Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy. Issue 3 (9th May 2014)
- Record Type:
- Journal Article
- Title:
- Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy. Issue 3 (9th May 2014)
- Main Title:
- Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy
- Authors:
- Wright, Christopher J.
Xue, Peng
Hirano, Takanori
Liu, Chengcheng
Whitmore, Sarah E.
Hackett, Murray
Lamont, Richard J. - Abstract:
- <abstract abstract-type="main" id="mbo3177-abs-0001"> <title>Abstract</title> <p>Interspecies communication between <italic>Porphyromonas gingivalis</italic> and <italic>Streptococcus gordonii</italic> underlies the development of synergistic dual species communities. Contact with <italic>S. gordonii</italic> initiates signal transduction within <italic>P. gingivalis</italic> that is based on protein tyrosine (de)phosphorylation. In this study, we characterize a bacterial tyrosine (BY) kinase (designated Ptk1) of <italic>P. gingivalis</italic> and demonstrate its involvement in interspecies signaling. Ptk1 can utilize ATP for autophosphorylation and is dephosphorylated by the <italic>P. gingivalis</italic> tyrosine phosphatase, Ltp1. Community development with <italic>S. gordonii</italic> is severely abrogated in a <italic>ptk1</italic> mutant of <italic>P. gingivalis</italic>, 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 <italic>S. gordonii</italic>. The <italic>ptk1</italic> 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 <italic>P. gingivalis</italic>. Ptk1 can phosphorylate the capsule related proteins PGN_0224, a UDP‐acetyl‐mannosamine dehydrogenase, and PGN_0613, a UDP‐glucose dehydrogenase, in<abstract abstract-type="main" id="mbo3177-abs-0001"> <title>Abstract</title> <p>Interspecies communication between <italic>Porphyromonas gingivalis</italic> and <italic>Streptococcus gordonii</italic> underlies the development of synergistic dual species communities. Contact with <italic>S. gordonii</italic> initiates signal transduction within <italic>P. gingivalis</italic> that is based on protein tyrosine (de)phosphorylation. In this study, we characterize a bacterial tyrosine (BY) kinase (designated Ptk1) of <italic>P. gingivalis</italic> and demonstrate its involvement in interspecies signaling. Ptk1 can utilize ATP for autophosphorylation and is dephosphorylated by the <italic>P. gingivalis</italic> tyrosine phosphatase, Ltp1. Community development with <italic>S. gordonii</italic> is severely abrogated in a <italic>ptk1</italic> mutant of <italic>P. gingivalis</italic>, 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 <italic>S. gordonii</italic>. The <italic>ptk1</italic> 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 <italic>P. gingivalis</italic>. Ptk1 can phosphorylate the capsule related proteins PGN_0224, a UDP‐acetyl‐mannosamine dehydrogenase, and PGN_0613, a UDP‐glucose dehydrogenase, in <italic>P. gingivalis</italic>. Knockout of <italic>ptk1</italic> in an encapsulated strain of <italic>P. gingivalis</italic> resulted in loss of capsule production. Collectively these results demonstrate that the <italic>P. gingivalis</italic> Ptk1 BY kinase regulates interspecies communication and controls heterotypic community development with <italic>S. gordonii</italic> through adjusting the levels of the Mfa1 adhesin and exopolysaccharide.</p> </abstract> … (more)
- Is Part Of:
- MicrobiologyOpen. Volume 3:Issue 3(2014:Jun.)
- Journal:
- MicrobiologyOpen
- Issue:
- Volume 3:Issue 3(2014:Jun.)
- Issue Display:
- Volume 3, Issue 3 (2014)
- Year:
- 2014
- Volume:
- 3
- Issue:
- 3
- Issue Sort Value:
- 2014-0003-0003-0000
- Page Start:
- 383
- Page End:
- 394
- Publication Date:
- 2014-05-09
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2045-8827 ↗ - DOI:
- 10.1002/mbo3.177 ↗
- Languages:
- English
- ISSNs:
- 2045-8827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3982.xml