mDia1 Assembles a Linear F-Actin Coat at Membrane Invaginations To Drive Listeria monocytogenes Cell-to-Cell Spreading

Peer reviewed: 
Yes, item is peer reviewed.
Scholarly level: 
Faculty/Staff
Final version published as: 

Dhanda Aaron S., Vogl A. Wayne, Ness Fern, Innocenti Metello, Guttman Julian A., & Miller Samuel I. (n.d.). MDia1 Assembles a Linear F-Actin Coat at Membrane Invaginations To Drive Listeria monocytogenes Cell-to-Cell Spreading. MBio, 0(0), e02939-21. https://doi.org/10.1128/mBio.02939-21.

Date created: 
2021-11-16
Identifier: 
DOI: 10.1128/mBio.02939-21
Keywords: 
Listeria monocytogenes
Actin, cytoskeleton
Endocytosis
Host-pathogen interactions
Abstract: 

Direct cell-to-cell spreading of Listeria monocytogenes requires the bacteria to induce actin-based finger-like membrane protrusions in donor host cells that are endocytosed through caveolin-rich membrane invaginations by adjacent receiving cells. An actin shell surrounds these endocytic sites; however, its structure, composition, and functional significance remain elusive. Here, we show that the formin mDia1, but surprisingly not the Arp2/3 complex, is enriched at the membrane invaginations generated by L. monocytogenes during HeLa and Jeg-3 cell infections. Electron microscopy reveals a band of linear actin filaments that run along the longitudinal axis of the invagination membrane. Mechanistically, mDia1 expression is vital for the assembly of this F-actin shell. mDia1 is also required for the recruitment of Filamin A, a caveola-associated F-actin cross-linking protein, and caveolin-1 to the invaginations. Importantly, mixed-cell infection assays show that optimal caveolin-based L. monocytogenes cell-to-cell spreading correlates with the formation of the linear actin filament-containing shell by mDia1.

Language: 
English
Document type: 
Article
Rights: 
Rights remain with the authors.
File(s): 
Statistics: