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  • Characterization of the DsbA oxidative folding catalyst from Pseudomonas aeruginosa reveals a highly oxidizing protein that binds small molecules

    Author(s)
    Shouldice, Stephen R
    Heras, Begona
    Jarrott, Russell
    Sharma, Pooja
    Scanlon, Martin J
    Martin, Jennifer L
    Griffith University Author(s)
    Martin, Jennifer
    Jarrott, Russell J.
    Year published
    2010
    Metadata
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    Abstract
    Bacterial antibiotic resistance is an emerging global crisis, and treatment of multidrug-resistant gram-negative infections, particularly those caused by the opportunistic human pathogen Pseudomonas aeruginosa, remains a major challenge. This problem is compounded by a lack of new antibiotics in the development pipeline: only two new classes have been developed since the 1960s, and both are indicated for multidrug-resistant gram-positive infections. A promising new approach to combat antibiotic resistance is by targeting bacterial virulence, rather than bacterial viability. The bacterial periplasmic protein DsbA represents ...
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    Bacterial antibiotic resistance is an emerging global crisis, and treatment of multidrug-resistant gram-negative infections, particularly those caused by the opportunistic human pathogen Pseudomonas aeruginosa, remains a major challenge. This problem is compounded by a lack of new antibiotics in the development pipeline: only two new classes have been developed since the 1960s, and both are indicated for multidrug-resistant gram-positive infections. A promising new approach to combat antibiotic resistance is by targeting bacterial virulence, rather than bacterial viability. The bacterial periplasmic protein DsbA represents a central point for antivirulence intervention because its oxidoreductase activity is essential for the folding and function of almost all exported virulence factors. Here we describe the three-dimensional structure of this DsbA target from P. aeruginosa, and we establish for the first time that a member of this enzyme family is capable of binding small molecules. We also describe biochemical assays that validate the redox activity of PaDsbA. Together, the structural and functional characterization of PaDsbA provides the basis for future studies aimed at designing a new class of antivirulence compounds to combat antibiotic-resistant P. aeruginosa infection.
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    Journal Title
    Antioxidants & Redox Signaling
    Volume
    12
    Issue
    8
    DOI
    https://doi.org/10.1089/ars.2009.2736
    Subject
    Medical Biochemistry and Metabolomics not elsewhere classified
    Biochemistry and Cell Biology
    Medical Biochemistry and Metabolomics
    Pharmacology and Pharmaceutical Sciences
    Publication URI
    http://hdl.handle.net/10072/345720
    Collection
    • Journal articles

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