Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus.
Bacterial type III protein secretion systems inject effector proteins into eukaryotic host cells in order to promote survival and colonization of Gram-negative pathogens and symbionts. Secretion across the bacterial cell envelope and injection into host cells is facilitated by a so-called injectisom...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-12-01
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| Series: | PLoS Pathogens |
| Online Access: | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006071&type=printable |
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| author | Tobias Dietsche Mehari Tesfazgi Mebrhatu Matthias J Brunner Patrizia Abrusci Jun Yan Mirita Franz-Wachtel Charlotta Schärfe Susann Zilkenat Iwan Grin Jorge E Galán Oliver Kohlbacher Susan Lea Boris Macek Thomas C Marlovits Carol V Robinson Samuel Wagner |
| author_facet | Tobias Dietsche Mehari Tesfazgi Mebrhatu Matthias J Brunner Patrizia Abrusci Jun Yan Mirita Franz-Wachtel Charlotta Schärfe Susann Zilkenat Iwan Grin Jorge E Galán Oliver Kohlbacher Susan Lea Boris Macek Thomas C Marlovits Carol V Robinson Samuel Wagner |
| author_sort | Tobias Dietsche |
| collection | DOAJ |
| description | Bacterial type III protein secretion systems inject effector proteins into eukaryotic host cells in order to promote survival and colonization of Gram-negative pathogens and symbionts. Secretion across the bacterial cell envelope and injection into host cells is facilitated by a so-called injectisome. Its small hydrophobic export apparatus components SpaP and SpaR were shown to nucleate assembly of the needle complex and to form the central "cup" substructure of a Salmonella Typhimurium secretion system. However, the in vivo placement of these components in the needle complex and their function during the secretion process remained poorly defined. Here we present evidence that a SpaP pentamer forms a 15 Å wide pore and provide a detailed map of SpaP interactions with the export apparatus components SpaQ, SpaR, and SpaS. We further refine the current view of export apparatus assembly, consolidate transmembrane topology models for SpaP and SpaR, and present intimate interactions of the periplasmic domains of SpaP and SpaR with the inner rod protein PrgJ, indicating how export apparatus and needle filament are connected to create a continuous conduit for substrate translocation. |
| format | Article |
| id | doaj-art-47f61fc5df8947a58c7922337e021a69 |
| institution | OA Journals |
| issn | 1553-7366 1553-7374 |
| language | English |
| publishDate | 2016-12-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj-art-47f61fc5df8947a58c7922337e021a692025-08-20T02:31:59ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742016-12-011212e100607110.1371/journal.ppat.1006071Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus.Tobias DietscheMehari Tesfazgi MebrhatuMatthias J BrunnerPatrizia AbrusciJun YanMirita Franz-WachtelCharlotta SchärfeSusann ZilkenatIwan GrinJorge E GalánOliver KohlbacherSusan LeaBoris MacekThomas C MarlovitsCarol V RobinsonSamuel WagnerBacterial type III protein secretion systems inject effector proteins into eukaryotic host cells in order to promote survival and colonization of Gram-negative pathogens and symbionts. Secretion across the bacterial cell envelope and injection into host cells is facilitated by a so-called injectisome. Its small hydrophobic export apparatus components SpaP and SpaR were shown to nucleate assembly of the needle complex and to form the central "cup" substructure of a Salmonella Typhimurium secretion system. However, the in vivo placement of these components in the needle complex and their function during the secretion process remained poorly defined. Here we present evidence that a SpaP pentamer forms a 15 Å wide pore and provide a detailed map of SpaP interactions with the export apparatus components SpaQ, SpaR, and SpaS. We further refine the current view of export apparatus assembly, consolidate transmembrane topology models for SpaP and SpaR, and present intimate interactions of the periplasmic domains of SpaP and SpaR with the inner rod protein PrgJ, indicating how export apparatus and needle filament are connected to create a continuous conduit for substrate translocation.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006071&type=printable |
| spellingShingle | Tobias Dietsche Mehari Tesfazgi Mebrhatu Matthias J Brunner Patrizia Abrusci Jun Yan Mirita Franz-Wachtel Charlotta Schärfe Susann Zilkenat Iwan Grin Jorge E Galán Oliver Kohlbacher Susan Lea Boris Macek Thomas C Marlovits Carol V Robinson Samuel Wagner Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. PLoS Pathogens |
| title | Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. |
| title_full | Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. |
| title_fullStr | Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. |
| title_full_unstemmed | Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. |
| title_short | Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. |
| title_sort | structural and functional characterization of the bacterial type iii secretion export apparatus |
| url | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006071&type=printable |
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