Mechanistic insight into bacterial entrapment by septin cage reconstitution

Septins are cytoskeletal proteins that assemble into hetero-oligomeric complexes and sense micron-scale membrane curvature. During infection with Shigella flexneri, an invasive enteropathogen, septins restrict actin tail formation by entrapping bacteria in cage-like structures. Here, we reconstitute septin cages in vitro using purified recombinant septin complexes (SEPT2-SEPT6-SEPT7), and study how these recognize bacterial cells and assemble on their surface. We show that septin complexes recognize the pole of growing Shigella cells. An amphipathic helix domain in human SEPT6 enables septins to sense positively curved membranes and entrap bacterial cells. Shigella strains lacking lipopolysaccharide components are more efficiently entrapped in septin cages. Finally, cryo-electron tomography of in vitro cages reveals how septins assemble as filaments on the bacterial cell surface. Septins are cytoskeletal proteins that assemble into complexes and contribute to immunity by entrapping intracellular bacteria in cage-like structures. Here, Lobato-Marquez et al. reconstitute septin cages in vitro using purified recombinant complexes, and study how these recognize bacterial cells and assemble as filaments on their surface.

Automated summary

Septins are cytoskeletal proteins that form cage-like structures to restrict the movement of bacteria within cells. Research shows that septin complexes can recognize bacterial cells and assemble as filaments on their surface.