ArticlePLoS pathogens2014
A substrate-fusion protein is trapped inside the Type III Secretion System channel in Shigella flexneri.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- From gut colonization to recurrence:Gut microbes · 2026Review
- Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026Article
- A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.bioRxiv : the preprint server for biology · 2026Article
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- Evolutionary Conservation, Variability, and Adaptation of Type III Secretion Systems.The Journal of membrane biology · 2022Review
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation.Nature communications · 2021Article
- TheMicroorganisms · 2021Review
- Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021Review
- Staying out or Going in? The Interplay between Type 3 and Type 5 Secretion Systems in Adhesion and Invasion of Enterobacterial Pathogens.International journal of molecular sciences · 2020Review
- Delivery of Heterologous Proteins, Enzymes, and Antigens via the Bacterial Type III Secretion System.Microorganisms · 2020Review
- Cryo-EM structure of the Shigella type III needle complex.PLoS pathogens · 2020Article
- Identification of specific sequence motif of YopN of Yersinia pseudotuberculosis required for systemic infection.Virulence · 2019Article
- Review
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- YopN Is Required for Efficient Effector Translocation and Virulence in Yersinia pseudotuberculosis.Infection and immunity · 2018Article
- Flagella-mediated secretion of a novelCommunications biology · 2018Article
- Assembly, structure, function and regulation of type III secretion systems.Nature reviews. Microbiology · 2017Review
- Tracking Proteins Secreted by Bacteria: What's in the Toolbox?Frontiers in cellular and infection microbiology · 2017Review
- Identification of novel substrates of Shigella T3SA through analysis of its virulence plasmid-encoded secretome.PloS one · 2017Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Type III Secretion System (T3SS) is a macromolecular complex used by Gram-negative bacteria to secrete effector proteins from the cytoplasm across the bacterial envelope in a single step. For many pathogens, the T3SS is an essential virulence factor that enables the bacteria to interact with and manipulate their respective host. A characteristic structural feature of the T3SS is the needle complex (NC). The NC resembles a syringe with a basal body spanning both bacterial membranes and a long needle-like structure that protrudes from the bacterium. Based on the paradigm of a syringe-like mechanism, it is generally assumed that effectors and translocators are unfolded and secreted from the bacterial cytoplasm through the basal body and needle channel. Despite extensive research on T3SS, this hypothesis lacks experimental evidence and the mechanism of secretion is not fully understood. In order to elucidate details of the T3SS secretion mechanism, we generated fusion proteins consisting of a T3SS substrate and a bulky protein containing a knotted motif. Because the knot cannot be unfolded, these fusions are accepted as T3SS substrates but remain inside the NC channel and obstruct the T3SS. To our knowledge, this is the first time substrate fusions have been visualized together with isolated NCs and we demonstrate that substrate proteins are secreted directly through the channel with their N-terminus first. The channel physically encloses the fusion protein and shields it from a protease and chemical modifications. Our results corroborate an elementary understanding of how the T3SS works and provide a powerful tool for in situ-structural investigations in the future. This approach might also be applicable to other protein secretion systems that require unfolding of their substrates prior to secretion.
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