Towards discovery of inhibitors of the undecaprenyl-pyrophosphate phosphatase BacA by virtual high-throughput screening

Autor: Marko Jukič, Rodolphe Auger, Victor Folcher, Matic Proj, Hélène Barreteau, Stanislav Gobec, Thierry Touzé

Publikováno v: Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 2360-2371 (2022)

Increasing resistance to common antibiotics is becoming a major challenge that requires the development of new antibacterial agents. Peptidoglycan is an essential heteropolymer of the bacterial envelope that ensures the integrity and shape of all bac

Externí odkaz: https://doaj.org/article/c46b1d1a607541adb2ed8da2b9d1a317

LpxT-Dependent Phosphorylation of Lipid A in Escherichia coli Increases Resistance to Deoxycholate and Enhances Gut Colonization

Autor: Xudong Tian, Guillaume Manat, Elise Gasiorowski, Rodolphe Auger, Samia Hicham, Dominique Mengin-Lecreulx, Ivo Gomperts Boneca, Thierry Touzé

Publikováno v: Frontiers in Microbiology, Vol 12 (2021)

The cell surface of Gram-negative bacteria usually exhibits a net negative charge mostly conferred by lipopolysaccharides (LPS). This property sensitizes bacterial cells to cationic antimicrobial peptides, such as polymyxin B, by favoring their bindi

Externí odkaz: https://doaj.org/article/4fe97d1e463f46199baca02806b86190

Membrane Topology and Biochemical Characterization of the Escherichia coli BacA Undecaprenyl-Pyrophosphate Phosphatase.

Autor: Guillaume Manat, Meriem El Ghachi, Rodolphe Auger, Karima Baouche, Samir Olatunji, Frédéric Kerff, Thierry Touzé, Dominique Mengin-Lecreulx, Ahmed Bouhss

Publikováno v: PLoS ONE, Vol 10, Iss 11, p e0142870 (2015)

Several integral membrane proteins exhibiting undecaprenyl-pyrophosphate (C55-PP) phosphatase activity were previously identified in Escherichia coli that belonged to two distinct protein families: the BacA protein, which accounts for 75% of the C55-

Externí odkaz: https://doaj.org/article/1701164c9a5a47f2961811ce12dcb10e

Insight into the dual function of lipid phosphate phosphatase PgpB involved in two essential cell-envelope metabolic pathways in Escherichia coli

Autor: Dominique Mengin-Lecreulx, Rodolphe Auger, Xudong Tian, Guillaume Manat, Frédéric Kerff, Thierry Touzé

Publikováno v: Scientific Reports
Scientific Reports, Nature Publishing Group, 2020, 10 (1), pp.13209. ⟨10.1038/s41598-020-70047-5⟩
Scientific Reports, Vol 10, Iss 1, Pp 1-15 (2020)
Scientific Reports, 2020, 10 (1), pp.13209. ⟨10.1038/s41598-020-70047-5⟩

Ubiquitous PAP2 lipid phosphatases are involved in a wide array of central physiological functions. PgpB from Escherichia coli constitutes the archetype of this subfamily of membrane proteins. It displays a dual function by catalyzing the biosynthesi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ad556c92fc380dd2decb210358d06f0
https://hal.archives-ouvertes.fr/hal-02928167

Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis

Autor: Alexandre Lambion, L. Vogeley, Dominique Mengin-Lecreulx, Sophie Roure, Juan-Carlos Rengifo-Gonzalez, Eric Sauvage, Sabine Peslier, Thierry Touzé, Paulette Charlier, Meriem El Ghachi, Frédéric Kerff, Maryline Foglino, Nicole Howe, Annick Guiseppi, Martin Caffrey, Guillaume Manat, François Delbrassine, Rodolphe Auger

Publikováno v: Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, Springer Verlag, 2017, 74 (12), pp.2319--2332. ⟨10.1007/s00018-017-2464-6⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2017, 74 (12), pp.2319--2332. 〈10.1007/s00018-017-2464-6〉
Cellular and Molecular Life Sciences, 2017, 74 (12), pp.2319--2332. ⟨10.1007/s00018-017-2464-6⟩

International audience; Type 2 phosphatidic acid phosphatases (PAP2s) can be either soluble or integral membrane enzymes. In bacteria, integral membrane PAP2s play major roles in the metabolisms of glycerophospholipids, undecaprenyl-phosphate (C-55-P

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c36694a3235d12ba5550b68dc81ebdfb
https://hal.archives-ouvertes.fr/hal-01640041