ArticleMicrobiologyOpen2014
Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy.
Article in MicrobiologyOpen, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 61 citations in OpenAlex.
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- Characterization and application of in situ curcumin/ZNP hydrogels for periodontitis treatment.BMC oral health · 2024Article
- Porphyromonas gingivalis Tyrosine Kinase Is a Fitness Determinant in Polymicrobial Infections.Infection and immunity · 2022Article
- Tyrosine Kinases and Phosphatases: Enablers of theFrontiers in oral health · 2022Review
- Article
- Phosphorylation of major Porphyromonas gingivalis virulence factors is crucial for their processing and secretion.Molecular oral microbiology · 2021Article
- Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator.Molecular oral microbiology · 2021Article
- Polymicrobial communities in periodontal disease: Their quasi-organismal nature and dialogue with the host.Periodontology 2000 · 2021Review
- A bacterial tyrosine phosphatase modulates cell proliferation through targeting RGCC.PLoS pathogens · 2021Article
- A Novel Regulation of K-antigen Capsule Synthesis inFrontiers in oral health · 2021Article
- Protein Tyrosine and Serine/Threonine Phosphorylation in Oral Bacterial Dysbiosis and Bacteria-Host Interaction.Frontiers in cellular and infection microbiology · 2021Review
- The Roles of FOXO1 in Periodontal Homeostasis and Disease.Journal of immunology research · 2021Review
- Role of the RprY response regulator in P. gingivalis community development and virulence.Molecular oral microbiology · 2020Article
- Association or Causation? Exploring the Oral Microbiome and Cancer Links.Journal of dental research · 2020Article
- A Novel Small Molecule, 1,3-di-m-tolyl-urea, Inhibits and Disrupts Multispecies Oral Biofilms.Microorganisms · 2020Article
- Porphyromonas gingivalis adopts intricate and unique molecular mechanisms to survive and persist within the host: a critical update.Journal of oral microbiology · 2020Review
- A tyrosine phosphoregulatory system controls exopolysaccharide biosynthesis and biofilm formation in Vibrio cholerae.PLoS pathogens · 2020Article
- Porphyromonas gingivalis genes conferring fitness in a tobacco-rich environment.Molecular oral microbiology · 2020Article
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
Interspecies communication between Porphyromonas gingivalis and Streptococcus gordonii underlies the development of synergistic dual species communities. Contact with S. gordonii initiates signal transduction within P. gingivalis that is based on protein tyrosine (de)phosphorylation. In this study, we characterize a bacterial tyrosine (BY) kinase (designated Ptk1) of P. gingivalis and demonstrate its involvement in interspecies signaling. Ptk1 can utilize ATP for autophosphorylation and is dephosphorylated by the P. gingivalis tyrosine phosphatase, Ltp1. Community development with S. gordonii is severely abrogated in a ptk1 mutant of P. gingivalis, indicating that tyrosine kinase activity is required for maximal polymicrobial synergy. Ptk1 controls the levels of the transcriptional regulator CdhR and the fimbrial adhesin Mfa1 which mediates binding to S. gordonii. The ptk1 gene is in an operon with two genes involved in exopolysaccharide synthesis, and similar to other BY kinases, Ptk1 is necessary for exopolysaccharide production in P. gingivalis. Ptk1 can phosphorylate the capsule related proteins PGN_0224, a UDP-acetyl-mannosamine dehydrogenase, and PGN_0613, a UDP-glucose dehydrogenase, in P. gingivalis. Knockout of ptk1 in an encapsulated strain of P. gingivalis resulted in loss of capsule production. Collectively these results demonstrate that the P. gingivalis Ptk1 BY kinase regulates interspecies communication and controls heterotypic community development with S. gordonii through adjusting the levels of the Mfa1 adhesin and exopolysaccharide.
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