Helical packing of needles from functionally altered Shigella type III secretion systems.
Gram-negative bacteria commonly interact with eukaryotic host cells using type III secretion systems (TTSSs or secretons), which comprise cytoplasmic, transmembrane and extracellular domains. The extracellular domain is a hollow needle-like structure protruding 60 nm beyond the bacterial surface. Th...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2005
|
| _version_ | 1797099345615519744 |
|---|---|
| author | Cordes, F Daniell, S Kenjale, R Saurya, S Picking, W Picking, W Booy, F Lea, S Blocker, A |
| author_facet | Cordes, F Daniell, S Kenjale, R Saurya, S Picking, W Picking, W Booy, F Lea, S Blocker, A |
| author_sort | Cordes, F |
| collection | OXFORD |
| description | Gram-negative bacteria commonly interact with eukaryotic host cells using type III secretion systems (TTSSs or secretons), which comprise cytoplasmic, transmembrane and extracellular domains. The extracellular domain is a hollow needle-like structure protruding 60 nm beyond the bacterial surface. The TTSS is activated to transfer bacterial proteins directly into a host cell only upon physical contact with the target cell. We showed previously that the monomer of the Shigella flexneri needle, MxiH, assembles into a helical structure with parameters similar to those defining the architecture of the extracellular components of bacterial flagella. By analogy with flagella, which are known to exist in different helical states, we proposed that changes in the helical packing of the needle might be used to sense host cell contact. Here, we show that, on the contrary, mutations within MxiH that lock the TTSS into altered secretion states do not detectably alter the helical packing of needles. This implies that either: (1) host cell contact is signalled through the TTSS via helical changes in the needle that are significantly smaller than those linked to structural changes in the flagellar filament and therefore too small to be detected by our analysis methods or (2) that signal transduction in this system occurs via a novel molecular mechanism. |
| first_indexed | 2024-03-07T05:22:30Z |
| format | Journal article |
| id | oxford-uuid:df66f8bd-9222-43cd-ba66-ff8cc9264e94 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:22:30Z |
| publishDate | 2005 |
| record_format | dspace |
| spelling | oxford-uuid:df66f8bd-9222-43cd-ba66-ff8cc9264e942022-03-27T09:39:10ZHelical packing of needles from functionally altered Shigella type III secretion systems.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:df66f8bd-9222-43cd-ba66-ff8cc9264e94EnglishSymplectic Elements at Oxford2005Cordes, FDaniell, SKenjale, RSaurya, SPicking, WPicking, WBooy, FLea, SBlocker, AGram-negative bacteria commonly interact with eukaryotic host cells using type III secretion systems (TTSSs or secretons), which comprise cytoplasmic, transmembrane and extracellular domains. The extracellular domain is a hollow needle-like structure protruding 60 nm beyond the bacterial surface. The TTSS is activated to transfer bacterial proteins directly into a host cell only upon physical contact with the target cell. We showed previously that the monomer of the Shigella flexneri needle, MxiH, assembles into a helical structure with parameters similar to those defining the architecture of the extracellular components of bacterial flagella. By analogy with flagella, which are known to exist in different helical states, we proposed that changes in the helical packing of the needle might be used to sense host cell contact. Here, we show that, on the contrary, mutations within MxiH that lock the TTSS into altered secretion states do not detectably alter the helical packing of needles. This implies that either: (1) host cell contact is signalled through the TTSS via helical changes in the needle that are significantly smaller than those linked to structural changes in the flagellar filament and therefore too small to be detected by our analysis methods or (2) that signal transduction in this system occurs via a novel molecular mechanism. |
| spellingShingle | Cordes, F Daniell, S Kenjale, R Saurya, S Picking, W Picking, W Booy, F Lea, S Blocker, A Helical packing of needles from functionally altered Shigella type III secretion systems. |
| title | Helical packing of needles from functionally altered Shigella type III secretion systems. |
| title_full | Helical packing of needles from functionally altered Shigella type III secretion systems. |
| title_fullStr | Helical packing of needles from functionally altered Shigella type III secretion systems. |
| title_full_unstemmed | Helical packing of needles from functionally altered Shigella type III secretion systems. |
| title_short | Helical packing of needles from functionally altered Shigella type III secretion systems. |
| title_sort | helical packing of needles from functionally altered shigella type iii secretion systems |
| work_keys_str_mv | AT cordesf helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT daniells helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT kenjaler helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT sauryas helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT pickingw helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT pickingw helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT booyf helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT leas helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems AT blockera helicalpackingofneedlesfromfunctionallyalteredshigellatypeiiisecretionsystems |