ArticleThe Journal of biological chemistry2014
The VgrG proteins are "à la carte" delivery systems for bacterial type VI effectors.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
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Who cites it
136 citing papers in PubMed, 203 citations in OpenAlex.
- Global identification of Chromobacterium violaceum T6SS effectors reveals an Rhs antibacterial toxin featuring FIX and ADP-ribosyltransferase domains.The Journal of biological chemistry · 2026Article
- Molecular basis of type VI secretion system effector loading.Nature microbiology · 2026Article
- Pan-genome insights into type VI secretion systems and their functional repertoires inmSystems · 2026Article
- AnMicrobiology spectrum · 2026Article
- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Effector conformational plasticity enables lineage-specific secretion via Hcp heterohexamers in gut symbionts.Nature communications · 2026Article
- Structural insights into the antibacterial function of the Pseudomonas putida effector Tke5.The EMBO journal · 2026Article
- Biophysical characterization of Eag chaperones suggests the mechanism of effector transmembrane domain release.Nature communications · 2026Article
- The Putative RNA Methyltransferase Modulates T3SS Expression and Host NF-κB Activation via T6SS-Mediated Translocation inInternational journal of molecular sciences · 2026Article
- Distinct immunity protein families mediate compartment-specific neutralization of a bacterial toxin.Cell reports · 2025Article
- Genomic profiling and experimental validation of type VI secretion system-associated proteins in Klebsiella.PLoS genetics · 2025Article
- The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux.PLoS pathogens · 2025Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- A new class of type VI secretion system effectors can carry two toxic domains and are recognized through the WHIX motif for export.PLoS biology · 2025Article
- Distribution of the four type VI secretion systems in Pseudomonas aeruginosa and classification of their core and accessory effectors.Nature communications · 2025Article
- Specialized killing across the domains of life by the type VI secretion systems of Pseudomonas aeruginosa.The Biochemical journal · 2025Review
- Proteogenomic annotation of T6SS components identified inFrontiers in microbiology · 2025Article
- Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition.PLoS genetics · 2024Article
- Advanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein.Nature communications · 2024Article
76 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The bacterial type VI secretion system (T6SS) is a supra-molecular complex akin to bacteriophage tails, with VgrG proteins acting as a puncturing device. The Pseudomonas aeruginosa H1-T6SS has been extensively characterized. It is involved in bacterial killing and in the delivery of three toxins, Tse1-3. Here, we demonstrate the independent contribution of the three H1-T6SS co-regulated vgrG genes, vgrG1abc, to bacterial killing. A putative toxin is encoded in the vicinity of each vgrG gene, supporting the concept of specific VgrG/toxin couples. In this respect, VgrG1c is involved in the delivery of an Rhs protein, RhsP1. The RhsP1 C terminus carries a toxic activity, from which the producing bacterium is protected by a cognate immunity. Similarly, VgrG1a-dependent toxicity is associated with the PA0093 gene encoding a two-domain protein with a putative toxin domain (Toxin_61) at the C terminus. Finally, VgrG1b-dependent killing is detectable upon complementation of a triple vgrG1abc mutant. The VgrG1b-dependent killing is mediated by PA0099, which presents the characteristics of the superfamily nuclease 2 toxin members. Overall, these data develop the concept that VgrGs are indispensable components for the specific delivery of effectors. Several additional vgrG genes are encoded on the P. aeruginosa genome and are not linked genetically to other T6SS genes. A closer inspection of these clusters reveals that they also encode putative toxins. Overall, these associations further support the notion of an original form of secretion system, in which VgrG acts as the carrier.
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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.