ArticleJournal of bacteriology2012
CspR, a cold shock RNA-binding protein involved in the long-term survival and the virulence of Enterococcus faecalis.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Insights into ecology, pathogenesis, and biofilm formation ofMicrobiology and molecular biology reviews : MMBR · 2025Review
- Leptospira interrogans biofilm transcriptome highlights adaption to starvation and general stress while maintaining virulence.NPJ biofilms and microbiomes · 2024Article
- Review
- Role of cold shock proteins B and D inInfection and immunity · 2024Article
- From Stress Tolerance to Virulence: Recognizing the Roles of Csps in Pathogenicity and Food Contamination.Pathogens (Basel, Switzerland) · 2024Review
- Identification of the RNA-binding domain-containing protein RbpA that acts as a global regulator of the pathogenicity ofVirulence · 2022Article
- Deciphering the global roles of Cold shock proteins inFrontiers in microbiology · 2022Article
- Article
- Review
- Cold Shock Proteins Promote Nisin Tolerance inFrontiers in microbiology · 2021Article
- Adaptation to Adversity: the Intermingling of Stress Tolerance and Pathogenesis in Enterococci.Microbiology and molecular biology reviews : MMBR · 2019Review
- Interplay of cold shock protein E with an uncharacterized protein, YciF, lowers porin expression and enhances bile resistance inThe Journal of biological chemistry · 2019Article
- Article
- Contribution of the cold shock protein CspA to virulence in Xanthomonas oryzae pv. oryzae.Molecular plant pathology · 2019Article
- The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus.Nucleic acids research · 2018Article
- Review
- Cold-Shock Domain Family Proteins (Csps) Are Involved in Regulation of Virulence, Cellular Aggregation, and Flagella-Based Motility inFrontiers in cellular and infection microbiology · 2017Article
- Galleria mellonella infection models for the study of bacterial diseases and for antimicrobial drug testing.Virulence · 2016Review
- Cold Shock Proteins: A Minireview with Special Emphasis on Csp-family of Enteropathogenic Yersinia.Frontiers in microbiology · 2016Review
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 ΔcspR 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 ΔcspR 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 ΔcspR 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 ΔcspR 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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