2022Article
- Unique Features of Alarmone Metabolism in Clostridioides difficile.Journal of bacteriology · 2022Article
- Detection of Newly Secreted Antibodies Predicts Nonrecurrence in Primary Clostridioides difficile Infection.Journal of clinical microbiology · 2022Article
- Antigen-Specific vs. Neutralizing Antibodies Against Conditioned Media of Patients WithFrontiers in microbiology · 2022Article
- Extracellular DNA, cell surface proteins and c-di-GMP promote biofilm formation in Clostridioides difficile.Scientific reports · 2021Article
- Spo0A SuppressesmSphere · 2020Article
- Diverse Energy-Conserving Pathways in Clostridium difficile: Growth in the Absence of Amino Acid Stickland Acceptors and the Role of the Wood-Ljungdahl Pathway.Journal of bacteriology · 2020Article
- How the Anaerobic EnteropathogenmBio · 2020Article
- A Two-Step Approach for Diagnosing Glutamate Dehydrogenase Genes by Conventional Polymerase Chain Reaction fromMiddle East journal of digestive diseases · 2019Article
- Pleiotropic roles of Clostridium difficile sin locus.PLoS pathogens · 2018Article
- Role of the leukocyte response in normal and immunocompromised host after Clostridium difficile infection.Anaerobe · 2017Review
- Current knowledge on the laboratory diagnosis ofWorld journal of gastroenterology · 2017Review
- Investigation of the Cross-talk Mechanism in Caco-2 Cells duringFrontiers in immunology · 2017Article
- Neutrophil-mediated inflammation in the pathogenesis of Clostridium difficile infections.Anaerobe · 2016Review
- Clostridium difficile colitis: pathogenesis and host defence.Nature reviews. Microbiology · 2016Review
- Reactive Oxygen Species as Additional Determinants for Cytotoxicity of Clostridium difficile Toxins A and B.Toxins · 2016Review
- Importance of Glutamate Dehydrogenase (GDH) in Clostridium difficile Colonization In Vivo.PloS one · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Clostridium difficile produces an NAD-specific glutamate dehydrogenase (GDH), which converts l-glutamate into α-ketoglutarate through an irreversible reaction. The enzyme GDH is detected in the stool samples of patients with C. difficile-associated disease and serves as one of the diagnostic tools to detect C. difficile infection (CDI). We demonstrate here that supernatant fluids of C. difficile cultures contain GDH. To understand the role of GDH in the physiology of C. difficile, an isogenic insertional mutant of gluD 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 C. difficile physiology. In TY (tryptose yeast extract) medium, the gluD mutant grew slower than the parent strain. Complementation of the gluD mutant with the functional gluD 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 H2O2 in the gluD mutant as compared to the parent strain. Complementation of the gluD mutant with the functional gluD gene reversed the H2O2 sensitivity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.