Journal
MOLECULAR MICROBIOLOGY
Volume 79, Issue 2, Pages 533-551Publisher
WILEY
DOI: 10.1111/j.1365-2958.2010.07470.x
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Funding
- US National Institutes of Health (NIH) [AI25098]
- US NIH [AI080937, U54 AI057157]
- National Science Foundation [AI25098, MCB0645876]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI025098, U19AI090872, K22AI080937, U54AI057157, R29AI025098] Funding Source: NIH RePORTER
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P>Cyclic di-GMP (c-di-GMP) is a signalling molecule that governs the transition between planktonic and biofilm states. Previously, we showed that the diguanylate cyclase HmsT and the putative c-di-GMP phosphodiesterase HmsP inversely regulate biofilm formation through control of HmsHFRS-dependent poly-beta-1,6-N-acetylglucosamine synthesis. Here, we systematically examine the functionality of the genes encoding putative c-di-GMP metabolic enzymes in Yersinia pestis. We determine that, in addition to hmsT and hmsP, only the gene y3730 encodes a functional enzyme capable of synthesizing c-di-GMP. The seven remaining genes are pseudogenes or encode proteins that do not function catalytically or are not expressed. Furthermore, we show that HmsP has c-di-GMP-specific phosphodiesterase activity. We report that a mutant incapable of c-di-GMP synthesis is unaffected in virulence in plague mouse models. Conversely, an hmsP mutant, unable to degrade c-di-GMP, is defective in virulence by a subcutaneous route of infection due to poly-beta-1,6-N-acetylglucosamine overproduction. This suggests that c-di-GMP signalling is not only dispensable but deleterious for Y. pestis virulence. Our results show that a key event in the evolution of Y. pestis from the ancestral Yersinia pseudotuberculosis was a significant reduction in the complexity of its c-di-GMP signalling network likely resulting from the different disease cycles of these human pathogens.
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