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Updated: Jul 18, 2026

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
Published on: September 19, 2013
[Listeria-induced host cellular actin cytoskeleton rearrangement and phospholipase D]
Li Han1, Xu-Qin Wu, Yu-Fen Meng
1Chinese PLA Center for Disease Control & Prevention, Beijing 100071, China. Lihan@301hospital.com
Abstract:
Either phagocytosis of macrophage to pathogen or pathogen-induced invasion into non-professional phagocytes, such as epithelial cells, require actin cytoskeletal rearrangements and remodeling of the plasma membrane, which are regulated precisely by monogeric GTPase and the correlated proteins. As a key signaling molecule in the cell, phosphotidicphospholipase D (PLD) regulates or interacts directly with cellular actin cytoskeleton rearrangement. Phospholipase D plays an important role in FcgammaRI and C-reactive protein-mediated phagocytosis and phosphorylated cofilin, a ADF (actin depolymerizing factor) is able to bind to phospholipase D and stimulate it; meanwhile, the Listeria-induced actin cytoskeleton rearrangement during the infection is controlled by the phosphorylation of cofilin. Thus, it made challenge to disclose the function of PLD on the regulation of Listeria-induced actin cytoskeleton rearrangement during infection, furthermore, it may provide us more understanding on the role of PLD in the infection and inflammation, which is essential to dissect the molecular mechanism of bacterial-host interaction more thoroughly.
Insights
Phospholipase D (PLD) regulates actin cytoskeleton rearrangement, crucial for pathogen invasion and macrophage phagocytosis. Understanding PLD
Area of Science:
- Cell Biology
- Microbiology
- Biochemistry
Context:
- Pathogen entry into host cells and macrophage phagocytosis rely on actin cytoskeleton dynamics.
- Monomeric GTPases and associated proteins precisely control these cellular rearrangements.
- Phosphatidylinositol-specific phospholipase D (PLD) is a key signaling molecule interacting with the actin cytoskeleton.
Purpose:
- To investigate the function of PLD in regulating Listeria-induced actin cytoskeleton rearrangement during infection.
- To elucidate the molecular mechanisms underlying bacterial-host interactions.
Summary:
- PLD regulates actin cytoskeleton rearrangement, essential for phagocytosis and pathogen invasion.
- PLD interacts with cofilin, a key regulator of actin dynamics, influencing Listeria infection.
- This study challenges the understanding of PLD's role in Listeria-induced cytoskeletal changes.
Impact:
- Provides deeper insights into PLD's role in infection and inflammation.
- Enhances understanding of bacterial-host molecular interactions.
- Contributes to dissecting the complex signaling pathways in host-pathogen dynamics.
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