Peptidoglycan structure and architecture.
- W. Vollmer, D. Blanot, M. de Pedro
- Biology, ChemistryFEMS Microbiology Reviews
- 1 March 2008
In several species examined, the fine structure of the peptidoglycan significantly varies with the growth conditions, and the different models for the architecture are discussed with respect to structural and physical parameters.
Cytoplasmic steps of peptidoglycan biosynthesis.
- H. Barreteau, Andreja Kovač, A. Boniface, M. Sova, S. Gobec, D. Blanot
- Biology, ChemistryFEMS Microbiology Reviews
- 1 March 2008
This review deals with the cytoplasmic steps of peptidoglycan biosynthesis and the chemical and enzymatic synthesis of the nucleotide precursor substrates that are not commercially available and the search for specific inhibitors that could act as antibacterial compounds.
Peptidoglycan Molecular Requirements Allowing Detection by Nod1 and Nod2*
- S. Girardin, L. Travassos, D. Mengin-Lecreulx
- BiologyJournal of Biological Chemistry
- 24 October 2003
It is shown here that Nod1 and Nod2 have evolved divergent strategies to achieve PG sensing, and how PG processing and modifications, either by host or bacterial enzymes, may affect innate immune responses.
Toll‐like receptor 2‐dependent bacterial sensing does not occur via peptidoglycan recognition
- L. Travassos, S. Girardin, I. Boneca
- BiologyEMBO Reports
- 1 October 2004
It is shown that elicited peritoneal murine macrophages do not produce tumour necrosis factor‐α or interleukin‐6 in response to purified PGs, suggesting that PG detection is more likely to occur intracellularly (through Nod1/Nod2) rather than from the extracellular compartment.
The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection.
- A. Zaidman-Rémy, M. Hervé, B. Lemaître
- BiologyImmunity
- 1 April 2006
Determination of the MurD mechanism through crystallographic analysis of enzyme complexes.
- J. Bertrand, G. Auger, O. Dideberg
- Chemistry, BiologyJournal of Molecular Biology
- 11 June 1999
The crystal structures of three complexes of Escherichia coli MurD with a variety of substrates and products have been determined to high resolution and a key feature in the reaction intermediate is the presence of two magnesium ions bridging negatively charged groups.
The Peptidoglycan of Stationary-Phase Mycobacterium tuberculosis Predominantly Contains Cross-Links Generated by l,d-Transpeptidation
- M. Lavollay, M. Arthur, J. Mainardi
- BiologyJournal of Bacteriology
- 11 April 2008
It is shown that a complex adaptive response thought to endow M. tuberculosis with the capacity to survive several months of combinatorial antibiotic treatment may involve remodeling of the peptidoglycan network by substitution of 4-->3 cross-links generated by the D,D-transpeptidase activity of penicillin-binding proteins by 3-->3Cross- links generated by a transpePTidase of L,D specificity.
Purification and Characterization of the Bacterial MraY Translocase Catalyzing the First Membrane Step of Peptidoglycan Biosynthesis*
- A. Bouhss, M. Crouvoisier, D. Blanot, D. Mengin-Lecreulx
- Biology, ChemistryJournal of Biological Chemistry
- 16 July 2004
Conditions for the high level overproduction and for the first time the purification to homogeneity of milligram quantities of MraY protein are reported.
The bacA Gene of Escherichia coli Encodes an Undecaprenyl Pyrophosphate Phosphatase Activity*
- M. E. Ghachi, A. Bouhss, D. Blanot, D. Mengin-Lecreulx
- BiologyJournal of Biological Chemistry
- 16 July 2004
The bacA gene, the overexpression of which results in bacitracin resistance, was inactivated and shown to be non-essential for growth of Escherichia coli and was overproduced and purified to near homogeneity, revealing the first gene encoding undecaprenyl pyrophosphate phosphatase identified to date.
Crystal structure of UDP‐N‐acetylmuramoyl‐L‐alanine:D‐glutamate ligase from Escherichia coli
- J. Bertrand, G. Auger, O. Dideberg
- Biology, ChemistryEMBO Journal
- 15 June 1997
The study describes the first structure of the UDP‐N‐acetylmuramoyl‐peptide ligase family, which reveals the binding site of the substrate UMA, and comparison with known NTP complexes allows the identification of residues interacting with ATP.
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