Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system
Pathogenicity Islands play a major role in the pathogenesis of infections by Salmonella enterica. The molecular function of Salmonella Pathogenicity Island 4 (SPI4) is largely unknown, but recent work indicated a role of SPI4 for Salmonella pathogenesis in certain animal models. We analysed the viru...
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| Veröffentlicht in: | Cellular microbiology 2007-07, Vol.9 (7), p.1834-1850 |
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| creator | Gerlach, Roman G Jäckel, Daniela Stecher, Bärbel Wagner, Carolin Lupas, Andrei Hardt, Wolf-Dietrich Hensel, Michael |
| description | Pathogenicity Islands play a major role in the pathogenesis of infections by Salmonella enterica. The molecular function of Salmonella Pathogenicity Island 4 (SPI4) is largely unknown, but recent work indicated a role of SPI4 for Salmonella pathogenesis in certain animal models. We analysed the virulence functions of SPI4 and observed that SPI4 is contributing to intestinal inflammation in a mouse model. On a cellular level, SPI4 mediates adhesion to epithelial cells. We demonstrate the function of SPI4-encoded proteins as a type I secretion system (T1SS) and identify SiiE as the substrate protein of the T1SS. SiiE is secreted into the culture medium but mediates contact-dependent adhesion to epithelial cell surfaces. SiiE is a very large non-fimbrial adhesin of 600 kDa and consists of 53 repeats of Ig domains. Our study describes the first T1SS-secreted protein that functions as a non-fimbrial adhesin in binding to eukaryotic cells. The SPI4-encoded T1SS and SiiE might functionally resemble the type I fimbrial adhesins. |
| doi_str_mv | 10.1111/j.1462-5822.2007.00919.x |
| format | Article |
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The molecular function of Salmonella Pathogenicity Island 4 (SPI4) is largely unknown, but recent work indicated a role of SPI4 for Salmonella pathogenesis in certain animal models. We analysed the virulence functions of SPI4 and observed that SPI4 is contributing to intestinal inflammation in a mouse model. On a cellular level, SPI4 mediates adhesion to epithelial cells. We demonstrate the function of SPI4-encoded proteins as a type I secretion system (T1SS) and identify SiiE as the substrate protein of the T1SS. SiiE is secreted into the culture medium but mediates contact-dependent adhesion to epithelial cell surfaces. SiiE is a very large non-fimbrial adhesin of 600 kDa and consists of 53 repeats of Ig domains. Our study describes the first T1SS-secreted protein that functions as a non-fimbrial adhesin in binding to eukaryotic cells. 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The molecular function of Salmonella Pathogenicity Island 4 (SPI4) is largely unknown, but recent work indicated a role of SPI4 for Salmonella pathogenesis in certain animal models. We analysed the virulence functions of SPI4 and observed that SPI4 is contributing to intestinal inflammation in a mouse model. On a cellular level, SPI4 mediates adhesion to epithelial cells. We demonstrate the function of SPI4-encoded proteins as a type I secretion system (T1SS) and identify SiiE as the substrate protein of the T1SS. SiiE is secreted into the culture medium but mediates contact-dependent adhesion to epithelial cell surfaces. SiiE is a very large non-fimbrial adhesin of 600 kDa and consists of 53 repeats of Ig domains. Our study describes the first T1SS-secreted protein that functions as a non-fimbrial adhesin in binding to eukaryotic cells. 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Jäckel, Daniela ; Stecher, Bärbel ; Wagner, Carolin ; Lupas, Andrei ; Hardt, Wolf-Dietrich ; Hensel, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5149-e951cc25783af68041a9734f989b25f1c4ca7619f5b8a5c4c4f9e0bbf9066f143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adhesins, Bacterial - genetics</topic><topic>Adhesins, Bacterial - metabolism</topic><topic>Animals</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacterial Proteins - secretion</topic><topic>Caco-2 Cells</topic><topic>Cell Line</topic><topic>Colitis - microbiology</topic><topic>Genomic Islands</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Intestinal Mucosa - microbiology</topic><topic>Macrophages</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Rabbits</topic><topic>Salmonella enterica</topic><topic>Salmonella Infections, Animal - microbiology</topic><topic>Salmonella typhimurium - genetics</topic><topic>Salmonella typhimurium - metabolism</topic><topic>Salmonella typhimurium - pathogenicity</topic><topic>Virulence Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gerlach, Roman G</creatorcontrib><creatorcontrib>Jäckel, Daniela</creatorcontrib><creatorcontrib>Stecher, Bärbel</creatorcontrib><creatorcontrib>Wagner, Carolin</creatorcontrib><creatorcontrib>Lupas, Andrei</creatorcontrib><creatorcontrib>Hardt, Wolf-Dietrich</creatorcontrib><creatorcontrib>Hensel, Michael</creatorcontrib><collection>AGRIS</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cellular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gerlach, Roman G</au><au>Jäckel, Daniela</au><au>Stecher, Bärbel</au><au>Wagner, Carolin</au><au>Lupas, Andrei</au><au>Hardt, Wolf-Dietrich</au><au>Hensel, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system</atitle><jtitle>Cellular microbiology</jtitle><addtitle>Cell Microbiol</addtitle><date>2007-07</date><risdate>2007</risdate><volume>9</volume><issue>7</issue><spage>1834</spage><epage>1850</epage><pages>1834-1850</pages><issn>1462-5814</issn><eissn>1462-5822</eissn><abstract>Pathogenicity Islands play a major role in the pathogenesis of infections by Salmonella enterica. The molecular function of Salmonella Pathogenicity Island 4 (SPI4) is largely unknown, but recent work indicated a role of SPI4 for Salmonella pathogenesis in certain animal models. We analysed the virulence functions of SPI4 and observed that SPI4 is contributing to intestinal inflammation in a mouse model. On a cellular level, SPI4 mediates adhesion to epithelial cells. We demonstrate the function of SPI4-encoded proteins as a type I secretion system (T1SS) and identify SiiE as the substrate protein of the T1SS. SiiE is secreted into the culture medium but mediates contact-dependent adhesion to epithelial cell surfaces. SiiE is a very large non-fimbrial adhesin of 600 kDa and consists of 53 repeats of Ig domains. Our study describes the first T1SS-secreted protein that functions as a non-fimbrial adhesin in binding to eukaryotic cells. 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| subjects | Adhesins, Bacterial - genetics Adhesins, Bacterial - metabolism Animals Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacterial Proteins - secretion Caco-2 Cells Cell Line Colitis - microbiology Genomic Islands HeLa Cells Humans Intestinal Mucosa - microbiology Macrophages Membrane Proteins - genetics Membrane Proteins - metabolism Mice Mice, Inbred C57BL Rabbits Salmonella enterica Salmonella Infections, Animal - microbiology Salmonella typhimurium - genetics Salmonella typhimurium - metabolism Salmonella typhimurium - pathogenicity Virulence Factors |
| title | Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system |
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