Palladin Compensates for the Arp2/3 Complex and Supports Actin Structures during Listeria Infections

Peer reviewed: 
Yes, item is peer reviewed.
Scholarly level: 
Graduate student (PhD)
Final version published as: 

Palladin Compensates for the Arp2/3 Complex and Supports Actin Structures during Listeria Infections. Aaron S. Dhanda, A. Wayne Vogl, Sharifah E. Albraiki, Carol A. Otey, Moriah R. Beck, Julian A. Guttman mBio Apr 2018, 9 (2) e02259-17; DOI: https://doi.org/ 10.1128/mBio.02259-17.

Date created: 
2018-04-10
Keywords: 
Actin nucleation
Actin polymerization
Listeria monocytogenes
Abstract: 

Palladin is an important component of motile actin-rich structures and nucleates branched actin filament arrays in vitro. Here we examine the role of palladin during Listeria monocytogenes infections in order to tease out novel functions of palladin. We show that palladin is co-opted by L. monocytogenes during its cellular entry and intracellular motility. Depletion of palladin resulted in shorter and misshapen comet tails, and when actin- or VASP-binding mutants of palladin were overexpressed in cells, comet tails disintegrated or became thinner. Comet tail thinning resulted in parallel actin bundles within the structures. To determine whether palladin could compensate for the Arp2/3 complex, we overexpressed palladin in cells treated with the Arp2/3 inhibitor CK-666. In treated cells, bacterial motility could be initiated and maintained when levels of palladin were increased. To confirm these findings, we utilized a cell line depleted of multiple Arp2/3 complex subunits. Within these cells, L. monocytogenes failed to generate comet tails. When palladin was overexpressed in this Arp2/3 functionally null cell line, the ability of L. monocytogenes to generate comet tails was restored. Using purified protein components, we demonstrate that L. monocytogenes actin clouds and comet tails can be generated (in a cell-free system) by palladin in the absence of the Arp2/3 complex. Collectively, our results demonstrate that palladin can functionally replace the Arp2/3 complex during bacterial actin-based motility.

Description: 

The full text of this paper will be available in April, 2020 due to the embargo policies of mBio for works funded by Natural Sciences and Engineering Research Council of Canada (NSERC). Contact summit@sfu.ca to enquire if the full text of the accepted manuscript can be made available to you.” 

Language: 
English
File(s): 
Sponsor(s): 
Natural Sciences and Engineering Research Council of Canada (NSERC)
National Institutes of Health (NIH)
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