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| Título: | PorZ, an Essential Component of the Type IX Secretion System of Porphyromonas gingivalis, Delivers Anionic Lipopolysaccharide to the PorU Sortase for Transpeptidase Processing of T9SS Cargo Proteins |
Autor: | Madej, Mariusz; Nowakowska, Zuzanna; Ksiazek, Miroslaw; Lasica, Anna M.; Mizgalska, Danuta; Nowak, Magdalena; Jacula, Anna; Bzowska, Monika; Scavenius, Carsten; Enghild, Jan J.; Aduse-Opoku, Joseph; Curtis, Michael A.; Gomis-Rüth, F. Xavier CSIC ORCID ; Potempa, Jan | Palabras clave: | Porphyromonas gingivalis T9SS Gingipains Lipopolysaccharide Secretion |
Fecha de publicación: | ene-2021 | Editor: | American Society for Microbiology | Citación: | mBio 12(1): 02262-20 (2021) | Resumen: | Cargo proteins of the type IX secretion system (T9SS) in human pathogens from the Bacteroidetes phylum invariably possess a conserved C-terminal domain (CTD) that functions as a signal for outer membrane (OM) translocation. In Porphyromonas gingivalis, the CTD of cargos is cleaved off after translocation, and anionic lipopolysaccharide (A-LPS) is attached. This transpeptidase reaction anchors secreted proteins to the OM. PorZ, a cell surface-associated protein, is an essential component of the T9SS whose function was previously unknown. We recently solved the crystal structure of PorZ and found that it consists of two β-propeller moieties, followed by a CTD. In this study, we performed structure-based modeling, suggesting that PorZ is a carbohydrate-binding protein. Indeed, we found that recombinant PorZ specifically binds A-LPS in vitro. Binding was blocked by monoclonal antibodies that specifically react with a phosphorylated branched mannan in the anionic polysaccharide (A-PS) component of A-LPS, but not with the core oligosaccharide or the lipid A endotoxin. Examination of A-LPS derived from a cohort of mutants producing various truncations of A-PS confirmed that the phosphorylated branched mannan is indeed the PorZ ligand. Moreover, purified recombinant PorZ interacted with the PorU sortase in an A-LPS-dependent manner. This interaction on the cell surface is crucial for the function of the “attachment complex” composed of PorU, PorZ, and the integral OM β-barrel proteins PorV and PorQ, which is involved in posttranslational modification and retention of T9SS cargos on the bacterial surface. | Descripción: | © 2021 Madej et al. | Versión del editor: | http://dx.doi.org/10.1128/mBio.02262-20 | URI: | http://hdl.handle.net/10261/263267 | DOI: | 10.1128/mBio.02262-20 | E-ISSN: | 2150-7511 |
| Aparece en las colecciones: | (IBMB) Artículos |
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| PorZ, an Essential Component_Madej_PV_Art2021.pdf | 2,34 MB | Adobe PDF |  Visualizar/Abrir |
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