Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system.
BACKGROUND: Type III secretion systems (TTSS) are employed by numerous pathogenic and symbiotic bacteria to inject a cocktail of different "effector proteins" into host cells. These effectors subvert host cell signaling to establish symbiosis or disease. METHODOLOGY/PRINCIPAL FINDINGS: We...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2008-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2364654?pdf=render |
| _version_ | 1818700551998668800 |
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| author | Brit Winnen Markus C Schlumberger Alexander Sturm Kaspar Schüpbach Stefan Siebenmann Patrick Jenny Wolf-Dietrich Hardt |
| author_facet | Brit Winnen Markus C Schlumberger Alexander Sturm Kaspar Schüpbach Stefan Siebenmann Patrick Jenny Wolf-Dietrich Hardt |
| author_sort | Brit Winnen |
| collection | DOAJ |
| description | BACKGROUND: Type III secretion systems (TTSS) are employed by numerous pathogenic and symbiotic bacteria to inject a cocktail of different "effector proteins" into host cells. These effectors subvert host cell signaling to establish symbiosis or disease. METHODOLOGY/PRINCIPAL FINDINGS: We have studied the injection of SipA and SptP, two effector proteins of the invasion-associated Salmonella type III secretion system (TTSS-1). SipA and SptP trigger different host cell responses. SipA contributes to triggering actin rearrangements and invasion while SptP reverses the actin rearrangements after the invasion has been completed. Nevertheless, SipA and SptP were both pre-formed and stored in the bacterial cytosol before host cell encounter. By time lapse microscopy, we observed that SipA was injected earlier than SptP. Computer modeling revealed that two assumptions were sufficient to explain this injection hierarchy: a large number of SipA and SptP molecules compete for transport via a limiting number of TTSS; and the TTSS recognize SipA more efficiently than SptP. CONCLUSIONS/SIGNIFICANCE: This novel mechanism of hierarchical effector protein injection may serve to avoid functional interference between SipA and SptP. An injection hierarchy of this type may be of general importance, allowing bacteria to precisely time the host cell manipulation by type III effectors. |
| first_indexed | 2024-12-17T15:06:45Z |
| format | Article |
| id | doaj.art-3ec97c46628f4e648cd1637db6ca951a |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T15:06:45Z |
| publishDate | 2008-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-3ec97c46628f4e648cd1637db6ca951a2022-12-21T21:43:46ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-01-0135e217810.1371/journal.pone.0002178Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system.Brit WinnenMarkus C SchlumbergerAlexander SturmKaspar SchüpbachStefan SiebenmannPatrick JennyWolf-Dietrich HardtBACKGROUND: Type III secretion systems (TTSS) are employed by numerous pathogenic and symbiotic bacteria to inject a cocktail of different "effector proteins" into host cells. These effectors subvert host cell signaling to establish symbiosis or disease. METHODOLOGY/PRINCIPAL FINDINGS: We have studied the injection of SipA and SptP, two effector proteins of the invasion-associated Salmonella type III secretion system (TTSS-1). SipA and SptP trigger different host cell responses. SipA contributes to triggering actin rearrangements and invasion while SptP reverses the actin rearrangements after the invasion has been completed. Nevertheless, SipA and SptP were both pre-formed and stored in the bacterial cytosol before host cell encounter. By time lapse microscopy, we observed that SipA was injected earlier than SptP. Computer modeling revealed that two assumptions were sufficient to explain this injection hierarchy: a large number of SipA and SptP molecules compete for transport via a limiting number of TTSS; and the TTSS recognize SipA more efficiently than SptP. CONCLUSIONS/SIGNIFICANCE: This novel mechanism of hierarchical effector protein injection may serve to avoid functional interference between SipA and SptP. An injection hierarchy of this type may be of general importance, allowing bacteria to precisely time the host cell manipulation by type III effectors.http://europepmc.org/articles/PMC2364654?pdf=render |
| spellingShingle | Brit Winnen Markus C Schlumberger Alexander Sturm Kaspar Schüpbach Stefan Siebenmann Patrick Jenny Wolf-Dietrich Hardt Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. PLoS ONE |
| title | Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. |
| title_full | Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. |
| title_fullStr | Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. |
| title_full_unstemmed | Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. |
| title_short | Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. |
| title_sort | hierarchical effector protein transport by the salmonella typhimurium spi 1 type iii secretion system |
| url | http://europepmc.org/articles/PMC2364654?pdf=render |
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