Dataset Information

Characterization of Metronidazole-tolerant Porphyromonas gingivalis Persisters

ABSTRACT: This project investigated the phenotypic characteristics of Metronidazole-tolerant Porphyromonas gingivalis persisters, the relevant modulatory effects of hemin and their underlying survival mechanisms. Proteomic analysis was performed to delineate the protein expression profiles of Metronidazole-tolerant P. gingivalis persister fractions and the controls incubated with different levels of hemin supplementation.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Porphyromonas Gingivalis Atcc 33277

SUBMITTER: Peng Li

LAB HEAD: Lijian Jin

PROVIDER: PXD008976 | Pride | 2018-08-29

REPOSITORIES: Pride

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Publications

Controlled cellular redox, repressive hemin utilization and adaptive stress responses are crucial to metronidazole tolerance of Porphyromonas gingivalis persisters.

Li Peng P Fung Yi-Man Eva YE Yin Xiaohui X Seneviratne Chaminda J CJ Che Chi-Ming CM Jin Lijian L

Journal of clinical periodontology 20181001 10

<h4>Background</h4>Antimicrobial-tolerant microbial persisters critically account for various infections and inflammation. This study identified the characteristics of Porphyromonas gingivalis persisters, and explored their underlying survival mechanisms through proteomic profiling.<h4>Methods</h4>Porphyromonas gingivalis cultured with different concentrations of hemin was treated with 100 μg/ml of metronidazole (MTZ). The viability of P. gingivalis persisters was determined by colony-forming un ...[more]

PMID: 30125959

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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.

Dataset Information

Characterization of Metronidazole-tolerant Porphyromonas gingivalis Persisters

Publications

Controlled cellular redox, repressive hemin utilization and adaptive stress responses are crucial to metronidazole tolerance of Porphyromonas gingivalis persisters.

Similar Datasets

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