Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB‐type enterococci

Baptista, Manuela; Depardieu, Florence; Reynolds, Peter E.; Courvalin, Patrice; Arthur, Michel

doi:10.1046/j.1365-2958.1997.4401812.x

Cited by 89 publications

(125 citation statements)

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“…Transcription of the vanA and vanB clusters is regulated by the VanRS and VanR,S, two-component regulatory systems (Arthur et al, 1992;Evers & Courvalin, 1996). Phosphorylation of the VanR response regulator enhances the affinity of the protein for the regulatory regions of the PR and PH promoters and allows transcription of the regulatory (vanRS) and resistance ( u a n H A X Y Z ) genes, respectively (Holman et al, 1994;Arthur et al, 1997). Similarly, VanR, is required for activation of the PRB and PYB promoters located upstream from the regulatory and resistance genes of the uanB cluster (Evers & Courvalin, 1996;Silva et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

“…Similarly, VanR, is required for activation of the PRB and PYB promoters located upstream from the regulatory and resistance genes of the uanB cluster (Evers & Courvalin, 1996;Silva et al, 1998). The level of phosphorylation of VanR and VanR, is modulated by the kinase and phosphatase activities of the Vans and Vans, sensors, respectively (Wright et al, 1993;Arthur et al, 1997;Baptista et al, 1997). The response regulators can also be activated by kinases encoded by the host chromosome in the absence of their partner sensors (Arthur et al, 1997;Silva et al, 1998;Baptista et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

“…The level of phosphorylation of VanR and VanR, is modulated by the kinase and phosphatase activities of the Vans and Vans, sensors, respectively (Wright et al, 1993;Arthur et al, 1997;Baptista et al, 1997). The response regulators can also be activated by kinases encoded by the host chromosome in the absence of their partner sensors (Arthur et al, 1997;Silva et al, 1998;Baptista et al, 1999). VanH VanHB 67% v a n x Van& 71% Baptista et al (1996) This work Baptista et al (1999) Baptista et al ( ) Baptista et al (1999 mutants (Arthur et al, 1997) (Table 1).…”

Section: Introductionmentioning

confidence: 99%

“…The response regulators can also be activated by kinases encoded by the host chromosome in the absence of their partner sensors (Arthur et al, 1997;Silva et al, 1998;Baptista et al, 1999). VanH VanHB 67% v a n x Van& 71% Baptista et al (1996) This work Baptista et al (1999) Baptista et al ( ) Baptista et al (1999 mutants (Arthur et al, 1997) (Table 1). Glycopeptides and moenomycin inhibit the transglycosylation reaction by different mechanisms and are structurally unrelated, indicating that induction by these antibiotics is unlikely to involve direct interaction of the Vans sensor with the drugs (Handwerger & Kolokathis, 1990).…”

Section: Introductionmentioning

confidence: 99%

“…Glycopeptides and moenomycin inhibit the transglycosylation reaction by different mechanisms and are structurally unrelated, indicating that induction by these antibiotics is unlikely to involve direct interaction of the Vans sensor with the drugs (Handwerger & Kolokathis, 1990). Since moenomycin and glycopeptides block incorporation of lipid intermediate I1 into nascent peptidoglycan, accumulation of this precursor may be the signalling stimulus for Vans (Baptista et a[., 1996).…”

Section: Introductionmentioning

confidence: 99%

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Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci

Arthur¹,

Depardieu²,

Courvalin³

1999

Microbiology

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genes, respectively. Under non-inducing conditions, activation of VanR by cross-talk was blocked by the presence of a multicopy plasmid carrying Pw Presence of the high-affinity VanR-binding sites of the regulatory region of PH on the multicopy vector probably sequestered VanR, thereby preventing autoactivation of the PR promoter. Under such circumstances, stimulation of the host kinase by glycopeptides or moenomycin was required for expression of the resistance genes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci

Arthur¹,

Depardieu²,

Courvalin³

1999

Microbiology

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Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Friedman

2010

Chemistry & Biodiversity

162

108

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Exposure of food proteins to certain processing conditions induces two major chemical changes: racemization of all L-amino acids (LAAs) to D-amino acids (DAAs) and concurrent formation of cross-linked amino acids such as lysinoalanine (LAL). The diet contains both processing-induced and naturally-formed DAA. The latter include those found in microorganisms, plants, and marine invertebrates. Racemization impairs digestibility and nutritional quality. Racemization of LAA residues to their D-isomers in food and other proteins is pH-, time-, and temperature-dependent. Although racemization rates of LAA residues in a protein vary, relative rates in different proteins are similar. The nutritional utilization of different DAAs varies widely in animals and humans. Some DAAs may exert both adverse and beneficial biological effects. Thus, although D-Phe is utilized as a nutritional source of L-Phe, high concentrations of D-Tyr in such diets inhibit the growth of mice. Both D-Ser and LAL induce histological changes in the rat kidney. The wide variation in the utilization of DAAs is illustrated by the fact that, whereas D-Meth is largely utilized as a nutritional source of the L-isomer, D-Lys is not. Similarly, although L-CysSH has a sparing effect on L-Meth when fed to mice, D-CysSH does not. Since DAAs are consumed as part of their normal diet, a need exists to develop a better understanding of their roles in foods, microbiology, nutrition, and medicine. To contribute to this effort, this overview surveys our present knowledge of the chemistry, nutrition, safety, microbiology, and pharmacology of DAAs. Also covered are the origin and distribution of DAAs in food and possible roles of DAAs in human physiology, aging, and the etiology and therapy of human diseases.

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Structure‐Based Design of Benzoxazoles as new Inhibitors for D‐Alanyl – D‐Alanine Ligase

et al. 2009

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d-Alanyl -d-alanine ligase is an enzyme which catalyzes the dimerization of d-alanine, and, as such, has an essential role in bacterial cell wall biosynthesis. It has been shown that inhibition of d-alanyl -d-alanine ligase prevents bacterial growth. d-Alanyld-alanine ligase represents therefore a viable antimicrobial target. The 3D structure of this enzyme complexed with a phosphinophosphate inhibitor has been reported, which allows for structure-based design studies. Four softwares (LUDI, MCSS, Autodock, and Glide) developed either for fragment or full-molecule docking were compared and scored for their ability to position in the active site four prototypic ligands: two inhibitors, i.e. a phosphinophosphate derivative and d-cycloserine, d-alanine and d-alanyl -d-alanine. Best performances were obtained with Glide and MCSS. A short series of novel derivatives based on a 2-phenylbenzoxazole scaffold was designed de novo on the basis of computational data. The best compound was found to fully inhibit the d-alanyld-alanine ligase of E. faecalis with an IC 50 of 400 mM.

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Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB‐type enterococci

Cited by 89 publications

References 30 publications

Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci

Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Structure‐Based Design of Benzoxazoles as new Inhibitors for D‐Alanyl – D‐Alanine Ligase

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