Type
            <scp>VI</scp>
            secretion and bacteriophage tail tubes share a common assembly pathway

Brunet, Yannick R.; Hénin, Jérôme; Celia, Hervé; Cascales, Éric

doi:10.1002/embr.201337936

Cited by 118 publications

(137 citation statements)

References 26 publications

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“…assemble hexamers that stack on each other to form the T6SS tail tube (52,53). In addition to being a structural component of the apparatus, Hcp hexamers are delivered into target cells and serve as chaperone and cargo for toxin effectors (23, 53).…”

Section: Discussionmentioning

confidence: 99%

Salmonella Typhimurium utilizes a T6SS-mediated antibacterial weapon to establish in the host gut

Sana

Flaugnatti

Lugo

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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300

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The mammalian gastrointestinal tract is colonized by a high-density polymicrobial community where bacteria compete for niches and resources. One key competition strategy includes cell contact-dependent mechanisms of interbacterial antagonism, such as the type VI secretion system (T6SS), a multiprotein needle-like apparatus that injects effector proteins into prokaryotic and/or eukaryotic target cells. However, the contribution of T6SS antibacterial activity during pathogen invasion of the gut has not been demonstrated. We report that successful establishment in the gut by the enteropathogenic bacterium Salmonella enterica serovar Typhimurium requires a T6SS encoded within Salmonella pathogenicity island-6 (SPI-6). In an in vitro setting, we demonstrate that bile salts increase SPI-6 antibacterial activity and that S. Typhimurium kills commensal bacteria in a T6SS-dependent manner. Furthermore, we provide evidence that one of the two T6SS nanotube subunits, Hcp1, is required for killing Klebsiella oxytoca in vitro and that this activity is mediated by the specific interaction of Hcp1 with the antibacterial amidase Tae4. Finally, we show that K. oxytoca is killed in the host gut in an Hcp1-dependent manner and that the T6SS antibacterial activity is essential for Salmonella to establish infection within the host gut. Our findings provide an example of pathogen T6SS-dependent killing of commensal bacteria as a mechanism to successfully colonize the host gut.

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Section: Discussionmentioning

confidence: 99%

Salmonella Typhimurium utilizes a T6SS-mediated antibacterial weapon to establish in the host gut

Sana

Flaugnatti

Lugo

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

300

292

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“…Important components include Hcp, which forms a polymerized tubular structure that is secreted out of the cell and is essential for protein secretion, and VgrGs, which are present at the tip of this structure and can have effector activity or facilitate effector secretion (82). The T6SS bears striking similarity to bacteriophage, both structurally and functionally (83).…”

Section: Protein Secretionmentioning

confidence: 99%

Pathogenic Acinetobacter: from the Cell Surface to Infinity and Beyond

2016

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The genus Acinetobacter encompasses multiple nosocomial opportunistic pathogens that are of increasing worldwide relevance because of their ability to survive exposure to various antimicrobial and sterilization agents. Among these, Acinetobacter baumannii, Acinetobacter nosocomialis, and Acinetobacter pittii are the most frequently isolated in hospitals around the world. Despite the growing incidence of multidrug-resistant Acinetobacter spp., little is known about the factors that contribute to pathogenesis. New strategies for treating and managing infections caused by multidrug-resistant Acinetobacter strains are urgently needed, and this requires a detailed understanding of the pathobiology of these organisms. In recent years, some virulence factors important for Acinetobacter colonization have started to emerge. In this review, we focus on several recently described virulence factors that act at the bacterial surface level, such as the capsule, O-linked protein glycosylation, and adhesins. Furthermore, we describe the current knowledge regarding the type II and type VI secretion systems present in these strains.

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“…The system is composed of a long sheath surrounding an inner tube attached to a baseplate and anchored to a membrane complex that spans both membranes (Brunet et al , 2014, 2015; Durand et al , 2015). T6SS biogenesis starts by formation of the membrane complex composed of TssJLM, which recruits TssK to connect a baseplate composed of TssEFG, as well as VgrG/PAAR spike and effectors (Brunet et al , 2015; Durand et al , 2015).…”

Section: Introductionmentioning

confidence: 99%

Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

et al. 2017

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The bacterial Type VI secretion system (T6SS) assembles from three major parts: a membrane complex that spans inner and outer membranes, a baseplate, and a sheath–tube polymer. The baseplate assembles around a tip complex with associated effectors and connects to the membrane complex by TssK. The baseplate assembly initiates sheath–tube polymerization, which in some organisms requires TssA. Here, we analyzed both ends of isolated non‐contractile Vibrio cholerae sheaths by cryo‐electron microscopy. Our analysis suggests that the baseplate, solved to an average 8.0 Å resolution, is composed of six subunits of TssE/F2/G and the baseplate periphery is decorated by six TssK trimers. The VgrG/PAAR tip complex in the center of the baseplate is surrounded by a cavity, which may accommodate up to ~450 kDa of effector proteins. The distal end of the sheath, resolved to an average 7.5 Å resolution, shows sixfold symmetry; however, its protein composition is unclear. Our structures provide an important step toward an atomic model of the complete T6SS assembly.

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Type VI secretion and bacteriophage tail tubes share a common assembly pathway

Cited by 118 publications

References 26 publications

Salmonella Typhimurium utilizes a T6SS-mediated antibacterial weapon to establish in the host gut

Salmonella Typhimurium utilizes a T6SS-mediated antibacterial weapon to establish in the host gut

Pathogenic Acinetobacter: from the Cell Surface to Infinity and Beyond

Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

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