Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and…
- P. Veith, N. N. Nor Muhammad, E. Reynolds
- BiologyJournal of Proteome Research
- 23 September 2013
The CTD cleavage site of 10 different proteins from 3 different species was determined and found to be similar to the Cleavage site previously determined in P. gingivalis, suggesting that homologues of the C-terminal signal peptidase (PG0026) are responsible for the cleavage in these species.
The RgpB C-Terminal Domain Has a Role in Attachment of RgpB to the Outer Membrane and Belongs to a Novel C-Terminal-Domain Family Found in Porphyromonas gingivalis
- C. Seers, N. Slakeski, E. Reynolds
- BiologyJournal of Bacteriology
- 1 September 2006
The results suggest that the C-terminal domain is essential for outer membrane attachment and may be involved in a coordinated process of export and attachment to the cell surface.
PG0026 Is the C-terminal Signal Peptidase of a Novel Secretion System of Porphyromonas gingivalis♦
- M. Glew, P. Veith, E. Reynolds
- BiologyJournal of Biological Chemistry
- 16 May 2012
The data indicate that PG0026 is responsible for the cleavage of the CTD signal after substrates are secreted across the OM and is a novel C-terminal signal peptidase of a new type of secretion system.
Identification of a New Membrane-associated Protein That Influences Transport/Maturation of Gingipains and Adhesins of Porphyromonas gingivalis*
- Keiko Sato, E. Sakai, K. Nakayama
- BiologyJournal of Biological Chemistry
- 11 March 2005
Results suggest that the membrane-associated protein PorT is essential for transport of the kgp, r gpA, rgpB, and hagA gene products across the outer membrane from the periplasm to the cell surface, where they are processed and matured.
Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50.
- P. Veith, G. Talbo, E. Reynolds
- BiologyBiochemical Journal
- 1 April 2002
A proteomic study of the outer membrane of P. gingivalis strain W50 using two-dimensional gel electrophoresis and peptide mass fingerprinting found electrophoretic behaviour of these proteins, together with their immunoreactivity with a monoclonal antibody that recognizes lipopolysaccharide, is consistent with a modification that could anchor the proteins to the outer membranes.
The outer membrane protein LptO is essential for the O‐deacylation of LPS and the co‐ordinated secretion and attachment of A‐LPS and CTD proteins in Porphyromonas gingivalis
- Yu-Yen Chen, B. Peng, E. Reynolds
- Biology, ChemistryMolecular Microbiology
- 1 March 2011
The results suggest that LPS deacylation by LptO is linked to the co‐ordinated secretion of A‐LPS and CTD proteins by a novel secretion and attachment system to form a structured surface layer.
A Novel Porphyromonas gingivalis FeoB Plays a Role in Manganese Accumulation*
- S. Dashper, C. Butler, E. Reynolds
- BiologyJournal of Biological Chemistry
- 29 July 2005
Results indicate that FeoB2 is not involved in iron transport but plays a novel role in manganese transport.
Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors.
- P. Veith, Yu-Yen Chen, E. Reynolds
- BiologyJournal of Proteome Research
- 3 April 2014
Cryo-transmission electron microscopy analysis revealed that an electron dense surface layer known to comprise CTD proteins accounted for a large proportion of the OMVs' volume providing an explanation for the enrichment of CTDprotein, finding that P. gingivalis is able to specifically concentrate and release a large number of its virulence factors into the environment in the form of OMVs.
Mass spectrometric analyses of peptides and proteins in human gingival crevicular fluid.
- L. H. Ngo, P. Veith, Yu-Yen Chen, Dina Chen, I. Darby, E. Reynolds
- Biology, MedicineJournal of Proteome Research
- 22 January 2010
Thirty-three of the identified proteins, such as actin and the actin binding proteins profilin, cofilin and gelsolin, have not been reported inGCF before and are reported in GCF here for the first time.
Structural Insights into the PorK and PorN Components of the Porphyromonas gingivalis Type IX Secretion System
- D. G. Gorasia, P. Veith, E. Reynolds
- BiologyPLoS Pathogens
- 1 August 2016
PorK and PorN were protected from proteinase K cleavage when present in undisrupted cells, but were rapidly degraded when the cells were lysed, which suggests that the ring-shaped PorK/N complex may form part of the secretion channel of the T9SS.
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