Document Detail


Analysis of immunostimulatory activity of Porphyromonas gingivalis fimbriae conferred by Toll-like receptor 2.
MedLine Citation:
PMID:  20558141     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Bacterial fimbriae are an important pathogenic factor. It has been demonstrated that fimbrial protein encoded by fimA gene (FimA fimbriae) of Porphyromonas gingivalis not only contributes to the abilities of bacterial adhesion and invasion to host cells, but also strongly stimulates host innate immune responses. However, FimA fimbriae separated from P. gingivalis ATCC 33277 using a gentle procedure showed very weak proinflammatory activity compared with previous reports. Therefore, in the present study, biological characteristics of FimA fimbriae were further analyzed in terms of proinflammatory activity in macrophages. Macrophages differentiated from THP-1 cells were stimulated with native, heat-denatured, or either proteinase- or lipoprotein lipase-treated FimA fimbriae of P. gingivalis ATCC 33277. Stimulating activities of these FimA fimbriae were evaluated by TNF-alpha-inducing activity in the macrophages. To clarify the mode of action of FimA fimbriae, anti-Toll-like receptor (TLR) 2 blocking antibody was added prior to stimulation. Weak stimulatory activity of native FimA fimbriae was enhanced by heat treatment and low-dose proteinase K treatment. Higher dose of proteinase K treatment abrogated this up-regulation. The activity of treated FimA fimbriae was suppressed by anti-TLR2 antibody, and more substantially by lipoprotein lipase treatment. These results suggest that lipoproteins or lipopeptides associated with FimA fimbriae could at least in part account for signaling via TLR2 and subsequent TNF-alpha production in macrophages.
Authors:
Yukari Aoki; Koichi Tabeta; Yukitaka Murakami; Fuminobu Yoshimura; Kazuhisa Yamazaki
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-06-15
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  398     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-19     Completed Date:  2010-08-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  86-91     Citation Subset:  IM    
Copyright Information:
Copyright 2010 Elsevier Inc. All rights reserved.
Affiliation:
Center for Transdisciplinary Research, Niigata University, Niigata, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Antibodies, Blocking / immunology
Cell Line
Endopeptidase K / metabolism
Fimbriae Proteins / immunology*
Fimbriae, Bacterial / immunology*
Hot Temperature
Humans
Interleukin-1 Receptor-Associated Kinases / metabolism
Lipopeptides / immunology
Macrophages / immunology*
Porphyromonas gingivalis / immunology*
Protein Denaturation
Toll-Like Receptor 2 / antagonists & inhibitors,  biosynthesis*
Tumor Necrosis Factor-alpha / biosynthesis
Chemical
Reg. No./Substance:
0/Antibodies, Blocking; 0/Lipopeptides; 0/Pam(3)CSK(4) peptide; 0/Toll-Like Receptor 2; 0/Tumor Necrosis Factor-alpha; 0/fimbrillin; 147680-16-8/Fimbriae Proteins; EC 2.7.11.1/IRAK3 protein, human; EC 2.7.11.1/Interleukin-1 Receptor-Associated Kinases; EC 3.4.21.64/Endopeptidase K

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


Previous Document:  Functional dominant-negative mutation of sodium channel subunit gene SCN3B associated with atrial fi...
Next Document:  The regulatory mechanism of Hsp90alpha secretion from endothelial cells and its role in angiogenesis...