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  • Characterization of a complex chemosensory signal transduction system which controls twitching motility in Pseudomonas aeruginosa

    Author(s)
    Whitchurch, Cynthia B.
    Leech, Andrew J.
    Young, Michael D.
    Kennedy, Derek
    Sargent, Jennifer I.
    Bertrand, Jacob J.
    Semmler, Annalese B. T.
    Mellick, Albert S.
    Martin, Paul R.
    Alm, Richard A.
    Hobbs, Matthew
    Beatson, Scott A.
    Huang, Bixing
    Nguyen, Lam
    Commolli, James C.
    Engel, Joanne N.
    Darzins, Aldis
    Mattick, John S.
    Griffith University Author(s)
    Mellick, Albert S.
    Year published
    2004
    Metadata
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    Abstract
    Virulence of the opportunistic pathogen Pseudomonas aeruginosa involves the coordinate expression of a wide range of virulence factors including type IV pili which are required for colonization of host tissues and are associated with a form of surface translocation termed twitching motility. Twitching motility in P. aeruginosa is controlled by a complex signal transduction pathway which shares many modules in common with chemosensory systems controlling flagella rotation in bacteria and which is composed, in part, of the previously described proteins PilG, PilH, PilI, PilJ and PilK. Here we describe another three components ...
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    Virulence of the opportunistic pathogen Pseudomonas aeruginosa involves the coordinate expression of a wide range of virulence factors including type IV pili which are required for colonization of host tissues and are associated with a form of surface translocation termed twitching motility. Twitching motility in P. aeruginosa is controlled by a complex signal transduction pathway which shares many modules in common with chemosensory systems controlling flagella rotation in bacteria and which is composed, in part, of the previously described proteins PilG, PilH, PilI, PilJ and PilK. Here we describe another three components of this pathway: ChpA, ChpB and ChpC, as well as two downstream genes, ChpD and ChpE, which may also be involved. The central component of the pathway, ChpA, possesses nine potential sites of phosphorylation: six histidine-containing phosphotransfer (HPt) domains, two novel serine- and threonine-containing phosphotransfer (SPt, TPt) domains and a CheY-like receiver domain at its C-terminus, and as such represents one of the most complex signalling proteins yet described in nature. We show that the Chp chemosensory system controls twitching motility and type IV pili biogenesis through control of pili assembly and/or retraction as well as expression of the pilin subunit gene pilA. The Chp system is also required for full virulence in a mouse model of acute pneumonia.
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    Journal Title
    Molecular Microbiology
    Volume
    52
    Issue
    3
    DOI
    https://doi.org/10.1111/j.1365-2958.2004.04026.x
    Subject
    Biological Sciences
    Agricultural and Veterinary Sciences
    Medical and Health Sciences
    Publication URI
    http://hdl.handle.net/10072/178992
    Collection
    • Journal articles

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