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The PagN protein of Salmonella enterica serovar Typhimurium is an adhesin and invasin.

Lambert MA, Smith SG - BMC Microbiol. (2008)

Bottom Line: S. enterica sv Typhimurium pagN mutants display a reduction in adhesion to and invasion of epithelial cells.Typhimurium.Finally PagN can be added to an ever-growing repertoire of factors that contribute to the pathogenesis of Salmonella.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Clinical Microbiology, Trinity College Dublin, St James's Hospital, Dublin 8, Ireland. malamber79@gmail.com

ABSTRACT

Background: The pagN gene of Salmonella enterica serovar Typhimurium is a PhoP-regulated gene that is up-regulated during growth within macrophages and in vivo in murine models of infection. The PagN protein displays similarity to the Hek and Tia invasins/adhesins of Escherichia coli. Thus far no function has been ascribed to the PagN protein.

Results: 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 Escherichia coli the PagN protein supports adhesion to and invasion of mammalian cells in a manner that is dependent on cytoskeletal rearrangements. S. enterica sv Typhimurium pagN 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.

Conclusion: PagN is an outer membrane protein that may contribute to the virulence of S. 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,pagN mutants have been shown to be less competitive in vivo 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 Salmonella.

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Adhesion of HT-29 cells by S. TyphimuriumSL1344 and a pagN mutant. Cell association levels werecalculated for wild-type S. Typhimurium strain SL1344 andthe pagN mutant, strain ML6. Levels were also calculated for the pagN mutant harbouring the plasmid pML10 (PagN+). Data presented are averages of triplicate wells. ** indicates statistical significance, P < 0.01.
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Figure 6: Adhesion of HT-29 cells by S. TyphimuriumSL1344 and a pagN mutant. Cell association levels werecalculated for wild-type S. Typhimurium strain SL1344 andthe pagN mutant, strain ML6. Levels were also calculated for the pagN mutant harbouring the plasmid pML10 (PagN+). Data presented are averages of triplicate wells. ** indicates statistical significance, P < 0.01.

Mentions: Adhesion to the HT-29 cell line by S. Typhimurium strain SL1344 and adhesion-defects due to the absence of the PagN protein in strain ML6 were investigated. Standard cell association assays were performed comparing the levels of cell association displayed by wild-type and PagN-defective S. Typhimurium (Fig. 6). Wild-type bacteria were recovered in higher numbers compared to PagN-defective bacteria (0.98 ± 0.093% as compared to 0.48 ± 0.01%). Complementation of the pagN mutation with the pagN-containing multi-copy plasmid pML10 increased cell association to 10-fold greater than that exhibited by wild-type S. Typhimurium.


The PagN protein of Salmonella enterica serovar Typhimurium is an adhesin and invasin.

Lambert MA, Smith SG - BMC Microbiol. (2008)

Adhesion of HT-29 cells by S. TyphimuriumSL1344 and a pagN mutant. Cell association levels werecalculated for wild-type S. Typhimurium strain SL1344 andthe pagN mutant, strain ML6. Levels were also calculated for the pagN mutant harbouring the plasmid pML10 (PagN+). Data presented are averages of triplicate wells. ** indicates statistical significance, P < 0.01.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2553418&req=5

Figure 6: Adhesion of HT-29 cells by S. TyphimuriumSL1344 and a pagN mutant. Cell association levels werecalculated for wild-type S. Typhimurium strain SL1344 andthe pagN mutant, strain ML6. Levels were also calculated for the pagN mutant harbouring the plasmid pML10 (PagN+). Data presented are averages of triplicate wells. ** indicates statistical significance, P < 0.01.
Mentions: Adhesion to the HT-29 cell line by S. Typhimurium strain SL1344 and adhesion-defects due to the absence of the PagN protein in strain ML6 were investigated. Standard cell association assays were performed comparing the levels of cell association displayed by wild-type and PagN-defective S. Typhimurium (Fig. 6). Wild-type bacteria were recovered in higher numbers compared to PagN-defective bacteria (0.98 ± 0.093% as compared to 0.48 ± 0.01%). Complementation of the pagN mutation with the pagN-containing multi-copy plasmid pML10 increased cell association to 10-fold greater than that exhibited by wild-type S. Typhimurium.

Bottom Line: S. enterica sv Typhimurium pagN mutants display a reduction in adhesion to and invasion of epithelial cells.Typhimurium.Finally PagN can be added to an ever-growing repertoire of factors that contribute to the pathogenesis of Salmonella.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Clinical Microbiology, Trinity College Dublin, St James's Hospital, Dublin 8, Ireland. malamber79@gmail.com

ABSTRACT

Background: The pagN gene of Salmonella enterica serovar Typhimurium is a PhoP-regulated gene that is up-regulated during growth within macrophages and in vivo in murine models of infection. The PagN protein displays similarity to the Hek and Tia invasins/adhesins of Escherichia coli. Thus far no function has been ascribed to the PagN protein.

Results: 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 Escherichia coli the PagN protein supports adhesion to and invasion of mammalian cells in a manner that is dependent on cytoskeletal rearrangements. S. enterica sv Typhimurium pagN 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.

Conclusion: PagN is an outer membrane protein that may contribute to the virulence of S. 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,pagN mutants have been shown to be less competitive in vivo 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 Salmonella.

Show MeSH
Related in: MedlinePlus