» Articles » PMID: 1510445

Analysis of Peptidoglycan Precursors in Vancomycin-resistant Enterococci

Overview
Specialty Pharmacology
Date 1992 Jul 1
PMID 1510445
Citations 20
Authors
Affiliations
Soon will be listed here.
Abstract

Analysis by high-pressure liquid chromatography of the cytoplasmic peptidoglycan precursors of a high- and a low-level vancomycin-resistant Enterococcus spp. was performed before and after induction of resistance. This analysis showed a decrease of the D-Ala-D-Ala and UDP-MurNac-pentapeptide pools, an increase of the UDP-MurNac-tripeptide pool, and the appearance of new UDP-MurNac-containing material. These results lead us to suggest that the vancomycin-induced carboxypeptidase activity cleaves the D-Ala-D-Ala (L. Gutmann, D. Billot-Klein, S. Al-Obeid, I. Klare, S. Francoul, E. Collatz, and J. van Heijenoort, Antimicrob. Agents Chemother. 36:77-80, 1992), which in turn would prevent formation of the normal UDP-MurNac-pentapeptide and thereby of the vancomycin target. The novel UDP-MurNac-containing material is thought to correspond to peptidoglycan precursors which might be synthesized by an alternate pathway (T. D. H. Bugg, G. D. Wright, S. Dutka-Malen, M. Arthur, P. Courvalin, and C. T. Walsh, Biochemistry 30:10408-10415, 1991) and which would be unable to bind vancomycin in glycopeptide-resistant enterococci.

Citing Articles

Regulation of Resistance in Vancomycin-Resistant Enterococci: The VanRS Two-Component System.

Guffey A, Loll P Microorganisms. 2021; 9(10).

PMID: 34683347 PMC: 8541618. DOI: 10.3390/microorganisms9102026.


Effect of Vancomycin on Cytoplasmic Peptidoglycan Intermediates and Operon mRNA Levels in VanA-Type Vancomycin-Resistant Enterococcus faecium.

Gargvanshi S, Vemula H, Gutheil W J Bacteriol. 2021; 203(16):e0023021.

PMID: 34060906 PMC: 8297532. DOI: 10.1128/JB.00230-21.


Hidden Mode of Action of Glycopeptide Antibiotics: Inhibition of Wall Teichoic Acid Biosynthesis.

Singh M, Chang J, Coffman L, Kim S J Phys Chem B. 2017; 121(16):3925-3932.

PMID: 28368603 PMC: 6013045. DOI: 10.1021/acs.jpcb.7b00324.


Quantification of the d-Ala-d-Lac-Terminated Peptidoglycan Structure in Vancomycin-Resistant Enterococcus faecalis Using a Combined Solid-State Nuclear Magnetic Resonance and Mass Spectrometry Analysis.

Chang J, Foster E, Yang H, Kim S Biochemistry. 2017; 56(4):612-622.

PMID: 28040891 PMC: 6906607. DOI: 10.1021/acs.biochem.6b00774.


vanM, a new glycopeptide resistance gene cluster found in Enterococcus faecium.

Xu X, Lin D, Yan G, Ye X, Wu S, Guo Y Antimicrob Agents Chemother. 2010; 54(11):4643-7.

PMID: 20733041 PMC: 2976141. DOI: 10.1128/AAC.01710-09.


References
1.
Bugg T, Arthur M, Courvalin P, WALSH C . Identification of vancomycin resistance protein VanA as a D-alanine:D-alanine ligase of altered substrate specificity. Biochemistry. 1991; 30(8):2017-21. DOI: 10.1021/bi00222a002. View

2.
Courvalin P . Resistance of enterococci to glycopeptides. Antimicrob Agents Chemother. 1990; 34(12):2291-6. PMC: 172048. DOI: 10.1128/AAC.34.12.2291. View

3.
Duncan K, van Heijenoort J, WALSH C . Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli. Biochemistry. 1990; 29(9):2379-86. DOI: 10.1021/bi00461a023. View

4.
Williamson R, Al-Obeid S, Shlaes J, Goldstein F, Shlaes D . Inducible resistance to vancomycin in Enterococcus faecium D366. J Infect Dis. 1989; 159(6):1095-104. DOI: 10.1093/infdis/159.6.1095. View

5.
Gondre B, Flouret B, van Heijenoort J . Release of D-alanyl-D-alanine from the precursor of the cell wall peptidoglycan by a peptidase of Escherichia coli K 12. Biochimie. 1973; 55(6):685-91. DOI: 10.1016/s0300-9084(73)80022-7. View