Glycopeptide Resistance in Enterococci

Author(s):  
Florence Depardieu ◽  
Patrice Courvalin
PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e21577 ◽  
Author(s):  
Adriana Renzoni ◽  
Diego O. Andrey ◽  
Ambre Jousselin ◽  
Christine Barras ◽  
Antoinette Monod ◽  
...  

2017 ◽  
Vol 133 ◽  
pp. 74-85 ◽  
Author(s):  
Fernando Santos-Beneit ◽  
María Ordóñez-Robles ◽  
Juan F. Martín

2005 ◽  
Vol 49 (7) ◽  
pp. 2625-2633 ◽  
Author(s):  
Henry Fraimow ◽  
Christopher Knob ◽  
Inmaculada A. Herrero ◽  
Robin Patel

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.


2000 ◽  
Vol 44 (5) ◽  
pp. 1362-1364 ◽  
Author(s):  
Ana L. C. Darini ◽  
Marie-France I. Palepou ◽  
Neil Woodford

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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