Journal article
Porphyromonas gingivalis Type IX Secretion Substrates Are Cleaved and Modified by a Sortase-Like Mechanism
DG Gorasia, PD Veith, D Chen, CA Seers, HA Mitchell, YY Chen, MD Glew, SG Dashper, EC Reynolds
Plos Pathogens | Published : 2015
Abstract
The type IX secretion system (T9SS) of Porphyromonas gingivalis secretes proteins possessing a conserved C-terminal domain (CTD) to the cell surface. The C-terminal signal is essential for these proteins to translocate across the outer membrane via the T9SS. On the surface the CTD of these proteins is cleaved prior to extensive glycosylation. It is believed that the modification on these CTD proteins is anionic lipopolysaccharide (A-LPS), which enables the attachment of CTD proteins to the cell surface. However, the exact site of modification and the mechanism of attachment of CTD proteins to the cell surface are unknown. In this study we characterized two wbaP (PG1964) mutants that did not ..
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Awarded by National Science Foundation
Funding Acknowledgements
This work was supported by the Australian National Health and Medical Research Council Project Grant Number 1027812. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.