PG1058 Is a Novel Multidomain Protein Component of the Bacterial Type IX Secretion System
Jacqueline E Heath, Christine A Seers, Paul D Veith, Catherine A Butler, Nor A Nor Muhammad, Yu-Yen Chen, Nada Slakeski, Benjamin Peng, Lianyi Zhang, Stuart G Dashper, Keith J Cross, Steven M Cleal, Caroline Moore, Eric C Reynolds
PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2016
Porphyromonas gingivalis utilises the Bacteroidetes-specific type IX secretion system (T9SS) to export proteins across the outer membrane (OM), including virulence factors such as the gingipains. The secreted proteins have a conserved carboxy-terminal domain essential for type IX secretion that is cleaved upon export. In P. gingivalis the T9SS substrates undergo glycosylation with anionic lipopolysaccharide (A-LPS) and are attached to the OM. In this study, comparative analyses of 24 Bacteroidetes genomes identified ten putative novel components of the T9SS in P. gingivalis, one of which was PG1058. Computer modelling of the PG1058 structure predicted a novel N- to C-terminal architecture co..View full abstract
Awarded by Australian Government, Department of Industry, Innovation and Science
Australian Government, Department of Industry, Innovation and Science Grant 20080108. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.