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Nature. 2015 Jul 30;523(7562):555-60. doi: 10.1038/nature14667. Epub 2015 Jul 22.

Biogenesis and structure of a type VI secretion membrane core complex.

Author information

1
1] Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France [2] Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France [3] G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [4] UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [5] AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
2
1] Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France [2] AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
3
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
4
UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France.
5
1] UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [2] Unité de Bioinformatique Structurale, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France.
6
1] G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [2] UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France.

Abstract

Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence determinant during bacterial infections. It assembles a nano-crossbow-like structure in the cytoplasm of the attacker cell that propels an arrow made of a haemolysin co-regulated protein (Hcp) tube and a valine-glycine repeat protein G (VgrG) spike and punctures the prey's cell wall. The nano-crossbow is stably anchored to the cell envelope of the attacker by a membrane core complex. Here we show that this complex is assembled by the sequential addition of three type VI subunits (Tss)-TssJ, TssM and TssL-and present a structure of the fully assembled complex at 11.6 Å resolution, determined by negative-stain electron microscopy. With overall C5 symmetry, this 1.7-megadalton complex comprises a large base in the cytoplasm. It extends in the periplasm via ten arches to form a double-ring structure containing the carboxy-terminal domain of TssM (TssMct) and TssJ that is anchored in the outer membrane. The crystal structure of the TssMct-TssJ complex coupled to whole-cell accessibility studies suggest that large conformational changes induce transient pore formation in the outer membrane, allowing passage of the attacking Hcp tube/VgrG spike.

PMID:
26200339
DOI:
10.1038/nature14667
[Indexed for MEDLINE]
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