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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa

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da Mata Madeira, Paulo Vinicius [1] ; Zouhir, Samira [1] ; Basso, Pauline [2, 3, 4, 5, 6] ; Neves, David [1] ; Laubier, Aurelie [7, 8] ; Salacha, Richard [7, 8] ; Bleves, Sophie [7, 8] ; Faudry, Eric [2, 3, 4, 5, 6] ; Contreras-Martel, Carlos [2, 3, 4, 9] ; Dessen, Andrea [1, 2, 3, 4, 9]
Total Authors: 10
[1] CNPEM, Brazilian Natl Lab Biosci LNBio, Sao Paulo - Brazil
[2] CNRS, IBS, Grenoble - France
[3] BIG, Grenoble - France
[4] CEA Grenoble, IBS, F-38054 Grenoble - France
[5] Univ Grenoble Alpes, Bacterial Pathogenesis & Cellular Responses Grp, Inst Biosci & Biotechnol Grenoble BIG, Grenoble - France
[6] INSERM, Biol Canc & Infect Lab, UMR S 1036, Grenoble - France
[7] CNRS, Marseille - France
[8] Aix Marseille Univ, Inst Microbiol Mediterranee, Lab Ingn Syst Macromol, UMR7255, Marseille - France
[9] Univ Grenoble Alpes, IBS, Grenoble - France
Total Affiliations: 9
Document type: Journal article
Source: Journal of Molecular Biology; v. 428, n. 9, A, p. 1790-1803, MAY 8 2016.
Web of Science Citations: 9

The type V secretion system is a macromolecular machine employed by a number of bacteria to secrete virulence factors into the environment. The human pathogen Pseudomonas aeruginosa employs the newly described type Vd secretion system to secrete a soluble variant of PIpD, a lipase of the patatin-like family synthesized as a single macromolecule that also carries a polypeptide transport-associated domain and a 16-stranded beta-barrel. Here we report the crystal structure of the secreted form of PIpD in its biologically active state. PIpD displays a classical lipase alpha/beta hydrolase fold with a catalytic site located within a highly hydrophobic channel that entraps a lipidic molecule. The active site is covered by a flexible lid, as in other lipases, indicating that this region in PlpD must modify its conformation in order for catalysis at the water lipid interface to occur. PlpD displays phospholipase A(1) activity and is able to recognize a number of phosphatidylinositols and other phosphatidyl analogs. PIpD is the first example of an active phospholipase secreted through the type V secretion system, for which there are more than 200 homologs, revealing details of the lipid destruction arsenal expressed by P. aeruginosa in order to establish infection. (C) 2016 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 11/52067-6 - Assembly and structure of macromolecular complexes involved in bacterial cell wall: biosynthesis and virulence
Grantee:Andrea Dessen de Souza e Silva
Support type: Research Projects - SPEC Program
FAPESP's process: 13/01962-0 - Structure and function of bacterial virulence factors
Grantee:Samira Zouhir
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 14/11980-9 - Identification and structural characterization of new compounds for PBPs inhibition
Grantee:Paulo Vinicius da Mata Madeira
Support type: Scholarships in Brazil - Doctorate