Glycopeptide Resistance

2011 ◽  
pp. 515-542 ◽  
Author(s):  
Bruno Périchon ◽  
Patrice Courvalin
Keyword(s):  
Glycopeptide Resistance

Glycopeptide Resistance in Coagulase-Negative Staphylococci

2000 ◽  
Vol 19 (6) ◽  
pp. 403-417 ◽  
Author(s):  
F. Biavasco ◽  
C. Vignaroli ◽  
P. E. Varaldo
Keyword(s):  
Coagulase Negative Staphylococci ◽  
Glycopeptide Resistance

scholarly journals Whole Genome Sequencing and Complete Genetic Analysis Reveals Novel Pathways to Glycopeptide Resistance in Staphylococcus aureus

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e21577 ◽  
Author(s):  
Adriana Renzoni ◽  
Diego O. Andrey ◽  
Ambre Jousselin ◽  
Christine Barras ◽  
Antoinette Monod ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Genetic Analysis ◽  
Whole Genome Sequencing ◽  
Genome Sequencing ◽  
Whole Genome ◽  
Glycopeptide Resistance

scholarly journals Glycopeptide resistance: Links with inorganic phosphate metabolism and cell envelope stress

2017 ◽  
Vol 133 ◽  
pp. 74-85 ◽  
Author(s):  
Fernando Santos-Beneit ◽  
María Ordóñez-Robles ◽  
Juan F. Martín
Keyword(s):  
Inorganic Phosphate ◽  
Cell Envelope ◽  
Phosphate Metabolism ◽  
Glycopeptide Resistance ◽  
Envelope Stress

scholarly journals Putative VanRS-Like Two-Component Regulatory System Associated with the Inducible Glycopeptide Resistance Cluster of Paenibacillus popilliae

2005 ◽  
Vol 49 (7) ◽  
pp. 2625-2633 ◽  
Author(s):  
Henry Fraimow ◽  
Christopher Knob ◽  
Inmaculada A. Herrero ◽  
Robin Patel
Keyword(s):  
Regulatory System ◽  
Growth Curves ◽  
Upstream Region ◽  
Bacillus Halodurans ◽  
Human Pathogens ◽  
Glycopeptide Resistance ◽  
Transposase Gene ◽  
Two Component ◽  
Genes Encoding ◽  
Paenibacillus Lentimorbus

ABSTRACT Paenibacillus popilliae contains vanF encoding a putative d-Ala:d-lactate (d-Lac) ligase, VanF, as part of the vanY F Z F H F FX F cluster that is similar in structure to the enterococcal vanA and vanB clusters. Using growth curves, we demonstrated that vancomycin resistance in P. popilliae is inducible. Using degenerate oligonucleotides targeted at bacterial cell wall ligases, we identified a second ligase gene with features of a d-Ala:d-Ala ligase in both P. popilliae and the related, vancomycin-susceptible, Paenibacillus lentimorbus. The 3,380-bp region upstream of vanY F Z F H F FX F in P. popilliae ATCC 14706 was sequenced and found to contain genes encoding a putative two-component regulator, VanRFSF, similar to VanRS but more closely related to a family of two-component regulators linked to VanY-like carboxypeptidases in several glycopeptide-susceptible Bacillus species. This upstream region also included a transposase similar to a transposase found in Bacillus halodurans and, in some strains, a 99-bp insertion of unknown function with 95% nucleotide identity to a portion of the Tn1546 transposase gene. Analysis of glycopeptide resistance-associated clusters from soil and/or insect-dwelling organisms may provide important clues to the molecular evolution of acquired glycopeptide resistance elements in human pathogens.

scholarly journals Effects of the Movement of Insertion Sequences on the Structure of VanA Glycopeptide Resistance Elements in Enterococcus faecium

2000 ◽  
Vol 44 (5) ◽  
pp. 1362-1364 ◽  
Author(s):  
Ana L. C. Darini ◽  
Marie-France I. Palepou ◽  
Neil Woodford
Keyword(s):  
Structural Change ◽  
Inverted Repeat ◽  
Enterococcus Faecium ◽  
Insertion Sequence ◽  
Host Strain ◽  
Insertion Sequences ◽  
Glycopeptide Resistance ◽  
Related Element

ABSTRACT A Tn1546-related element with IS1216V at position 8839 underwent a structural change after storage of the host strain of Enterococcus faecium at 4°C. The element acquired IS1542 at position 3932, nucleotides 8732 to 8831 were deleted, and the first 3417 nucleotides were lost and replaced by an inverted copy of the IS1216V–vanY–vanZ-inverted-repeat block from the 3′ end. Insertion sequence movement is likely to play a key role in the evolution of VanA resistance elements.

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