Document Detail

PilT is required for PI(3,4,5)P3-mediated crosstalk between Neisseria gonorrhoeae and epithelial cells.
MedLine Citation:
PMID:  16098215     Owner:  NLM     Status:  MEDLINE    
The retractile type IV pilus participates in a number of fundamental bacterial processes, including motility, DNA transformation, fruiting body formation and attachment to host cells. Retraction of the N. gonorrhoeae type IV pilus requires a functional pilT. Retraction generates substantial force on its substrate (> 100 pN per retraction event), and it has been speculated that epithelial cells sense and respond to these forces during infection. We provide evidence that piliated, Opa non-expressing Neisseria gonorrhoeae activates the stress-responsive PI-3 kinase/Akt (PKB) pathway in human epithelial cells, and activation is enhanced by a functional pilT. PI-3 kinase inhibitors wortmannin and LY294002 reduce cell entry by 81% and 50%, respectively, illustrating the importance of this cascade in bacterial invasion. PI-3 kinase and its direct downstream effectors [PI(3,4,5)P3] and Akt are concentrated in the cell cortex beneath adherent bacteria, particularly at the periphery of the bacterial microcolonies. Furthermore, [PI(3,4,5)P3] is translocated to the outer leaflet of the plasma membrane. Finally, we show that [PI(3,4,5)P3] stimulates microcolony formation and upregulates pilT expression in vitro. We conclude that N. gonorrhoeae activation of PI-3 kinase triggers the host cell to produce a lipid second messenger that influences bacterial behaviour.
Shaun W Lee; Dustin L Higashi; Aurelie Snyder; Alexey J Merz; Laura Potter; Magdalene So
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cellular microbiology     Volume:  7     ISSN:  1462-5814     ISO Abbreviation:  Cell. Microbiol.     Publication Date:  2005 Sep 
Date Detail:
Created Date:  2005-08-15     Completed Date:  2006-02-21     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  100883691     Medline TA:  Cell Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1271-84     Citation Subset:  IM    
Department of Molecular Microbiology and Immunology, L220, Oregon Health and Science University, Portland, OR 97239-3098, USA.
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MeSH Terms
1-Phosphatidylinositol 3-Kinase / antagonists & inhibitors,  metabolism
Adenosine Triphosphatases / metabolism*
Androstadienes / pharmacology
Bacterial Adhesion
Bacterial Proteins / metabolism*
Cell Line, Tumor
Cell Membrane / metabolism
Chromones / pharmacology
Enzyme Activation
Epithelial Cells / metabolism*,  microbiology
Fimbriae, Bacterial / metabolism*
Molecular Motor Proteins / metabolism*
Morpholines / pharmacology
Neisseria gonorrhoeae / metabolism,  physiology*
Phosphatidylinositols / metabolism*
Protein Binding
Proto-Oncogene Proteins c-akt / metabolism
Signal Transduction
Grant Support
Reg. No./Substance:
0/Androstadienes; 0/Bacterial Proteins; 0/Chromones; 0/Molecular Motor Proteins; 0/Morpholines; 0/Phosphatidylinositols; 0/phosphoinositide-3,4,5-triphosphate; 154447-36-6/2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; 19545-26-7/wortmannin; EC 3-Kinase; EC Proteins c-akt; EC 3.6.1.-/Adenosine Triphosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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