Cyclic di-GMP signalling and the regulation of bacterial virulence

Robert P. Ryan

    Research output: Contribution to journalArticle

    50 Citations (Scopus)

    Abstract

    Signal transduction pathways involving the second messenger cyclic di-GMP [bis-(3'-5')-cyclic di-guanosine monophosphate] occur widely in bacteria where they act to link perception of environmental or intracellular cues and signals to specific alterations in cellular function. Such alterations can contribute to bacterial lifestyle transitions including biofilm formation and virulence. The cellular levels of the nucleotide are controlled through the opposing activities of diguanylate cyclases (DGCs) and phosphodiesterases (PDEs). The GGDEF domain of DGCs catalyses the synthesis of cyclic di-GMP from GTP, whereas EAL or HD-GYP domains in different classes of PDE catalyse cyclic di-GMP degradation to pGpG and GMP. We are now beginning to understand how alterations in cyclic di-GMP exert a regulatory action through binding to diverse receptors or effectors that include a small 'adaptor' protein domain called PilZ, transcription factors and riboswitches. The regulatory action of enzymically active cyclic di-GMP signalling proteins is, however, not restricted to an influence on the level of nucleotide. Here, I will discuss our recent findings that highlight the role that protein-protein interactions involving these signalling proteins have in regulating functions that contribute to bacterial virulence.
    Original languageEnglish
    Pages (from-to)1286-1297
    Number of pages12
    JournalMicrobiology
    Volume159
    Issue number7
    DOIs
    Publication statusPublished - Jul 2013

    Fingerprint

    Cyclic GMP
    Virulence
    Phosphoric Diester Hydrolases
    Proteins
    Nucleotides
    Riboswitch
    Second Messenger Systems
    Biofilms
    Guanosine Triphosphate
    Cues
    Life Style
    Signal Transduction
    Transcription Factors
    Bacteria
    diguanylate cyclase

    Cite this

    Ryan, Robert P. / Cyclic di-GMP signalling and the regulation of bacterial virulence. In: Microbiology. 2013 ; Vol. 159, No. 7. pp. 1286-1297.
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    abstract = "Signal transduction pathways involving the second messenger cyclic di-GMP [bis-(3'-5')-cyclic di-guanosine monophosphate] occur widely in bacteria where they act to link perception of environmental or intracellular cues and signals to specific alterations in cellular function. Such alterations can contribute to bacterial lifestyle transitions including biofilm formation and virulence. The cellular levels of the nucleotide are controlled through the opposing activities of diguanylate cyclases (DGCs) and phosphodiesterases (PDEs). The GGDEF domain of DGCs catalyses the synthesis of cyclic di-GMP from GTP, whereas EAL or HD-GYP domains in different classes of PDE catalyse cyclic di-GMP degradation to pGpG and GMP. We are now beginning to understand how alterations in cyclic di-GMP exert a regulatory action through binding to diverse receptors or effectors that include a small 'adaptor' protein domain called PilZ, transcription factors and riboswitches. The regulatory action of enzymically active cyclic di-GMP signalling proteins is, however, not restricted to an influence on the level of nucleotide. Here, I will discuss our recent findings that highlight the role that protein-protein interactions involving these signalling proteins have in regulating functions that contribute to bacterial virulence.",
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    Cyclic di-GMP signalling and the regulation of bacterial virulence. / Ryan, Robert P.

    In: Microbiology, Vol. 159, No. 7, 07.2013, p. 1286-1297.

    Research output: Contribution to journalArticle

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    AB - Signal transduction pathways involving the second messenger cyclic di-GMP [bis-(3'-5')-cyclic di-guanosine monophosphate] occur widely in bacteria where they act to link perception of environmental or intracellular cues and signals to specific alterations in cellular function. Such alterations can contribute to bacterial lifestyle transitions including biofilm formation and virulence. The cellular levels of the nucleotide are controlled through the opposing activities of diguanylate cyclases (DGCs) and phosphodiesterases (PDEs). The GGDEF domain of DGCs catalyses the synthesis of cyclic di-GMP from GTP, whereas EAL or HD-GYP domains in different classes of PDE catalyse cyclic di-GMP degradation to pGpG and GMP. We are now beginning to understand how alterations in cyclic di-GMP exert a regulatory action through binding to diverse receptors or effectors that include a small 'adaptor' protein domain called PilZ, transcription factors and riboswitches. The regulatory action of enzymically active cyclic di-GMP signalling proteins is, however, not restricted to an influence on the level of nucleotide. Here, I will discuss our recent findings that highlight the role that protein-protein interactions involving these signalling proteins have in regulating functions that contribute to bacterial virulence.

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