Colicin M hydrolyses branched lipids II from Gram-positive bacteria |
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Authors: | Patin Delphine Barreteau Hélène Auger Geneviève Magnet Sophie Crouvoisier Muriel Bouhss Ahmed Touzé Thierry Arthur Michel Mengin-Lecreulx Dominique Blanot Didier |
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Institution: | Univ Paris-Sud, Laboratoire des Enveloppes Bactériennes et Antibiotiques, UMR 8619, Orsay, F-91405, France. |
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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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Keywords: | Branched lipid II Chemo-enzymatic synthesis Colicin M Gram-positive bacteria Peptidoglycan |
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