PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System

Abstract Porphyromonas gingivalis is a keystone pathogen associated with chronic periodontitis. Major virulence factors named gingipains (cysteine proteinases, RgpA, RgpB and Kgp) are secreted via the Type IX Secretion System (T9SS). These, together with approximately 30 other proteins, are secreted...

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Autores principales:	Michelle D. Glew, Paul D. Veith, Dina Chen, Dhana G. Gorasia, Ben Peng, Eric C. Reynolds
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f4f1dab080e94ec3b9703f64a2ffd9aa
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spelling	oai:doaj.org-article:f4f1dab080e94ec3b9703f64a2ffd9aa2021-12-02T12:32:28ZPorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System10.1038/s41598-017-09412-w2045-2322https://doaj.org/article/f4f1dab080e94ec3b9703f64a2ffd9aa2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-09412-whttps://doaj.org/toc/2045-2322Abstract Porphyromonas gingivalis is a keystone pathogen associated with chronic periodontitis. Major virulence factors named gingipains (cysteine proteinases, RgpA, RgpB and Kgp) are secreted via the Type IX Secretion System (T9SS). These, together with approximately 30 other proteins, are secreted to the cell surface and anchored to the outer membrane by covalent modification to anionic lipopolysaccharide (A-LPS) via the novel Gram negative sortase, PorU. PorU is localised on the cell surface and cleaves the C-terminal domain signal (CTD) of T9SS substrates and conjugates their new C-termini to A-LPS. A 440 kDa-attachment complex was identified in the wild-type (WT) comprising of PorU:PorV:PorQ:PorZ. In mutant strains, sub-complexes comprising PorU:PorV or PorQ:PorZ were also identified at smaller native sizes suggesting that PorU and PorZ are anchored to the cell surface via interaction with the PorV and PorQ outer membrane proteins, respectively. Analysis of porU mutants and a CTD cleavage mutant revealed accumulation of immature T9SS substrates in a PorV-bound form. Quantitative label-free proteomics of WT whole cell lysates estimated that the proportion of secretion channels:attachment complexes:free PorV:T9SS substrates was 1:6:110:2000 supporting a role for PorV as a shuttle protein delivering secreted proteins to the attachment complex for CTD signal cleavage and A-LPS modification.Michelle D. GlewPaul D. VeithDina ChenDhana G. GorasiaBen PengEric C. ReynoldsNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Michelle D. Glew Paul D. Veith Dina Chen Dhana G. Gorasia Ben Peng Eric C. Reynolds PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System
description	Abstract Porphyromonas gingivalis is a keystone pathogen associated with chronic periodontitis. Major virulence factors named gingipains (cysteine proteinases, RgpA, RgpB and Kgp) are secreted via the Type IX Secretion System (T9SS). These, together with approximately 30 other proteins, are secreted to the cell surface and anchored to the outer membrane by covalent modification to anionic lipopolysaccharide (A-LPS) via the novel Gram negative sortase, PorU. PorU is localised on the cell surface and cleaves the C-terminal domain signal (CTD) of T9SS substrates and conjugates their new C-termini to A-LPS. A 440 kDa-attachment complex was identified in the wild-type (WT) comprising of PorU:PorV:PorQ:PorZ. In mutant strains, sub-complexes comprising PorU:PorV or PorQ:PorZ were also identified at smaller native sizes suggesting that PorU and PorZ are anchored to the cell surface via interaction with the PorV and PorQ outer membrane proteins, respectively. Analysis of porU mutants and a CTD cleavage mutant revealed accumulation of immature T9SS substrates in a PorV-bound form. Quantitative label-free proteomics of WT whole cell lysates estimated that the proportion of secretion channels:attachment complexes:free PorV:T9SS substrates was 1:6:110:2000 supporting a role for PorV as a shuttle protein delivering secreted proteins to the attachment complex for CTD signal cleavage and A-LPS modification.
format	article
author	Michelle D. Glew Paul D. Veith Dina Chen Dhana G. Gorasia Ben Peng Eric C. Reynolds
author_facet	Michelle D. Glew Paul D. Veith Dina Chen Dhana G. Gorasia Ben Peng Eric C. Reynolds
author_sort	Michelle D. Glew
title	PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System
title_short	PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System
title_full	PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System
title_fullStr	PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System
title_full_unstemmed	PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System
title_sort	porv is an outer membrane shuttle protein for the type ix secretion system
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f4f1dab080e94ec3b9703f64a2ffd9aa
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PorV is an Outer Membrane Shuttle Protein for the Type IX Secretion System

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