The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin
<p>Abstract</p> <p>Background</p> <p>The <it>pagN </it>gene of <it>Salmonella enterica </it>serovar Typhimurium is a PhoP-regulated gene that is up-regulated during growth within macrophages and <it>in vivo </it>in murine models of in...
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| Format: | Article |
| Language: | English |
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BMC
2008-09-01
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| Series: | BMC Microbiology |
| Online Access: | http://www.biomedcentral.com/1471-2180/8/142 |
| _version_ | 1811275584218595328 |
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| author | Lambert Matthew A Smith Stephen GJ |
| author_facet | Lambert Matthew A Smith Stephen GJ |
| author_sort | Lambert Matthew A |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>The <it>pagN </it>gene of <it>Salmonella enterica </it>serovar Typhimurium is a PhoP-regulated gene that is up-regulated during growth within macrophages and <it>in vivo </it>in murine models of infection. The PagN protein displays similarity to the Hek and Tia invasins/adhesins of <it>Escherichia coli</it>. Thus far no function has been ascribed to the PagN protein.</p> <p>Results</p> <p>Here we show that the outer membrane located PagN protein mediates agglutination of red blood cells and that this can be masked by LPS. When expressed in <it>Escherichia coli </it>the PagN protein supports adhesion to and invasion of mammalian cells in a manner that is dependent on cytoskeletal rearrangements. <it>S. enterica </it>sv Typhimurium <it>pagN </it>mutants display a reduction in adhesion to and invasion of epithelial cells. Finally, we demonstrate that over-expression of PagN in a SPI-1 mutant can partially compensate for the lack of a functional invasasome.</p> <p>Conclusion</p> <p>PagN is an outer membrane protein that may contribute to the virulence of <it>S</it>. Typhimurium. This protein is a haemagglutinin and contributes to the adherence to mammalian cells. In addition, PagN can mediate high-level invasion of CHO-K1 cells. Previously,<it>pagN </it>mutants have been shown to be less competitive <it>in vivo </it>and thus this may be due to their lessened ability to interact with mammalian cells. Finally PagN can be added to an ever-growing repertoire of factors that contribute to the pathogenesis of <it>Salmonella</it>.</p> |
| first_indexed | 2024-04-12T23:41:34Z |
| format | Article |
| id | doaj.art-610655ff231c44efb7a8af745bc62f4f |
| institution | Directory Open Access Journal |
| issn | 1471-2180 |
| language | English |
| last_indexed | 2024-04-12T23:41:34Z |
| publishDate | 2008-09-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Microbiology |
| spelling | doaj.art-610655ff231c44efb7a8af745bc62f4f2022-12-22T03:11:59ZengBMCBMC Microbiology1471-21802008-09-018114210.1186/1471-2180-8-142The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasinLambert Matthew ASmith Stephen GJ<p>Abstract</p> <p>Background</p> <p>The <it>pagN </it>gene of <it>Salmonella enterica </it>serovar Typhimurium is a PhoP-regulated gene that is up-regulated during growth within macrophages and <it>in vivo </it>in murine models of infection. The PagN protein displays similarity to the Hek and Tia invasins/adhesins of <it>Escherichia coli</it>. Thus far no function has been ascribed to the PagN protein.</p> <p>Results</p> <p>Here we show that the outer membrane located PagN protein mediates agglutination of red blood cells and that this can be masked by LPS. When expressed in <it>Escherichia coli </it>the PagN protein supports adhesion to and invasion of mammalian cells in a manner that is dependent on cytoskeletal rearrangements. <it>S. enterica </it>sv Typhimurium <it>pagN </it>mutants display a reduction in adhesion to and invasion of epithelial cells. Finally, we demonstrate that over-expression of PagN in a SPI-1 mutant can partially compensate for the lack of a functional invasasome.</p> <p>Conclusion</p> <p>PagN is an outer membrane protein that may contribute to the virulence of <it>S</it>. Typhimurium. This protein is a haemagglutinin and contributes to the adherence to mammalian cells. In addition, PagN can mediate high-level invasion of CHO-K1 cells. Previously,<it>pagN </it>mutants have been shown to be less competitive <it>in vivo </it>and thus this may be due to their lessened ability to interact with mammalian cells. Finally PagN can be added to an ever-growing repertoire of factors that contribute to the pathogenesis of <it>Salmonella</it>.</p>http://www.biomedcentral.com/1471-2180/8/142 |
| spellingShingle | Lambert Matthew A Smith Stephen GJ The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin BMC Microbiology |
| title | The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin |
| title_full | The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin |
| title_fullStr | The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin |
| title_full_unstemmed | The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin |
| title_short | The PagN protein of <it>Salmonella enterica </it>serovar Typhimurium is an adhesin and invasin |
| title_sort | pagn protein of it salmonella enterica it serovar typhimurium is an adhesin and invasin |
| url | http://www.biomedcentral.com/1471-2180/8/142 |
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