The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity
It was suggested that minor differences in the structure of FimH are most likely associated with differences in its adhesion specificities and may determine the tropism of various Salmonella serovars to different species and tissues. We have recently shown that FimH adhesins from host-adapted serova...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2017-07-01
|
| Series: | Frontiers in Cellular and Infection Microbiology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/article/10.3389/fcimb.2017.00326/full |
| _version_ | 1818265709587726336 |
|---|---|
| author | Krzysztof Grzymajlo Maciej Ugorski Jaroslaw Suchanski Anna E. Kedzierska Rafal Kolenda Anna Jarzab Agnieszka Biernatowska Peter Schierack |
| author_facet | Krzysztof Grzymajlo Maciej Ugorski Jaroslaw Suchanski Anna E. Kedzierska Rafal Kolenda Anna Jarzab Agnieszka Biernatowska Peter Schierack |
| author_sort | Krzysztof Grzymajlo |
| collection | DOAJ |
| description | It was suggested that minor differences in the structure of FimH are most likely associated with differences in its adhesion specificities and may determine the tropism of various Salmonella serovars to different species and tissues. We have recently shown that FimH adhesins from host-adapted serovars, e.g., Salmonella Choleraesuis (SCh), bind to other glycoprotein receptors compared to FimH from host-unrestricted Salmonella Enteritidis (SE). Here we identify porcine calreticulin expressed by swine intestinal cells as a host-specific receptor for SCh FimH adhesin, suggesting that such an interaction may contribute to SCh host specificity. Calreticulin was identified by 2D electrophoresis and mass spectrometry as a glycoprotein that was bound specifically by recombinant SCh FimH protein, but not by FimH from SE. The functionality of calreticulin as a specific receptor of SCh FimH adhesin was further confirmed by adhesion and invasion of mutated strains of SCh carrying different variants of FimH proteins to IPEC-J2 cells with overexpression and silenced expression of calreticulin. It was found that SCh carrying the active variant of FimH adhered and invaded IPEC-J2 cells with calreticulin overexpression at significantly higher numbers than those of SCh expressing the non-active variant or SE variant of FimH. Moreover, binding of SCh carrying the active variant of FimH to IPEC-J2 with silenced calreticulin expression was significantly weaker. Furthermore, we observed that SCh infection induces translocation of calreticulin to cell membrane. All of the aforementioned results lead to the general conclusion that Salmonella host specificity requires not only special mechanisms and proteins expressed by the pathogen but also specifically recognized receptors expressed by a specific host. |
| first_indexed | 2024-12-12T19:55:07Z |
| format | Article |
| id | doaj.art-64be1a95d8764be0bda77c896d2a14d1 |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-12-12T19:55:07Z |
| publishDate | 2017-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-64be1a95d8764be0bda77c896d2a14d12022-12-22T00:13:54ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882017-07-01710.3389/fcimb.2017.00326278583The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host SpecificityKrzysztof Grzymajlo0Maciej Ugorski1Jaroslaw Suchanski2Anna E. Kedzierska3Rafal Kolenda4Anna Jarzab5Agnieszka Biernatowska6Peter Schierack7Department of Biochemistry and Molecular Biology, Faculty of Veterinary Sciences, Wrocław University of Environmental and Life SciencesWrocław, PolandDepartment of Biochemistry and Molecular Biology, Faculty of Veterinary Sciences, Wrocław University of Environmental and Life SciencesWrocław, PolandDepartment of Biochemistry and Molecular Biology, Faculty of Veterinary Sciences, Wrocław University of Environmental and Life SciencesWrocław, PolandLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesWrocław, PolandFaculty of Environment and Natural Sciences, Institute of Biotechnology, Brandenburg University of Technology Cottbus-SenftenbergSenftenberg, GermanyLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesWrocław, PolandLaboratory of Cytobiochemistry, Faculty of Biotechnology, University of WrocławWrocław, PolandFaculty of Environment and Natural Sciences, Institute of Biotechnology, Brandenburg University of Technology Cottbus-SenftenbergSenftenberg, GermanyIt was suggested that minor differences in the structure of FimH are most likely associated with differences in its adhesion specificities and may determine the tropism of various Salmonella serovars to different species and tissues. We have recently shown that FimH adhesins from host-adapted serovars, e.g., Salmonella Choleraesuis (SCh), bind to other glycoprotein receptors compared to FimH from host-unrestricted Salmonella Enteritidis (SE). Here we identify porcine calreticulin expressed by swine intestinal cells as a host-specific receptor for SCh FimH adhesin, suggesting that such an interaction may contribute to SCh host specificity. Calreticulin was identified by 2D electrophoresis and mass spectrometry as a glycoprotein that was bound specifically by recombinant SCh FimH protein, but not by FimH from SE. The functionality of calreticulin as a specific receptor of SCh FimH adhesin was further confirmed by adhesion and invasion of mutated strains of SCh carrying different variants of FimH proteins to IPEC-J2 cells with overexpression and silenced expression of calreticulin. It was found that SCh carrying the active variant of FimH adhered and invaded IPEC-J2 cells with calreticulin overexpression at significantly higher numbers than those of SCh expressing the non-active variant or SE variant of FimH. Moreover, binding of SCh carrying the active variant of FimH to IPEC-J2 with silenced calreticulin expression was significantly weaker. Furthermore, we observed that SCh infection induces translocation of calreticulin to cell membrane. All of the aforementioned results lead to the general conclusion that Salmonella host specificity requires not only special mechanisms and proteins expressed by the pathogen but also specifically recognized receptors expressed by a specific host.http://journal.frontiersin.org/article/10.3389/fcimb.2017.00326/fullSalmonellahost specificitytype 1 fimbriaeFimHadhesioncalreticulin |
| spellingShingle | Krzysztof Grzymajlo Maciej Ugorski Jaroslaw Suchanski Anna E. Kedzierska Rafal Kolenda Anna Jarzab Agnieszka Biernatowska Peter Schierack The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity Frontiers in Cellular and Infection Microbiology Salmonella host specificity type 1 fimbriae FimH adhesion calreticulin |
| title | The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity |
| title_full | The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity |
| title_fullStr | The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity |
| title_full_unstemmed | The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity |
| title_short | The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity |
| title_sort | novel type 1 fimbriae fimh receptor calreticulin plays a role in salmonella host specificity |
| topic | Salmonella host specificity type 1 fimbriae FimH adhesion calreticulin |
| url | http://journal.frontiersin.org/article/10.3389/fcimb.2017.00326/full |
| work_keys_str_mv | AT krzysztofgrzymajlo thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT maciejugorski thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT jaroslawsuchanski thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT annaekedzierska thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT rafalkolenda thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT annajarzab thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT agnieszkabiernatowska thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT peterschierack thenoveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT krzysztofgrzymajlo noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT maciejugorski noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT jaroslawsuchanski noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT annaekedzierska noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT rafalkolenda noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT annajarzab noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT agnieszkabiernatowska noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity AT peterschierack noveltype1fimbriaefimhreceptorcalreticulinplaysaroleinsalmonellahostspecificity |