Cargando…
Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle
Tyrosine phosphorylation modifies the functionality of bacterial proteins and forms the basis of a versatile and tunable signal transduction system. The integrated action of tyrosine kinases and phosphatases controls bacterial processes important for metabolism and virulence. Porphyromonas gingivali...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8863745/ https://www.ncbi.nlm.nih.gov/pubmed/35224543 http://dx.doi.org/10.3389/froh.2022.835586 |
_version_ | 1784655297420197888 |
---|---|
author | Lamont, Richard J. Miller, Daniel P. |
author_facet | Lamont, Richard J. Miller, Daniel P. |
author_sort | Lamont, Richard J. |
collection | PubMed |
description | Tyrosine phosphorylation modifies the functionality of bacterial proteins and forms the basis of a versatile and tunable signal transduction system. The integrated action of tyrosine kinases and phosphatases controls bacterial processes important for metabolism and virulence. Porphyromonas gingivalis, a keystone pathogen in periodontal disease, possesses an extensive phosphotyrosine signaling network. The phosphorylation reaction is catalyzed by a bacterial tyrosine (BY) kinase, Ptk1, and a Ubiquitous bacterial Kinase UbK1. Dephosphorylation is mediated by a low-molecular-weight phosphatase, Ltp1 and a polymerase and histidinol phosphatase, Php1. Phosphotyrosine signaling controls exopolysaccharide production, gingipain activity, oxidative stress responses and synergistic community development with Streptococcus gordonii. Additionally, Ltp1 is secreted extracellularly and can be delivered inside gingival epithelial cells where it can override host cell signaling and readjust cellular physiology. The landscape of coordinated tyrosine kinase and phosphatase activity thus underlies the adaptive responses of P. gingivalis to both the polymicrobial environment of bacterial communities and the intracellular environment of gingival epithelial cells. |
format | Online Article Text |
id | pubmed-8863745 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-88637452022-02-24 Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle Lamont, Richard J. Miller, Daniel P. Front Oral Health Oral Health Tyrosine phosphorylation modifies the functionality of bacterial proteins and forms the basis of a versatile and tunable signal transduction system. The integrated action of tyrosine kinases and phosphatases controls bacterial processes important for metabolism and virulence. Porphyromonas gingivalis, a keystone pathogen in periodontal disease, possesses an extensive phosphotyrosine signaling network. The phosphorylation reaction is catalyzed by a bacterial tyrosine (BY) kinase, Ptk1, and a Ubiquitous bacterial Kinase UbK1. Dephosphorylation is mediated by a low-molecular-weight phosphatase, Ltp1 and a polymerase and histidinol phosphatase, Php1. Phosphotyrosine signaling controls exopolysaccharide production, gingipain activity, oxidative stress responses and synergistic community development with Streptococcus gordonii. Additionally, Ltp1 is secreted extracellularly and can be delivered inside gingival epithelial cells where it can override host cell signaling and readjust cellular physiology. The landscape of coordinated tyrosine kinase and phosphatase activity thus underlies the adaptive responses of P. gingivalis to both the polymicrobial environment of bacterial communities and the intracellular environment of gingival epithelial cells. Frontiers Media S.A. 2022-02-09 /pmc/articles/PMC8863745/ /pubmed/35224543 http://dx.doi.org/10.3389/froh.2022.835586 Text en Copyright © 2022 Lamont and Miller. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Oral Health Lamont, Richard J. Miller, Daniel P. Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle |
title | Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle |
title_full | Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle |
title_fullStr | Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle |
title_full_unstemmed | Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle |
title_short | Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle |
title_sort | tyrosine kinases and phosphatases: enablers of the porphyromonas gingivalis lifestyle |
topic | Oral Health |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8863745/ https://www.ncbi.nlm.nih.gov/pubmed/35224543 http://dx.doi.org/10.3389/froh.2022.835586 |
work_keys_str_mv | AT lamontrichardj tyrosinekinasesandphosphatasesenablersoftheporphyromonasgingivalislifestyle AT millerdanielp tyrosinekinasesandphosphatasesenablersoftheporphyromonasgingivalislifestyle |