The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems
ABSTRACT Export of proteins through type III secretion systems (T3SS) is critical for motility and virulence of many major bacterial pathogens. Proteins are exported through a genetically defined export gate complex consisting of three proteins. We have recently shown at 4.2 Å that the flagellar com...
Guardado en:
Autores principales: | , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
American Society for Microbiology
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/440945dcd4ea43eaa5c20d25e64a9515 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:440945dcd4ea43eaa5c20d25e64a9515 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:440945dcd4ea43eaa5c20d25e64a95152021-11-15T15:55:23ZThe Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems10.1128/mBio.00818-192150-7511https://doaj.org/article/440945dcd4ea43eaa5c20d25e64a95152019-06-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00818-19https://doaj.org/toc/2150-7511ABSTRACT Export of proteins through type III secretion systems (T3SS) is critical for motility and virulence of many major bacterial pathogens. Proteins are exported through a genetically defined export gate complex consisting of three proteins. We have recently shown at 4.2 Å that the flagellar complex of these three putative membrane proteins (FliPQR in flagellar systems, SctRST in virulence systems) assembles into an extramembrane helical assembly that likely seeds correct assembly of the rod. Here we present the structure of an equivalent complex from the Shigella virulence system at 3.5 Å by cryo-electron microscopy. This higher-resolution structure yields a more precise description of the structure and confirms the prediction of structural conservation in this core complex. Analysis of particle heterogeneity also suggests how the SctS/FliQ subunits sequentially assemble in the complex. IMPORTANCE Although predicted on the basis of sequence conservation, the work presented here formally demonstrates that all classes of type III secretion systems, flagellar or virulence, share the same architecture at the level of the core structures. This absolute conservation of the unusual extramembrane structure of the core export gate complex now allows work to move to focusing on both mechanistic studies of type III but also on fundamental studies of how such a complex is assembled.Steven JohnsonLucas KuhlenJustin C. DemePatrizia AbrusciSusan M. LeaAmerican Society for MicrobiologyarticleT3SScryo-EMprotein secretionvirulence determinantsMicrobiologyQR1-502ENmBio, Vol 10, Iss 3 (2019) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
T3SS cryo-EM protein secretion virulence determinants Microbiology QR1-502 |
spellingShingle |
T3SS cryo-EM protein secretion virulence determinants Microbiology QR1-502 Steven Johnson Lucas Kuhlen Justin C. Deme Patrizia Abrusci Susan M. Lea The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems |
description |
ABSTRACT Export of proteins through type III secretion systems (T3SS) is critical for motility and virulence of many major bacterial pathogens. Proteins are exported through a genetically defined export gate complex consisting of three proteins. We have recently shown at 4.2 Å that the flagellar complex of these three putative membrane proteins (FliPQR in flagellar systems, SctRST in virulence systems) assembles into an extramembrane helical assembly that likely seeds correct assembly of the rod. Here we present the structure of an equivalent complex from the Shigella virulence system at 3.5 Å by cryo-electron microscopy. This higher-resolution structure yields a more precise description of the structure and confirms the prediction of structural conservation in this core complex. Analysis of particle heterogeneity also suggests how the SctS/FliQ subunits sequentially assemble in the complex. IMPORTANCE Although predicted on the basis of sequence conservation, the work presented here formally demonstrates that all classes of type III secretion systems, flagellar or virulence, share the same architecture at the level of the core structures. This absolute conservation of the unusual extramembrane structure of the core export gate complex now allows work to move to focusing on both mechanistic studies of type III but also on fundamental studies of how such a complex is assembled. |
format |
article |
author |
Steven Johnson Lucas Kuhlen Justin C. Deme Patrizia Abrusci Susan M. Lea |
author_facet |
Steven Johnson Lucas Kuhlen Justin C. Deme Patrizia Abrusci Susan M. Lea |
author_sort |
Steven Johnson |
title |
The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems |
title_short |
The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems |
title_full |
The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems |
title_fullStr |
The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems |
title_full_unstemmed |
The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems |
title_sort |
structure of an injectisome export gate demonstrates conservation of architecture in the core export gate between flagellar and virulence type iii secretion systems |
publisher |
American Society for Microbiology |
publishDate |
2019 |
url |
https://doaj.org/article/440945dcd4ea43eaa5c20d25e64a9515 |
work_keys_str_mv |
AT stevenjohnson thestructureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT lucaskuhlen thestructureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT justincdeme thestructureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT patriziaabrusci thestructureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT susanmlea thestructureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT stevenjohnson structureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT lucaskuhlen structureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT justincdeme structureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT patriziaabrusci structureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems AT susanmlea structureofaninjectisomeexportgatedemonstratesconservationofarchitectureinthecoreexportgatebetweenflagellarandvirulencetypeiiisecretionsystems |
_version_ |
1718427210401972224 |