Septins regulate bacterial entry into host cells.

PloS One
Serge MostowyPascale Cossart

Abstract

Septins are conserved GTPases that form filaments and are required in many organisms for several processes including cytokinesis. We previously identified SEPT9 associated with phagosomes containing latex beads coated with the Listeria surface protein InlB. Here, we investigated septin function during entry of invasive bacteria in non-phagocytic mammalian cells. We found that SEPT9, and its interacting partners SEPT2 and SEPT11, are recruited as collars next to actin at the site of entry of Listeria and Shigella. SEPT2-depletion by siRNA decreased bacterial invasion, suggesting that septins have roles during particle entry. Incubating cells with InlB-coated beads confirmed an essential role for SEPT2. Moreover, SEPT2-depletion impaired InlB-mediated stimulation of Met-dependent signaling as shown by FRET. Together these findings highlight novel roles for SEPT2, and distinguish the roles of septin and actin in bacterial entry.

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Citations

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Methods Mentioned

BETA
GTPases
immunoprecipitation
scanning electron microscopy
fluorescence
FRET
GTPase
FCS
Transfection

Software Mentioned

ImageJ
Excel
Metamorph Imaging System
XPATH ERROR

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