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ProteomicsProduction and properties of adhesin-free gingipain proteinase RgpA
To obtain RgpA free of adhesin requires a means of separating the RgpA catalytic domain from the adhesins domains or adaptation of a method to prevent RgpA complex association.In this study, recombinant suicide plasmids were designed for use in homologous recombination with the rgpA locus so as to p...
ORGANISM(S): Porphyromonas gingivalis W50 
2023-06-02 | PXD036859 | Pride
Lc-msms 
ProteomicsO-glycoproteome of Tannerella forsythia
Tannerella forsythia is a Gram-negative oral pathogen known to possess an O-glycosylation system responsible for targeting multiple proteins associated with virulence at the three-residue motif (D)(S/T)(A/I/L/V/M/T). Multiple proteins have been identified to be decorated with a decasaccharide glycan...
ORGANISM(S): Tannerella forsythia 
2021-10-12 | PXD026989 | Pride
Tannerella forsythia O-glycosylation Trifluoromethanesulfonic acid 
ProteomicsO-glycoproteome of Porphyromonas gingivalis
Porphyromonas gingivalis is an important human pathogen and also a model organism for the Bacteroidetes phylum. O-glycosylation has been reported in this phylum with findings that include the O-glycosylation motif, the structure of the O-glycans in a few species and an extensive O-glycoproteome anal...
ORGANISM(S): Porphyromonas gingivalis ATCC 33277 
2022-02-15 | PXD028120 | Pride
Porphyromonas gingivalis Glycan biosynthesis O-glycosylation Trifluoromethanesulfonic acid 
ProteomicsCharacterization of the O-Glycoproteome of Prevotella intermedia
Prevotella intermedia is a Gram-negative bacterium belonging to the Bacteroidetes phylum and is notably linked to periodontitis. Several other species within this phylum have been reported to possess the general O-glycosylation system, and the O-glycoproteome has been well characterized in Tannerell...
ORGANISM(S): Prevotella intermedia ATCC 25611 = DSM 20706 
2024-02-14 | PXD047143 | Pride
Outer membrane vesicles O-glycosylation Bacteroidetes Type ix secretion system 
ProteomicsLocalisation of outer membrane proteins in Treponema denticola by quantitative proteome analyses of outer membrane vesicles and cellular fractions
The identification and localisation of outer membrane proteins (Omps) and lipoproteins in pathogenic treponemes such as T. denticola (periodontitis) and T. pallidum (syphilis) has been challenging largely due to the structural uniqueness of their outer membranes (OM), the high abundance of inner mem...
ORGANISM(S): Treponema denticola ATCC 35405 
2019-02-20 | PXD011495 | Pride
Treponema denticola Localization Outer membrane vesicles Bacterial lipoproteins Maxquant Outer membrane proteins Orbitrap 
ProteomicsGingipain transpeptidation - Porphyromonas gingivalis Gingipains Display Transpeptidation Activity
Porphyromonas gingivalis is a keystone periodontal pathogen that has been associated with autoimmune disorders. The cell surface proteases Lys-gingipain (Kgp) and Arg-gingipains (RgpA and RgpB) are major virulence factors and their proteolytic activity is enhanced by small peptides such as glycylgly...
ORGANISM(S): Homo sapiens (Human) 
2018-07-11 | PXD009950 | Pride
Transpeptidation Hemoglobin Gingipains Porphyromonas gingivalis 
ProteomicsNear atomic structure of the PorKN rings, disulfie bonded to PorG and bound to the Attachment Complexes, provide mechanistic insights into the Type IX Secretion System
The Type IX Secretion System exports proteins across the outer membrane (OM) of bacteria in the Bacteroidota phylum, however, the mechanistic details remain unknown. Here, we present a 3.5 angstrom cryo-EM structure of the periplasmic rings comprising 32-33 subunits each of PorK and PorN. Additional...
ORGANISM(S): Porphyromonas gingivalis W50 
2025-08-25 | PXD062800 | Pride
Type 9 secretion system Porphyromonas gingivalis 
ProteomicsNear atomic structure of the PorKN rings, disulfide bonded to PorG and bound to Attachment Complexes, provides mechanistic insights into the type IX secretion system: CE and Co-immunoprecipitation
The Type IX Secretion System exports proteins across the outer membrane (OM) of bacteria in the Bacteroidota phylum, however, the mechanistic details remain unknown. Here, we present a ~3.5Å cryo-EM structure of the periplasmic rings comprising 32-33 subunits each of PorK and PorN. Additionally, we ...
ORGANISM(S): Porphyromonas gingivalis ATCC 33277 Porphyromonas gingivalis (strain ATCC BAA-308 / W83) 
2025-07-21 | PXD062825 | Pride
Porphyromonas gingivalis Type ix secretion system 
ProteomicsPorphyromonas gingivalis Outer Membrane Vesicle and cell Proteome in heme excess and heme limited
Porphyromonas gingivalis is an anaerobic, Gram-negative oral pathogen associated with chronic periodontitis. P. gingivalis has an obligate requirement for heme which it obtains from the host. Heme availability has been linked to disease initiation and progression. In this study we used continuous cu...
ORGANISM(S): Porphyromonas gingivalis W50 
2018-05-18 | PXD009730 | Pride
Porphyromonas gingivalis Heme Maxquant Outer membrane vesicles 
TranscriptomicsPorphyromonas gingivalis 33277 wild-type vs Fur orthologue Har isogenic mutant ECR455
Porphyromonas gingivalis is a major pathogen associated with the microbial biofilm-mediated disease chronic periodontitis. P. gingivalis has an obligate requirement for iron and protoporphyrin IX which it satisfies by transporting heme and iron liberated from the human host. The level of cellular ir...
ORGANISM(S): Porphyromonas gingivalis ATCC 33277 
2015-04-01 | E-GEOD-37099 | biostudies-arrayexpress
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