A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.

The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "need...

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Autores principales:	Julien R C Bergeron, Liam J Worrall, Nikolaos G Sgourakis, Frank DiMaio, Richard A Pfuetzner, Heather B Felise, Marija Vuckovic, Angel C Yu, Samuel I Miller, David Baker, Natalie C J Strynadka
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/4db4112da9e849c689b527d13a3699fa
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spelling	oai:doaj.org-article:4db4112da9e849c689b527d13a3699fa2021-11-18T06:05:43ZA refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.1553-73661553-737410.1371/journal.ppat.1003307https://doaj.org/article/4db4112da9e849c689b527d13a3699fa2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23633951/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "needle" that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism.Julien R C BergeronLiam J WorrallNikolaos G SgourakisFrank DiMaioRichard A PfuetznerHeather B FeliseMarija VuckovicAngel C YuSamuel I MillerDavid BakerNatalie C J StrynadkaPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 4, p e1003307 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Julien R C Bergeron Liam J Worrall Nikolaos G Sgourakis Frank DiMaio Richard A Pfuetzner Heather B Felise Marija Vuckovic Angel C Yu Samuel I Miller David Baker Natalie C J Strynadka A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
description	The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "needle" that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism.
format	article
author	Julien R C Bergeron Liam J Worrall Nikolaos G Sgourakis Frank DiMaio Richard A Pfuetzner Heather B Felise Marija Vuckovic Angel C Yu Samuel I Miller David Baker Natalie C J Strynadka
author_facet	Julien R C Bergeron Liam J Worrall Nikolaos G Sgourakis Frank DiMaio Richard A Pfuetzner Heather B Felise Marija Vuckovic Angel C Yu Samuel I Miller David Baker Natalie C J Strynadka
author_sort	Julien R C Bergeron
title	A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
title_short	A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
title_full	A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
title_fullStr	A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
title_full_unstemmed	A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
title_sort	refined model of the prototypical salmonella spi-1 t3ss basal body reveals the molecular basis for its assembly.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/4db4112da9e849c689b527d13a3699fa
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A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.

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