Structural Characterization and Oligomerization of the TssL Protein, a Component Shared by Bacterial Type VI and Type IVb Secretion Systems

Durand, Éric; Zoued, Abdelrahim; Spinelli, S.; Watson, P. J.; Aschtgen, Marie‐Stéphanie; Journet, Laure; Cambillau, Christian; Cascales, Éric

doi:10.1074/jbc.m111.338731

Cited by 85 publications

(72 citation statements)

References 57 publications

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“…Characterization of the B. cenocepacia T6SS results were not surprising since, with the exception of BCAL0340, orthologues of all the genes annotated as critical components in our study were also identified as genes encoding conserved core subunits essential for the T6 secretory functions in other bacteria (Durand et al, 2012;English et al, 2014;Zheng & Leung, 2007;Zheng et al, 2011;Zoued et al, 2013). However, one major difference concerned the tssJ-like BCAL0339.…”

Section: Discussionmentioning

confidence: 59%

Quantification of type VI secretion system activity in macrophages infected with Burkholderia cenocepacia

Aubert

Valvano

2015

Microbiology

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The Gram-negative bacterial type VI secretion system (T6SS) delivers toxins to kill or inhibit the growth of susceptible bacteria, while other secretion systems target eukaryotic cells. Deletion of atsR, a negative regulator of virulence factors in B. cenocepacia K56-2, increases T6SS activity. Macrophages infected with a K56-2 DatsR mutant display dramatic alterations in their actin cytoskeleton architecture that rely on the T6SS, which is responsible for the inactivation of multiple Rho-family GTPases by an unknown mechanism. We employed a strategy to standardize the bacterial infection of macrophages and densitometrically quantify the T6SS-associated cellular phenotype, which allowed us to characterize the phenotype of systematic deletions of each gene within the T6SS cluster and ten vgrG genes in K56-2 DatsR. None of the genes from the T6SS core cluster nor the individual vgrG genes were directly responsible for the cytoskeletal changes in infected cells. However, a mutant strain with all vgrG genes deleted was unable to cause macrophage alterations. Despite not being able to identify a specific effector protein responsible for the cytoskeletal defects in macrophages, our strategy resulted in the identification of the critical core components and accessory proteins of the T6SS assembly machinery and provides a screening method to detect T6SS effectors targeting the actin cytoskeleton in macrophages by random mutagenesis.

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Section: Discussionmentioning

confidence: 59%

Quantification of type VI secretion system activity in macrophages infected with Burkholderia cenocepacia

Aubert

Valvano

2015

Microbiology

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“…Instead of a fully phage-like baseplate complex, the T6SS tube and sheath are anchored to the membrane via a complex related to the Legionella Dot/Icm T4SS that injects effector proteins into host cells (Figure 1). This complex consists of two inner membrane components, TssL (DotU-related) and TssM (IcmF-related) (Durand et al, 2012; Ma et al, 2009b; VanRheenen et al, 2004), and an outer-membrane lipoprotein (TssJ) (Felisberto-Rodrigues et al, 2011) (Figure 2). In some organisms this complex is thought to be anchored to the peptidoglycan through an extension domain of TssL or through an additional accessory protein (Aschtgen et al, 2010).…”

Section: T6ss Components Structure and Energeticsmentioning

confidence: 99%

A View to a Kill: The Bacterial Type VI Secretion System

Dong

Mekalanos

2014

Cell Host & Microbe

532

556

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The bacterial Type 6 Secretion System (T6SS) is an organelle that is structurally and mechanistically analogous to an intracellular membrane-attached contractile phage tail. Recent studies determined that a rapid conformational change in the structure of a sheath protein complex propels T6SS spike and tube components along with anti-bacterial and anti-eukaryotic effectors out of predatory T6SS+ cells and into prey cells. The contracted organelle is then recycled in an ATP-dependent process. T6SS is regulated at transcriptional and post-translational levels, the latter involving detection of membrane perturbation in some species. In addition to directly targeting eukaryotic cells, the T6SS can also target other bacteria co-infecting a mammalian host, highlighting the importance of the T6SS not only for bacterial survival in environmental ecosystems but also in the context of infection and disease. This review highlights these and other advances in our understanding of the structure, mechanical function, assembly, and regulation of the T6SS.

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“…Biochemical, structural, and protein-protein interaction studies have provided insights onto the characteristics of these subunits (26 -31). While TssL is a bitopic membrane protein with its N terminus located in the cytoplasm (28,30,31), TssM has three transmembrane helices (TMH) with a large C-terminal periplasmic domain interacting with the TssJ outer membrane lipoprotein (25,27,29). A cytoplasmic loop located between TMH2 and TMH3 contains an ATP binding and hydrolysis Walker A motif that was shown to be required for T6SS function in Agrobacterium tumefaciens (28).…”

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confidence: 99%

TssK Is a Trimeric Cytoplasmic Protein Interacting with Components of Both Phage-like and Membrane Anchoring Complexes of the Type VI Secretion System

Zoued

Durand

Bebeacua

et al. 2013

Journal of Biological Chemistry

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104

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Structural Characterization and Oligomerization of the TssL Protein, a Component Shared by Bacterial Type VI and Type IVb Secretion Systems

Cited by 85 publications

References 57 publications

Quantification of type VI secretion system activity in macrophages infected with Burkholderia cenocepacia

Quantification of type VI secretion system activity in macrophages infected with Burkholderia cenocepacia

A View to a Kill: The Bacterial Type VI Secretion System

TssK Is a Trimeric Cytoplasmic Protein Interacting with Components of Both Phage-like and Membrane Anchoring Complexes of the Type VI Secretion System

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