Type VI secretion requires a dynamic contractile phage tail-like structure
By Marek Basler, M. Pilhofer, Gregory P. Henderson, G. Jensen, J. Mekalanos. 2012
651 citations recorded by the source corpus.
Type VI secretion systems are bacterial virulence-associated nanomachines composed of proteins that are evolutionarily related to components of bacteriophage tails. Here we show that protein secretion by the type VI secretion system of Vibrio cholerae requires the action of a dynamic intracellular tubular structure that is structurally and functionally homologous to contractile phage tail sheath. Time-lapse fluorescence light microscopy reveals that sheaths of the type VI secretion system cycle between assembly, quick contraction, disassembly and re-assembly. Whole-cell electron cryotomography further shows that the sheaths appear as long tubular structures in either extended or contracted conformations that are connected to the inner membrane by a distinct basal structure. These data support a model in which the contraction of the type VI secretion system sheath provides the energy needed to translocate proteins out of effector cells and into adjacent target cells.
Subfields: Endocrinology, Genetics, Molecular Biology
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Citations in the corpus
- Probiotics and competitive exclusion of pathogens in shrimp aquaculture (2020, background): “Interestingly, the use of this system appears to be highly dynamic, with some species (such as Vibrio cholerae) employing highly offensive (non-directional) strategies (Basler et al., 2012), while others, such as P.”
- Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike (2020, neutral): “…in the envelope (Durand et al , 2015; Rapisarda et al , 2019), on which a platform that controls the assembly of a contractile tail tube/sheath structure is docked (Basler et al , 2012; Brunet et al , 2015; Logger et al , 2016; Taylor et al , 2016; Nguyen et al , 2017; Nazarov et al , 2018).”
- How the phage T4 injection machinery works including energetics, forces, and dynamic pathway (2019, background): “Despite differences in morphology, R-pyocins and phi812 (as well as T6SS) share a remarkably common structure in their injection machinery, namely, they all possess a contractile sheath composed of 6 interacting helical protein strands that drives the injection process.”
- Three-dimensional Structure of the Toxin-delivery Particle Antifeeding Prophage of Serratia entomophila * (2013, background): “This strongly validates the notion that the putative puncturing device in Afp and those in other protein-delivering T6SSs are structurally conserved, sharing a common mechanism for cell rupture (37).”