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(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.)

Assembly of an atypical alpha-macroglobulin complex from &ITPseudomonas aeruginosa&IT

Texto completo
Zouhir, Samira [1] ; Robert-Genthon, Mylene [2] ; Trindade, Daniel Maragno [1] ; Job, Viviana [3] ; Nedeljkovic, Marko [3] ; Breyton, Cecile [3] ; Ebel, Christine [3] ; Attree, Ina [2] ; Dessen, Andrea [1, 3]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] CNPEM, Brazilian Biosci Natl Lab LNBio, Campinas, SP - Brazil
[2] Univ Grenoble Alpes, Bacterial Pathogenesis & Cellular Responses Grp, Inst Biosci & Biotechnol Grenoble BIG, Grenoble - France
[3] Univ Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble - France
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: SCIENTIFIC REPORTS; v. 8, JAN 11 2018.
Citações Web of Science: 0

Alpha-2-macroglobulins (A2Ms) are large spectrum protease inhibitors that are major components of the eukaryotic immune system. Pathogenic and colonizing bacteria, such as the opportunistic pathogen Pseudomonas aeruginosa, also carry structural homologs of eukaryotic A2Ms. Two types of bacterial A2Ms have been identified: Type I, much like the eukaryotic form, displays a conserved thioester that is essential for protease targeting, and Type II, which lacks the thioester and to date has been poorly studied despite its ubiquitous presence in Gram-negatives. Here we show that MagD, the Type II A2M from P. aeruginosa that is expressed within the six-gene mag operon, specifically traps a target protease despite the absence of the thioester motif, comforting its role in protease inhibition. In addition, analytical ultracentrifugation and small angle scattering show that MagD forms higher order complexes with proteins expressed in the same operon (MagA, MagB, and MagF), with MagB playing the key stabilization role. A P. aeruginosa strain lacking magB cannot stably maintain MagD in the bacterial periplasm, engendering complex disruption. This suggests a regulated mechanism of Mag complex formation and stabilization that is potentially common to numerous Gram-negative organisms, and that plays a role in periplasm protection from proteases during infection or colonization. (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