ArticlePLoS pathogens2012
Structural basis for type VI secretion effector recognition by a cognate immunity protein.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 71 citations in OpenAlex.
- Molecular basis of type VI secretion system effector loading.Nature microbiology · 2026Article
- Structural and functional insights into Pseudomonas aeruginosa's secretion systems 1-6: regulation, role in microbial keratitis and drug targets.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- From past to present: the crosstalk between type VI secretion system of Salmonella and host.Archives of microbiology · 2025Review
- Article
- Rapidly evolving orphan immunity genes protect human gut bacteria from intoxication by the type VI secretion system.bioRxiv : the preprint server for biology · 2025Article
- Selective depletion of Campylobacter jejuni via T6SS dependent functionality: an approach for improving chickens gut health.Gut pathogens · 2024Article
- Xanthomonas immunity proteins protect against the cis-toxic effects of their cognate T4SS effectors.EMBO reports · 2024Article
- Location, Location, Location: an Antidote That Both Activates and Neutralizes a Toxin Used in Bacterial Warfare.Journal of bacteriology · 2023Article
- Effectiveness of Pseudomonas aeruginosa type VI secretion system relies on toxin potency and type IV pili-dependent interaction.PLoS pathogens · 2023Article
- Article
- The Breadth and Molecular Basis of Hcp-Driven Type VI Secretion System Effector Delivery.mBio · 2021Article
- O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli.Virulence · 2018Article
- Molecular Basis for Immunity Protein Recognition of a Type VII Secretion System Exported Antibacterial Toxin.Journal of molecular biology · 2018Article
- Mechanism of loading and translocation of type VI secretion system effector Tse6.Nature microbiology · 2018Article
- Effector⁻Immunity Pairs Provide the T6SS Nanomachine its Offensive and Defensive Capabilities.Molecules (Basel, Switzerland) · 2018Review
- The Self-Identity Protein IdsD Is Communicated between Cells in Swarming Proteus mirabilis Colonies.Journal of bacteriology · 2016Article
- The T6SSs of Pseudomonas aeruginosa Strain PAO1 and Their Effectors: Beyond Bacterial-Cell Targeting.Frontiers in cellular and infection microbiology · 2016Review
- Molecular weaponry: diverse effectors delivered by the Type VI secretion system.Cellular microbiology · 2015Review
- Article
- Kin cell lysis is a danger signal that activates antibacterial pathways of Pseudomonas aeruginosa.eLife · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The type VI secretion system (T6SS) has emerged as an important mediator of interbacterial interactions. A T6SS from Pseudomonas aeruginosa targets at least three effector proteins, type VI secretion exported 1-3 (Tse1-3), to recipient Gram-negative cells. The Tse2 protein is a cytoplasmic effector that acts as a potent inhibitor of target cell proliferation, thus providing a pronounced fitness advantage for P. aeruginosa donor cells. P. aeruginosa utilizes a dedicated immunity protein, type VI secretion immunity 2 (Tsi2), to protect against endogenous and intercellularly-transferred Tse2. Here we show that Tse2 delivered by the T6SS efficiently induces quiescence, not death, within recipient cells. We demonstrate that despite direct interaction of Tsi2 and Tse2 in the cytoplasm, Tsi2 is dispensable for targeting the toxin to the secretory apparatus. To gain insights into the molecular basis of Tse2 immunity, we solved the 1.00 Å X-ray crystal structure of Tsi2. The structure shows that Tsi2 assembles as a dimer that does not resemble previously characterized immunity or antitoxin proteins. A genetic screen for Tsi2 mutants deficient in Tse2 interaction revealed an acidic patch distal to the Tsi2 homodimer interface that mediates toxin interaction and immunity. Consistent with this finding, we observed that destabilization of the Tsi2 dimer does not impact Tse2 interaction. The molecular insights into Tsi2 structure and function garnered from this study shed light on the mechanisms of T6 effector secretion, and indicate that the Tse2-Tsi2 effector-immunity pair has features distinguishing it from previously characterized toxin-immunity and toxin-antitoxin systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.