Integrin-mediated signaling induced by simian virus 40 leads to transient uncoupling of cortical actin and the plasma membrane

Simian Virus 40 (SV40) is a paradigm pathogen with multivalent binding sites for the sphingolipid GM1, via which it induces its endocytosis for infection. Here we report that SV40 also utilizes cell surface integrins to activate signaling networks required for infection, even in the absence of the p...

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Bibliographic Details
Published in:PloS one 2013-02, Vol.8 (2), p.e55799-e55799
Main Authors: Stergiou, Lilli, Bauer, Manuel, Mair, Waltraud, Bausch-Fluck, Damaris, Drayman, Nir, Wollscheid, Bernd, Oppenheim, Ariella, Pelkmans, Lucas
Format: Article
Language:English
Subjects:
Actin
Actins - metabolism
Animals
Binding sites
Bioinformatics
Biology
Cell adhesion & migration
Cell Adhesion - physiology
Cell Line
Cell Membrane - metabolism
Cell membranes
Cell surface
Cellular signal transduction
Clathrin
Cortex
Cytoskeletal Proteins - metabolism
Cytoskeleton
Endocytosis
Epistasis, Genetic
Epithelial cells
Ezrin
Gangliosides
Gene Regulatory Networks
Glycosphingolipids
Glycosphingolipids - metabolism
Health aspects
Hematology
Humans
ILK protein
Infection
Infections
Integrins
Integrins - metabolism
Kinases
Medical research
Membrane Glycoproteins - metabolism
Muscle proteins
Phosphatidylinositol 3-Kinases - metabolism
Phosphorylation
Plasma
Polyomavirus Infections - genetics
Polyomavirus Infections - metabolism
Protein Binding
Protein Interaction Maps
Protein-Serine-Threonine Kinases - metabolism
Proteins
Proteomics
Proto-Oncogene Proteins c-akt
rhoA GTP-Binding Protein - metabolism
RhoA protein
RNA Interference
Signal Transduction
Signaling
Simian virus 40 - physiology
Virus Internalization
Viruses
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Description
Summary:Simian Virus 40 (SV40) is a paradigm pathogen with multivalent binding sites for the sphingolipid GM1, via which it induces its endocytosis for infection. Here we report that SV40 also utilizes cell surface integrins to activate signaling networks required for infection, even in the absence of the previously implicated glycosphingolipids. We identify ILK, PDK1, the RhoGAP GRAF1 and RhoA as core nodes of the signaling network activated upon SV40 engagement of integrins. We show that integrin-mediated signaling through host SV40 engagement induces the de-phosphorylation of Ezrin leading to uncoupling of the plasma membrane and cortical actin. Our results provide functional evidence for a mechanism by which SV40 activates signal transduction in human epithelial cells via integrins in the context of clathrin-independent endocytosis.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0055799