Colicin M hydrolyses branched lipids II from Gram-positive bacteria.

Biochimie

Univ Paris-Sud, Laboratoire des Enveloppes Bactériennes et Antibiotiques, UMR 8619, Orsay, F-91405, France.

Published: April 2012

AI Article Synopsis

  • Lipids II from some Gram-positive bacteria were created using radioactive l-lysine-containing UDP-MurNAc-pentapeptide.
  • Specific lateral chains unique to bacteria like Enterococcus faecalis, Enterococcus faecium, and Staphylococcus aureus were added through chemical synthesis techniques.
  • The resulting lipids were hydrolyzed by colicin M from Escherichia coli at similar rates as those found in Gram-negative bacteria, suggesting potential for colicin M as a broad-spectrum antibacterial agent.

Article Abstract

Lipids II found in some Gram-positive bacteria were prepared in radioactive form from l-lysine-containing UDP-MurNAc-pentapeptide. The specific lateral chains of Enterococcus faecalis, Enterococcus faecium and Staphylococcus aureus (di-L-alanine, D-isoasparagine, and pentaglycine, respectively) were introduced by chemical peptide synthesis using the Fmoc chemistry. The branched nucleotides obtained were converted into the corresponding lipids II by enzymatic synthesis using the MraY and MurG enzymes. All of the lipids were hydrolysed by Escherichia coli colicin M at approximately the same rate as the meso-diaminopimelate-containing lipid II found in Gram-negative bacteria, thereby opening the way to the use of this enzyme as a broad spectrum antibacterial agent.

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http://dx.doi.org/10.1016/j.biochi.2011.12.019DOI Listing

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