Toll-Like Receptor 2-Mediated Interleukin-8 Expression in Gingival Epithelial Cells by the Tannerella forsythia Leucine-Rich Repeat Protein BspA
Tannerella forsythia is a gram-negative anaerobe strongly associated with chronic human periodontitis. This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich re...
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| Veröffentlicht in: | Infection and Immunity 2008-01, Vol.76 (1), p.198-205 |
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| creator | Onishi, Shinsuke Honma, Kiyonobu Liang, Shuang Stathopoulou, Panagiota Kinane, Denis Hajishengallis, George Sharma, Ashu |
| description | Tannerella forsythia is a gram-negative anaerobe strongly associated with chronic human periodontitis. This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich repeat (LRR) and bacterial immunoglobulin-like protein families. BspA is, moreover, a multifunctional protein which interacts with a variety of host cells, including monocytes which appear to respond to BspA through Toll-like receptor (TLR) signaling. Since gingival epithelium forms a barrier against periodontal pathogens, this study was undertaken to determine if gingival epithelial cells respond to BspA challenge and if TLRs play any role in BspA recognition. This study was also directed towards identifying the BspA domains responsible for cellular activation. We provide direct evidence for BspA binding to TLR2 and demonstrate that the release of the chemokine interleukin-8 from human gingival epithelial cells by BspA is TLR2 dependent. Furthermore, the LRR domain of BspA is involved in activation of TLR2, while TLR1 serves as a signaling partner. Thus, our findings suggest that BspA is an important modulator of host innate immune responses through activation of TLR2 in cooperation with TLR1. |
| doi_str_mv | 10.1128/IAI.01139-07 |
| format | Article |
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This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich repeat (LRR) and bacterial immunoglobulin-like protein families. BspA is, moreover, a multifunctional protein which interacts with a variety of host cells, including monocytes which appear to respond to BspA through Toll-like receptor (TLR) signaling. Since gingival epithelium forms a barrier against periodontal pathogens, this study was undertaken to determine if gingival epithelial cells respond to BspA challenge and if TLRs play any role in BspA recognition. This study was also directed towards identifying the BspA domains responsible for cellular activation. We provide direct evidence for BspA binding to TLR2 and demonstrate that the release of the chemokine interleukin-8 from human gingival epithelial cells by BspA is TLR2 dependent. Furthermore, the LRR domain of BspA is involved in activation of TLR2, while TLR1 serves as a signaling partner. Thus, our findings suggest that BspA is an important modulator of host innate immune responses through activation of TLR2 in cooperation with TLR1.</description><identifier>ISSN: 0019-9567</identifier><identifier>EISSN: 1098-5522</identifier><identifier>DOI: 10.1128/IAI.01139-07</identifier><identifier>PMID: 17967853</identifier><identifier>CODEN: INFIBR</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Bacterial Proteins - pharmacology ; Bacteriology ; Bacteroides forsythus ; Biological and medical sciences ; Cell Line ; Epithelial Cells - drug effects ; Epithelial Cells - metabolism ; Fundamental and applied biological sciences. 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This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich repeat (LRR) and bacterial immunoglobulin-like protein families. BspA is, moreover, a multifunctional protein which interacts with a variety of host cells, including monocytes which appear to respond to BspA through Toll-like receptor (TLR) signaling. Since gingival epithelium forms a barrier against periodontal pathogens, this study was undertaken to determine if gingival epithelial cells respond to BspA challenge and if TLRs play any role in BspA recognition. This study was also directed towards identifying the BspA domains responsible for cellular activation. We provide direct evidence for BspA binding to TLR2 and demonstrate that the release of the chemokine interleukin-8 from human gingival epithelial cells by BspA is TLR2 dependent. 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Psychology</topic><topic>Gingiva - cytology</topic><topic>Gram-Negative Anaerobic Bacteria - metabolism</topic><topic>Host Response and Inflammation</topic><topic>Humans</topic><topic>Interleukin-8 - genetics</topic><topic>Interleukin-8 - metabolism</topic><topic>Membrane Proteins - pharmacology</topic><topic>Microbiology</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Toll-Like Receptor 1 - metabolism</topic><topic>Toll-Like Receptor 2 - metabolism</topic><topic>Toll-Like Receptor 6 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Onishi, Shinsuke</creatorcontrib><creatorcontrib>Honma, Kiyonobu</creatorcontrib><creatorcontrib>Liang, Shuang</creatorcontrib><creatorcontrib>Stathopoulou, Panagiota</creatorcontrib><creatorcontrib>Kinane, Denis</creatorcontrib><creatorcontrib>Hajishengallis, George</creatorcontrib><creatorcontrib>Sharma, Ashu</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Infection and Immunity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Onishi, Shinsuke</au><au>Honma, Kiyonobu</au><au>Liang, Shuang</au><au>Stathopoulou, Panagiota</au><au>Kinane, Denis</au><au>Hajishengallis, George</au><au>Sharma, Ashu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Toll-Like Receptor 2-Mediated Interleukin-8 Expression in Gingival Epithelial Cells by the Tannerella forsythia Leucine-Rich Repeat Protein BspA</atitle><jtitle>Infection and Immunity</jtitle><addtitle>Infect Immun</addtitle><date>2008-01-01</date><risdate>2008</risdate><volume>76</volume><issue>1</issue><spage>198</spage><epage>205</epage><pages>198-205</pages><issn>0019-9567</issn><eissn>1098-5522</eissn><coden>INFIBR</coden><abstract>Tannerella forsythia is a gram-negative anaerobe strongly associated with chronic human periodontitis. This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich repeat (LRR) and bacterial immunoglobulin-like protein families. BspA is, moreover, a multifunctional protein which interacts with a variety of host cells, including monocytes which appear to respond to BspA through Toll-like receptor (TLR) signaling. Since gingival epithelium forms a barrier against periodontal pathogens, this study was undertaken to determine if gingival epithelial cells respond to BspA challenge and if TLRs play any role in BspA recognition. This study was also directed towards identifying the BspA domains responsible for cellular activation. We provide direct evidence for BspA binding to TLR2 and demonstrate that the release of the chemokine interleukin-8 from human gingival epithelial cells by BspA is TLR2 dependent. Furthermore, the LRR domain of BspA is involved in activation of TLR2, while TLR1 serves as a signaling partner. Thus, our findings suggest that BspA is an important modulator of host innate immune responses through activation of TLR2 in cooperation with TLR1.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>17967853</pmid><doi>10.1128/IAI.01139-07</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacterial Proteins - pharmacology Bacteriology Bacteroides forsythus Biological and medical sciences Cell Line Epithelial Cells - drug effects Epithelial Cells - metabolism Fundamental and applied biological sciences. Psychology Gingiva - cytology Gram-Negative Anaerobic Bacteria - metabolism Host Response and Inflammation Humans Interleukin-8 - genetics Interleukin-8 - metabolism Membrane Proteins - pharmacology Microbiology Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Protein Binding Protein Structure, Tertiary Toll-Like Receptor 1 - metabolism Toll-Like Receptor 2 - metabolism Toll-Like Receptor 6 - metabolism |
| title | Toll-Like Receptor 2-Mediated Interleukin-8 Expression in Gingival Epithelial Cells by the Tannerella forsythia Leucine-Rich Repeat Protein BspA |
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