The Cold Shock Response of &lt;i&gt;Lactobacillus casei:&lt;/i&gt; Relation between HPr Phosphorylation and Resistance to Freeze/Thaw Cycles

Beaufils, Sophie; Sauvageot, Nicolas; Mazé, Alain; Laplace, Jean-Marie; Auffray, Yanick; Deutscher, Josef; Hartke, Axel

doi:10.1159/000103598

Cited by 21 publications

(21 citation statements)

References 85 publications

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“…HPr is involved in the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) and implicated in the concomitant uptake and phosphorylation of carbohydrates. The cold induction of this protein has already been observed for B. subtilis (20) and Lactobacillus sakei (2). Interestingly, some of the putative CspR targets seem to have a role in the translation process and/or cold shock response.…”

Section: Discussionmentioning

confidence: 71%

CspR, a Cold Shock RNA-Binding Protein Involved in the Long-Term Survival and the Virulence of Enterococcus faecalis

et al. 2012

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By coprecipitation, we identified RNA-binding proteins in the Gram-positive opportunistic pathogen Enterococcus faecalis known to be deficient of the RNA chaperone Hfq. In particular, we characterized one belonging to the cold shock protein (Csp) family (Ef2925) renamed CspR for cold shock protein RNA binding. Compared to the wild-type strain, the Δ cspR mutant was less virulent in an insect infection model ( Galleria mellonella ) and exhibited a decreased persistence in mouse kidneys and a low survival rate in peritoneal macrophages. As expected, we found that the Δ cspR mutant strain was more impaired in its growth than the parental strain under cold conditions and in its long-term survival under nutrient starvation. All these phenotypes were restored after complementation of the Δ cspR mutant. In addition, Western blot analysis showed that CspR was overexpressed under cold shock conditions and in the stationary phase. Since CspR may act as an RNA chaperone, putative targets were identified using a global proteomic approach completed with transcriptomic assays. This study revealed that 19 proteins were differentially expressed in the Δ cspR strain (9 upregulated, 10 downregulated) and that CspR mainly acted at the posttranscriptional level. These data highlight for the first time the role of the RNA-binding protein CspR as a regulator in E. faecalis and its requirement in stress response and virulence in this important human pathogen.

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Section: Discussionmentioning

confidence: 71%

CspR, a Cold Shock RNA-Binding Protein Involved in the Long-Term Survival and the Virulence of Enterococcus faecalis

et al. 2012

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“…In addition, various L. casei mutants affected in CCR exhibited reduced growth rates at low temperatures compared to that of the wild-type strain. Finally, the two mutants that were unable to form P-Ser-HPr (ptsH1 and hprK) showed an almost 100-fold-reduced survival rate after repeated freezing and thawing compared to the wild-type strain and other ptsH and ccpA mutants (47). It is not yet understood how the ability to form P-Ser-HPr increases the resistance to freezing and thawing.…”

Section: Discussionmentioning

confidence: 99%

“…The hrsA gene codes for a fructose-like EIIABC, and it was renamed mngA when it was found to catalyze the transport of the osmolyte 2-O-␣-mannosyl-D-glycerate (775). A connection between the cold shock response and the PTS was also inferred by the finding that an L. casei ptsH(Ile47Thr) mutant overproduced CspA (47), one of the small cold shock proteins found in most bacteria. Csps are normally among the first proteins overproduced in response to a cold shock.…”

Section: Discussionmentioning

confidence: 99%

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How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

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1,189

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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“…The results of this study may impact future cell therapy development efforts. Several novel cell-based therapy projects are currently focused on treating Parkinson's disease, congestive heart failure, and trophic ulcers of the lower limbs, to name a few (Polgar and Ng 2007;Tao and Li 2007;Sedov et al 2007). …”

Section: Introductionmentioning

confidence: 99%

CD90 Expression on human primary cells and elimination of contaminating fibroblasts from cell cultures

et al. 2009

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Cluster Differentiation 90 (CD90) is a cell surface glycoprotein originally identified on mouse thymocytes. Although CD90 has been identified on a variety of stem cells and at varying levels in non-lymphoid tissues such as on fibroblasts, brain cells, and activated endothelial cells, the knowledge about the levels of CD90 expression on different cell types, including human primary cells, is limited. The goal of this study was to identify CD90 as a human primary cell biomarker and to develop an efficient and reliable method for eliminating unwanted or contaminating fibroblasts from human primary cell cultures suitable for research pursuant to cell based therapy technologies.

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The Cold Shock Response of <i>Lactobacillus casei:</i> Relation between HPr Phosphorylation and Resistance to Freeze/Thaw Cycles

Cited by 21 publications

References 85 publications

CspR, a Cold Shock RNA-Binding Protein Involved in the Long-Term Survival and the Virulence of Enterococcus faecalis

CspR, a Cold Shock RNA-Binding Protein Involved in the Long-Term Survival and the Virulence of Enterococcus faecalis

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

CD90 Expression on human primary cells and elimination of contaminating fibroblasts from cell cultures

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