A Type VI Secretion System of Pseudomonas aeruginosa Targets a Toxin to Bacteria

By Rachel D. Hood, Pragya Singh, F. Hsu, Tüzün Güvener, Mike A. Carl, R. Trinidad, J. M. Silverman, Brooks B Ohlson, Kevin G. Hicks, R. Plemel and 6 more. Cell Host and Microbe, 2010

898 citations recorded by the source corpus.

The functional spectrum of a secretion system is defined by its substrates. Here we analyzed the secretomes of Pseudomonas aeruginosa mutants altered in regulation of the Hcp Secretion Island-I-encoded type VI secretion system (H1-T6SS). We identified three substrates of this system, proteins Tse1-3 (type six exported 1-3), which are coregulated with the secretory apparatus and secreted under tight posttranslational control. The Tse2 protein was found to be the toxin component of a toxin-immunity system and to arrest the growth of prokaryotic and eukaryotic cells when expressed intracellularly. In contrast, secreted Tse2 had no effect on eukaryotic cells; however, it provided a major growth advantage for P. aeruginosa strains, relative to those lacking immunity, in a manner dependent on cell contact and the H1-T6SS. This demonstration that the T6SS targets a toxin to bacteria helps reconcile the structural and evolutionary relationship between the T6SS and the bacteriophage tail and spike.

Subfields: Endocrinology, Molecular Biology, Molecular Medicine

View Paper: https://www.semanticscholar.org/paper/16a550f6878f0df06e1b37557963b86b554d5c04

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In Endocrinology

1. G. Waksman
2. J. Galán

In Molecular Biology

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2. Chengping Lu
3. Jinhu Huang
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In Molecular Medicine

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Citations in the corpus

• The Hcp proteins fused with diverse extended-toxin domains represent a novel pattern of antibacterial effectors in type VI secretion systems (2017, background): “for both the assembly of a functional T6SS and the export of its effectors.(22,23,26,43) Crystallographic data of Hcp homologs showed that the protein forms hexameric rings, which can stack into a tube.”
• Protein Injection Machines in Bacteria (2018, positive): “T6SSs can serve as effective weapons against Gram-negative bacteria both of the same or of different species (Hood et al., 2010; Journet and Cascales, 2016; Kapitein and Mogk, 2013; Russell et al., 2014).”
• A Phage Tail-Derived Element with Wide Distribution among Both Prokaryotic Domains: A Comparative Genomic and Phylogenetic Study (2014, background): “We thus suggest that Afp/PVC-like elements could be classified as phage-like-protein-translocation structures (PLTSs) rather than as pyocins.”
• Pseudomonas aeruginosa: pathogenesis, virulence factors, antibiotic resistance, interaction with host, technology advances and emerging therapeutics (2022, background): “The assembled T6SS appears to be an inverted phage tail, with the Hcp (hemolysin coregulated protein)/Vgr (valine-glycine repeat protein) complex forming the distal end of the cell-puncturing device.(95) The sheath transits the effectors into targeted cells by a contraction-based mechanism.”