TY - JOUR
T1 - A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly
AU - Bergeron, Julien R. C.
AU - Worrall, Liam J.
AU - Sgourakis, Nikolaos G.
AU - Dimaio, Frank
AU - Pfuetzner, Richard A.
AU - Felise, Heather B.
AU - Vuckovic, Marija
AU - Yu, Angel C.
AU - Miller, Samuel I.
AU - Baker, David
AU - Strynadka, Natalie C. J.
A2 - Kubori, Tomoko
PY - 2013/4/25
Y1 - 2013/4/25
N2 - The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a “basal body”, a lock-nut structure spanning both bacterial membranes, and a “needle” that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism.
AB - The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a “basal body”, a lock-nut structure spanning both bacterial membranes, and a “needle” that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism.
U2 - 10.1371/journal.ppat.1003307
DO - 10.1371/journal.ppat.1003307
M3 - Article
SN - 1553-7366
VL - 9
JO - PLoS Pathogens
JF - PLoS Pathogens
IS - 4
M1 - e1003307
ER -