Porphyromonas gingivalis Sphingolipids Affect Early Responses of Macrophages to Outer Membrane Vesicles (OMVs)
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ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE313285 | GEO | 2026/04/30
REPOSITORIES: GEO
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Project description:The outer membrane vesicles (OMVs) produced by Porphyromonas gingivalis (P. gingivalis) contain a variety of bioactive molecules that may be involved in the progression of periodontitis. However, the participation of P. gingivalis OMVs in the development of periodontitis has not been elucidated. Here we isolated P. gingivalis OMVs and confirmed their participation in periodontitis both in vivo and in vitro. Microcomputed Tomography (micro-CT) and histological analysis showed that under the stimulation of P. gingivalis OMVs, the alveolar bone of rats was significantly resorbed in vivo. We found that P. gingivalis OMVs were taken up by hPDLCs (human Periodontal Ligament Cells, hPDLCs) in vitro, then subsequently resulting in apoptosis and inflammatory cytokines releasing which was accomplished by the microRNA-size small RNAs (msRNAs) sRNA45033 in the P. gingivalis OMVs. Through bioinformatics analysis and screening of target genes, Chromobox 5 (CBX5) was identified as the downstream target of screened-out small RNA s45033. Using dual-luciferase reporter assay, overexpression, and knockdown methods, s45033 was confirmed to target CBX5 to regulate hPDLCs apoptosis. In addition, Cleavage Under Targets and Tagmentation (Cut&Tag) analysis confirmed the mechanism that CBX5 regulates apoptosis through the methylation of p53 DNA. Collectively, these findings indicate that the role of P. gingivalis OMVs is immunologically relevant and related to bacterial virulence in the development of periodontitis.
2022-11-30 | GSE218606 | GEO
Project description:Porphyromonas gingivalis Sphingolipids Affect Early Responses of Macrophages to Outer Membrane Vesicles (OMVs)
| PRJNA1378875 | ENA
Project description: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 culture of the bacterium to determine the effect of heme limitation and excess on the P. gingivalis proteome. Four biological replicates of whole cell lysate (WCL) and outer membrane vesicle (OMV) samples were digested with trypsin and analysed by tandem mass spectrometry and MaxQuant label-free quantification. In total, 1211 proteins were quantified with 108 and 49 proteins significantly changing in abundance more than 1.5-fold (p<0.05) in the WCLs and OMVs respectively. The proteins most upregulated in response to heme limitation were those involved in binding and transporting heme while the four proteins most upregulated in the heme excess condition constitute a putative heme efflux system. In general, the protein abundance ratios obtained for OMVs and WCLs agreed, indicating that changes to the OM protein composition are passed on to OMVs, however 16 proteins were preferentially packaged into OMVs in one condition more than the other. In particular, moonlighting cytoplasmic proteins were preferentially associated with OMVs under heme excess.
2018-05-18 | PXD009730 | Pride
Project description:Genotyping studies suggest that there is genetic variability among P. gingivalis strains, however the extent of variability remains unclear, and the regions of variability have only partially been identified. We previously used heteroduplex analysis of the ribosomal operon intergenic spacer region (ISR) to type P. gingivalis strains in several diverse populations, identifying 6 predominant heteroduplex types and many minor ones. In addition we used ISR sequence analysis to determine the relatedness of P. gingivalis strains to one another, and demonstrated a link between ISR sequence phylogeny and the disease-associated phenotype of P. gingivalis strains. The availability of whole genome microarrays based on the genomic sequence of strain W83 has allowed a more comprehensive analysis of P. gingivalis strain variability, using the entire genome. The objectives of this study were to define the phylogeny of P. gingivalis strains using the entire genome, to compare the phylogeny based on genome content to the phylogeny based on a single locus (ISR), and to identify genes that are associated with the strongly disease-associated strain W83 that could be important for virulence. Keywords: Comparative genomic hybridization
2008-10-09 | GSE13128 | GEO
Project description:Porphyromonas gingivalis plays a key role in periodontal disease and has been associated with several serious systemic diseases. Its fimbriae are a major virulence factor. We re-cently demonstrated the formation of bundles of long FimA fimbriae in strain ATCC 33277. Transmission (TEM) and scanning electron microscopy (SEM) were used to exam-ine a collection of P. gingivalis strains representing all seven known FimA genotypes (I, Ib, IIa, IIb, III–V) and a P. gulae strain (type A). Additionally, two P. gingivalis strains (ATCC 49417 and 84Pg1) were investigated in dual species approaches with Fusobacterium nucle-atum, Streptococcus oralis, and human gingival fibroblasts. To evaluate a suspected connec-tion with the fimbriae accessory proteins FimCDE, proteomic analysis of outer membrane vesicles (OMVs) was performed. Bundling was confirmed to occur regardless of FimA genotype but is impaired by strong capsule formation. For the first time fimbri-ae-associated OMVs (FAVs) were observed. Tubular and chain-like extensions of the outer membrane (OMEs) were identified in most strains examined, including P. gulae. Bundled fimbriae, FAVs, and OMEs were further suggested to connect to F. nucleatum and S. oralis. Proteome analysis revealed ratios of FimA to accessory proteins to be approximately 13:1 for FimC and FimD and approximately 7:1 for FimE. The results imply more accessory proteins per fimbriae or short FimA fimbriae in OMVs. Since FimCDE is known to be re-sponsible for the adhesion properties and autoaggregation of FimA fimbriae, we propose that it could also mediate the stability of bundled fimbriae and the binding of OMVs to (bundled) fimbriae.
2025-12-30 | PXD070506 | Pride
Project description:Genotyping studies suggest that there is genetic variability among P. gingivalis strains, however the extent of variability remains unclear, and the regions of variability have only partially been identified. We previously used heteroduplex analysis of the ribosomal operon intergenic spacer region (ISR) to type P. gingivalis strains in several diverse populations, identifying 6 predominant heteroduplex types and many minor ones. In addition we used ISR sequence analysis to determine the relatedness of P. gingivalis strains to one another, and demonstrated a link between ISR sequence phylogeny and the disease-associated phenotype of P. gingivalis strains. The availability of whole genome microarrays based on the genomic sequence of strain W83 has allowed a more comprehensive analysis of P. gingivalis strain variability, using the entire genome. The objectives of this study were to define the phylogeny of P. gingivalis strains using the entire genome, to compare the phylogeny based on genome content to the phylogeny based on a single locus (ISR), and to identify genes that are associated with the strongly disease-associated strain W83 that could be important for virulence. Keywords: Comparative genomic hybridization Comparative genomic analysis of 7 clinically prevalent P. gingivalis strains was performed, using whole genome microarrays based on the sequence of strain W83. Strain W83 was the reference strains and there were 6 test strains. Flip-dye replicates were performed.
2010-05-18 | E-GEOD-13128 | biostudies-arrayexpress
Project description:Porphyromonas gingivalis is a keystone periodontal pathogen implicated in a variety of diseases ranging from periodontitis to Alzheimer’s disease. A hallmark of P. gingivalis is the constitutive production of a peptidyl-arginine deiminase (PPAD), which converts positively charged arginine residues into charge-neutral citrulline residues. The PPAD enzyme is known to be localized to the bacterial outer membrane and outer membrane vesicles (OMVs). Our present study was aimed at dissecting the roles of PPAD in the bacterial evasion of human macrophages and passage of cellular barriers. Here, we show that PPAD is required for activity of the arginine-specific proteases RgpA and RgpB, which are critical virulence factors of P. gingivalis. Furthermore, we show that the absence of PPAD leads to an increased OMV charge. Both changes impact the immune evasion strategy of P. gingivalis, as the PPAD-deficient bacteria display increased biofilm formation while their ability to evade and kill human macrophages is strongly reduced. In fact, PPAD-deficient bacteria and OMVs are more effectively internalized by macrophages and they elicit altered inflammatory macrophage responses, as demonstrated by reduced secretion of pro-inflammatory cytokines and major changes in the macrophage proteome. Intriguingly, we show that P. gingivalis OMVs have a high propensity for in vitro blood-brain barrier passage through transcytosis, which is significantly increased by PPAD-deficiency. This implies that OMV citrullination is a critical determinant for trafficking of P. gingivalis-derived vesicles within the human host. Altogether, our present findings explain how PPAD shapes the immunomodulatory and invasive properties of P. gingivalis and its OMVs.
2026-05-14 | PXD066207 | Pride
Project description:Wild type Porphyromonas gingivalis strain ATCC33277 (V3176) and PG1626 - deficient mutant (V3177) were grown in iron replete conditions was used to compare to Porphyromonas gingivalis strains grown in iron chelated conditions.
2023-06-08 | GSE174493 | GEO
Project description:Aerobic transcriptome of Porphyromonas gingivalis
| PRJNA119925 | ENA
Project description:Porphyromonas gingivalis comparative genomic hybridization
| PRJNA109673 | ENA