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Porphyromonas gingivalis bundled fimbriae interact with outer membrane vesicles, commensals and fibroblasts

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Porphyromonas Gingivalis

SUBMITTER: Christian Preisinger

LAB HEAD: Prof. Dr. Georg Conrads

PROVIDER: PXD070506 | Pride | 2025-12-30

REPOSITORIES: Pride

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			Action	DRS
	20250801_124350_1071_GeCon.sne	Other
	20250901_182620_1127_GeCon.sne	Other
	GeCon_Report_1071_BGS_Factory_Report_Normal.tsv	Tabular
	GeCon_Report_1071_CP_01_with_unique_iBAQ.tsv	Tabular
	GeCon_Report_1127_BGS_Factory_Report_Normal.tsv	Tabular

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Project description:Background The Gram-negative bacteria Fusobacterium nucleatum and Porphyromonas gingivalis are associated with periodontitis and members of a complex microbial biofilm. The self-produced extracellular polymeric matrix (EPM) of biofilms generally consists of lipids, exopolysaccharides, nucleic acids and proteins. The proteinaceous components of the biofilm matrix play many roles in biofilm development and function. In this study the protein composition of the matrices in mono- and dual-species biofilms of F. nucleatum and P. gingivalis were analyzed. Methods The bacteria were grown in a static biofilm model. Extraction of EPM was performed by careful mechanical shearing and filtration. Initial tryptic digestion of EPMs was followed by liquid chromatography-tandem mass spectrometry to analyze the resulting peptide mixtures. Quantitative proteomic software MaxQuant was then employed for protein identifications and label-free quantitative (LFQ) analysis. Functional analyses of identified proteins were applied in classification and prediction of their possible roles in EPM. Results We identified 542 proteins in the matrix of F. nucleatum, 93 proteins in the matrix of P. gingivalis and 280 proteins in the dual-species biofilm matrix. Similarly, relative quantification based on LFQ intensity scores identified generally higher protein amounts in F. nucleatum and dual species EMPs, when compared to P. gingivalis EPM. Acetyl-CoA acetyltransferase, alkyl hydroperoxide reductase C22 protein, neutrophil-activating protein A, tryptophanase and glutamate dehydrogenase were the top five proteins in the matrix of F. nucleatum biofilm. The oxidoreductase NAD-specific glutamate dehydrogenase and the proteolytic and adhesive protein Lys-gingipain were most abundant in P. gingivalis EPM. In the dual species EPM, F. nucleatum contributed to four out of the five with glutamate dehydrogenase on top. NAD-specific dehydrogenase from P. gingivalis was among the top five. Functional analyses with respect to virulence for example, revealed the stress-induced protein yicC in F. nucleatum EPM, while hemagglutinin HagA and fimbriae minor component FimD were among the top 5 in P. gingivalis EPM. Conclusions We showed that the biofilm matrix of two important periodontal pathogens is abundant in proteins and nearly 70% of all EPM proteins originate from F. nucleatum when grown together with P. gingivalis. Outer membrane proteins, virulence related and oxidative stress proteins were among the most abundant proteins identified.

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Porphyromonas gingivalis bundled fimbriae interact with outer membrane vesicles, commensals and fibroblasts

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