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| Open AccessA dynamic and adaptive network of cytosolic interactions governs protein export by the T3SS injectisome
Bacterial type III secretion systems (T3SS) play important roles in pathogenesis. Here, Diepoldet al. show the dynamic nature of complexes formed of essential T3SS components in live bacteria, and that extracellular calcium concentrations influence these cytosolic complexes likely via SctK/YscK.
- Andreas Diepold
- , Erdinc Sezgin
- & Judith P. Armitage
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Article
| Open AccessFrancisella requires dynamic type VI secretion system and ClpB to deliver effectors for phagosomal escape
The pathogenicity ofFrancisellaspecies largely depends on their escape from phagosomes in macrophages, mediated by a type VI secretion system (T6SS). Here, the authors show dynamics of T6SS assembly and disassembly and identify the genes essential for phagosome escape and pathogenicity in mice.
- Maj Brodmann
- , Roland F. Dreier
- & Marek Basler
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| Open AccessA Pseudomonas T6SS effector recruits PQS-containing outer membrane vesicles for iron acquisition
Pathogens require iron for their metabolism and virulence. Here the authors identify an iron acquisition system inPseudomonas aeruginosainvolving a protein secreted by a type VI secretion system, the PQS signalling compound and siderophore receptors.
- Jinshui Lin
- , Weipeng Zhang
- & Xihui Shen
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Article
| Open AccessStructure of a bacterial type III secretion system in contact with a host membrane in situ
Bacterial type III secretion systems (T3SSs) inject virulence effector proteins into eukaryotic cells and are activated by host membrane contact. Here the authors report the in situ structure of the Chlamydia trachomatisT3SS in the presence or absence of host membrane, and observe compaction of the basal body embedded in the bacterial envelope.
- Andrea Nans
- , Mikhail Kudryashev
- & Richard D. Hayward
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Article
| Open AccessA common assembly module in injectisome and flagellar type III secretion sorting platforms
In bacteria, type III secretion systems (T3SS) allow the direct transport of protein across membranes, and related elements of a sorting platform facilitate hierarchical secretion of protein substrates. Here, the authors illustrate the mechanism of selective assembly of the T3SS sorting platforms in injectisome and flagellar systems.
- Ryan Q. Notti
- , Shibani Bhattacharya
- & C. Erec Stebbins
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Bacterial killing via a type IV secretion system
Bacterial secretion systems deliver proteins to the extracellular milieu or directly into the cytoplasm of other cells. Here Souza et al. show that a type IV secretion system (T4SS) allows Xanthomonas citrito kill other Gram-negative bacterial species in a contact-dependent manner.
- Diorge P. Souza
- , Gabriel U. Oka
- & Chuck S. Farah
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High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy
Solving structures of large protein complexes remains a significant challenge for structural biologists. Demers et al. determine the atomic structure of a Shigellatype-III secretion system using a Rosetta-based modelling strategy that draws on both solid-state NMR and cryo-electron microscopy data sets.
- Jean-Philippe Demers
- , Birgit Habenstein
- & Nikolaos G. Sgourakis
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Article
| Open AccessCooperative secretions facilitate host range expansion in bacteria
Understanding the factors determining pathogen host range is critical for human health. Here, the authors show that bacteria use cooperative secretions to modify their environment and to infect multiple host species, which suggests that cooperative secretions are key determinants of host range in bacteria.
- Luke McNally
- , Mafalda Viana
- & Sam P. Brown
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Article
| Open AccessThe Vibrio cholerae type VI secretion system employs diverse effector modules for intraspecific competition
Some strains of the pathogen Vibrio choleraecan kill each other by injecting effector proteins that are toxic in the absence of cognate ‘immunity’ proteins. Here, the authors show that strains with high pathogenic potential possess matching effector-immunity sets and can coexist.
- Daniel Unterweger
- , Sarah T. Miyata
- & Stefan Pukatzki
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| Open AccessAn energy transduction mechanism used in bacterial flagellar type III protein export
A bacterial export gate complex transports flagellar proteins across the cytoplasmic membrane, but the mechanism of this process is unclear. Here, the export gate complex is revealed as a proton–protein antiporter that uses separate components of the proton motive force for different steps of the export process.
- Tohru Minamino
- , Yusuke V. Morimoto
- & Keiichi Namba