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  • A Glutathione-Dependent Detoxification System Is Required for Formaldehyde Resistance and Optimal Survival of Neisseria meningitidis in Biofilms

    Author(s)
    Chen, Nathan H
    Counago, Rafael M
    Djoko, Karrera Y
    Jennings, Michael P
    Apicella, Michael A
    Kobe, Bostjan
    McEwan, Alastair G
    Griffith University Author(s)
    Jennings, Michael P.
    Year published
    2013
    Metadata
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    Abstract
    Aim:The glutathione-dependent, AdhC-EstD formaldehyde detoxification system is found in eukaryotes and prokaryotes. It is established that it confers protection against formaldehyde that is produced from environmental sources or methanol metabolism. Thus, its presence in the human host adapted bacterial pathogen Neisseria meningitidis is intriguing. This work defined the biological function of this system in the meningococcus using phenotypic analyses of mutants linked to biochemical and structural characterisation of purified enzymes. Results: We demonstrated that mutants in the adhC and/or estD were sensitive to killing ...
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    Aim:The glutathione-dependent, AdhC-EstD formaldehyde detoxification system is found in eukaryotes and prokaryotes. It is established that it confers protection against formaldehyde that is produced from environmental sources or methanol metabolism. Thus, its presence in the human host adapted bacterial pathogen Neisseria meningitidis is intriguing. This work defined the biological function of this system in the meningococcus using phenotypic analyses of mutants linked to biochemical and structural characterisation of purified enzymes. Results: We demonstrated that mutants in the adhC and/or estD were sensitive to killing by formaldehyde. Inactivation of adhC and/or estD also led to a loss of viability in biofilm communities, even in the absence of exogenous formaldehyde. Detailed biochemical and structural analyses of the esterase component demonstrated that S-formylglutathione was the only biologically relevant substrate for EstD. We further showed that an absolutely conserved cysteine residue was covalently modified by S-glutathionylation. This leads to inactivation of EstD. Innovation:The results provide several conceptual innovations. They provide new insight into formaldehyde detoxification in bacteria that do not generate formaldehyde during the catabolism of methanol. Our results also indicate that the conserved cysteine, found in all EstD enzymes from humans to microbes, is a site of enzyme regulation, probably via S-glutathionylation. Conclusion: The adhC/estD system protects against formaldehyde produced during endogenous metabolism.
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    Journal Title
    Antioxidants & Redox Signaling
    Volume
    18
    Issue
    7
    DOI
    https://doi.org/10.1089/ars.2012.4749
    Subject
    Biochemistry and cell biology
    Bacteriology
    Medical biochemistry and metabolomics
    Pharmacology and pharmaceutical sciences
    Publication URI
    http://hdl.handle.net/10072/55297
    Collection
    • Journal articles

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