Journal article

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



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..

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