Busca avançada
Ano de início
(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

Texto completo
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]
Número total de Autores: 10
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 9
Tipo de documento: Artigo Científico
Fonte: Journal of Molecular Biology; v. 428, n. 9, A, p. 1790-1803, MAY 8 2016.
Citações Web of Science: 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)

Processo FAPESP: 11/52067-6 - Estruturação de complexos macromoleculares da parede bacteriana: biossíntese e virulência
Beneficiário:Andrea Dessen de Souza e Silva
Linha de fomento: Auxílio à Pesquisa - Programa SPEC
Processo FAPESP: 13/01962-0 - Estrutura e função de fatores de virulência bacterianos
Beneficiário:Samira Zouhir
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 14/11980-9 - Identificação e caracterização estrutural de novos compostos inibidores de PBPs
Beneficiário:Paulo Vinicius da Mata Madeira
Linha de fomento: Bolsas no Brasil - Doutorado