Roles of Cyclic Diguanylate in the Regulation of Bacterial Pathogenesis

Tamayo, Rita; Pratt, Jason T.; Camilli, Andrew

doi:10.1146/annurev.micro.61.080706.093426

Cited by 429 publications

(427 citation statements)

References 91 publications

(115 reference statements)

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“…However, recombinant proteins EIL fimK and AIL fimK expressed PDE activity, and only AIL fimK exhibited lower enzyme activity levels. When responding to different internal and external signals, the sensory modules, such as PAS, GAF, HAMP, REC and HTH domains, commonly present with the GGDEF, EAL and HD-GYP domains, activate diguanylate cyclase or PDE activity (Ho et al, 2000;Galperin et al, 2001;Christen et al, 2005;Tamayo et al, 2007;Cruz et al, 2012). FimK exerted higher PDE activity when the N-terminal DNA-binding domain was removed, suggesting that PDE activity may be activated after the N-terminal domain is stimulated by a specific signal.…”

Section: Discussionmentioning

confidence: 99%

FimK regulation on the expression of type 1 fimbriae in Klebsiella pneumoniae CG43S3

Wang

Huang

et al. 2013

Microbiology

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Section: Discussionmentioning

confidence: 99%

FimK regulation on the expression of type 1 fimbriae in Klebsiella pneumoniae CG43S3

Wang

Huang

et al. 2013

Microbiology

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“…This fact suggests the possibility that MyD88-dependent cross-interference may protect the host from pathogenic bacteria infected with bacteriophages. Second, because various types of bacteria express the STING ligands cyclic di-GMP/AMP (35,36), it is plausible that the STING-type I IFN pathway is activated by these bacteria-derived ligands. Thus, the MyD88-dependent signaling interference, described here, may protect the host from extracellular bacteria as well.…”

Section: Discussionmentioning

confidence: 99%

Beneficial innate signaling interference for antibacterial responses by a Toll-like receptor–mediated enhancement of the MKP-IRF3 axis

Negishi

Matsuki

Endo

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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A major function of innate immune receptors is to recognize pathogen-associated molecular patterns and then evoke immune responses appropriate to the nature of the invading pathogen(s). Because innate immune cells express various types of these receptors, distinct combinations of signaling pathways are activated in response to a given pathogen. Although the conventional wisdom is that these signaling pathways cooperate with one another to ensure an effective host response, a more nuanced view recognizes antagonism between the individual pathways, where the attenuation of a signaling pathway(s) by others may shape the immune response. In this study, we show that, on Listeria monocytogenes infection, Toll-like receptor-triggered MyD88 signaling pathways suppress type I IFN gene induction, which is detrimental to macrophage bactericidal activity. These pathways target and suppress the IFN regulatory factor 3 (IRF3) transcription factor that is activated by the stimulator of IFN genes-TANK-binding kinase-1 kinase pathway. We also provide evidence for the involvement of the MAPK phosphatase family members, which renders IRF3 hypophosphorylated on Toll-like receptor signaling by enhancing the formation of an MAPK phosphatase-IRF3-TANK-binding kinase-1 ternary complex. This study, therefore, reveals a hitherto unrecognized and important contribution of a beneficial innate signaling interference against bacterial infections.signaling cross-talk | host defense | innate immune response

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“…Cyclic-di-GMP controls critical transitions such as the switch from a planktonic state to the formation of a biofilm (1,2). It also controls virulence in many pathogenic bacterial species (5,6).…”

mentioning

confidence: 99%

Structural basis of differential ligand recognition by two classes of bis-(3′-5′)-cyclic dimeric guanosine monophosphate-binding riboswitches

Smith

Shanahan

Moore

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

106

195

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The bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) signaling pathway regulates biofilm formation, virulence, and other processes in many bacterial species and is critical for their survival. Two classes of c-di-GMP-binding riboswitches have been discovered that bind this second messenger with high affinity and regulate diverse downstream genes, underscoring the importance of RNA receptors in this pathway. We have solved the structure of a c-di-GMP-II riboswitch, which reveals that the ligand is bound as part of a triplex formed with a pseudoknot. The structure also shows that the guanine bases of c-di-GMP are recognized through noncanonical pairings and that the phosphodiester backbone is not contacted by the RNA. Recognition is quite different from that observed in the c-di-GMP-I riboswitch, demonstrating that at least two independent solutions for RNA second messenger binding have evolved. We exploited these differences to design a c-di-GMP analog that selectively binds the c-di-GMP-II aptamer over the c-di-GMP-I RNA. There are several bacterial species that contain both types of riboswitches, and this approach holds promise as an important tool for targeting one riboswitch, and thus one gene, over another in a selective fashion.

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Roles of Cyclic Diguanylate in the Regulation of Bacterial Pathogenesis

Cited by 429 publications

References 91 publications

FimK regulation on the expression of type 1 fimbriae in Klebsiella pneumoniae CG43S3

FimK regulation on the expression of type 1 fimbriae in Klebsiella pneumoniae CG43S3

Beneficial innate signaling interference for antibacterial responses by a Toll-like receptor–mediated enhancement of the MKP-IRF3 axis

Structural basis of differential ligand recognition by two classes of bis-(3′-5′)-cyclic dimeric guanosine monophosphate-binding riboswitches

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