Abstract
The intrinsic ruggedness of Enterococcus faecalis is responsible for its widespread distribution in nature and is often viewed as an important virulence determinant. Previously, we showed that the ClpB ATPase is negatively regulated by CtsR and is required for thermotolerance and virulence in a Galleria mellonella invertebrate model. Here, we used in silico, Northern blot and quantitative real-time PCR analyses to identify additional members of the CtsR regulon, namely the clpP peptidase and the clpC and clpE ATPases. When compared to the parent strain, virulence of the ΔctsR strain in G. mellonella was significantly attenuated.
Keywords:
Enterococcus faecalis; Thermotolerance; Virulence; clp genes; ctsR regulon.
MeSH terms
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Adenosine Triphosphatases / biosynthesis*
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism
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Animals
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Bacterial Proteins / biosynthesis*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Base Sequence
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Endopeptidase Clp / biosynthesis
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Endopeptidase Clp / metabolism
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Enterococcus faecalis / genetics*
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Enterococcus faecalis / metabolism
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Enterococcus faecalis / pathogenicity*
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Gene Expression Regulation, Bacterial
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Heat-Shock Proteins / biosynthesis*
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Heat-Shock Proteins / genetics
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Heat-Shock Proteins / metabolism
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Heat-Shock Response / genetics
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Lepidoptera / microbiology*
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Promoter Regions, Genetic
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Repressor Proteins / biosynthesis*
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Repressor Proteins / genetics
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Repressor Proteins / metabolism
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Virulence
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Virulence Factors / biosynthesis
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Virulence Factors / genetics
Substances
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Bacterial Proteins
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ClpC protein, Bacteria
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CtsR protein, bacteria
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Heat-Shock Proteins
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Repressor Proteins
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Virulence Factors
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Endopeptidase Clp
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Adenosine Triphosphatases
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ClpE protein, bacteria