Biogenesis and structure of a type VI secretion membrane core complex

Eric Durand, Nguyen Van Son, Abdelrahim Zoued, Laureen Logger, Gérard Péhau-Arnaudet, Marie-Stéphanie Aschtgen, Silvia Spinelli, Aline Desmyter, Benjamin Bardiaux, Annick Dujeancourt, Alain Roussel, Christian Cambillau (), Eric Cascales () and Rémi Fronzes ()
Additional contact information
Eric Durand: Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255
Nguyen Van Son: Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
Abdelrahim Zoued: Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255
Laureen Logger: Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255
Gérard Péhau-Arnaudet: UMR 3528, CNRS, Institut Pasteur
Marie-Stéphanie Aschtgen: Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255
Silvia Spinelli: Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
Aline Desmyter: Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
Benjamin Bardiaux: UMR 3528, CNRS, Institut Pasteur
Annick Dujeancourt: G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur
Alain Roussel: Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
Christian Cambillau: Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
Eric Cascales: Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255
Rémi Fronzes: G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur

Nature, 2015, vol. 523, issue 7562, 555-560

Abstract: 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.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/nature14667 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:523:y:2015:i:7562:d:10.1038_nature14667

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature14667

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().