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Updated: Jul 17, 2026

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example
Published on: May 29, 2012
Tyrosine phosphorylation and lipid raft association of pseudorabies virus glycoprotein E during antibody-mediated
Ann S Desplanques1, Hans J Nauwynck, Kelly Tilleman
1Department of Virology, Parasitology and Immunology, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium. Ann.Desplanques@UGent.be
Abstract:
In specific cell types infected with the alphaherpesviruses herpes simplex virus and pseudorabies virus (PRV), addition of virus-specific antibodies results in redistribution of cell-surface-anchored viral proteins. This redistribution is triggered by the viral protein gE and consists of the directional movement of the antibody-antigen complexes to one pole of the cell. This viral capping process has been associated with increased antibody-resistant virus spread and strongly resembles immunoreceptor capping, a process that is crucial in activation of different immune cells (e.g. capping of Fcgamma-receptors, B and T cell receptors). Here, we report that the PRV gE-mediated viral capping process results in increased Src kinase-mediated tyrosine phosphorylation of the cytoplasmic domain of gE and that a fraction of gE associates with lipid rafts, all very reminiscent of immunoreceptor capping. These results provide evidence that gE-mediated capping is a viral mimicry of immunoreceptor capping.
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