Abstract
Heparan sulfate (HS) moieties on cell surfaces are known to provide attachment sites for many viruses including herpes simplex virus type-1 (HSV-1). Here, we demonstrate that cells respond to HSV-1 infection by enhancing filopodia formation. Filopodia express HS and are subsequently utilized for the transport of HSV-1 virions to cell bodies in a surfing-like phenomenon, which is facilitated by the underlying actin cytoskeleton and is regulated by transient activation of a small Rho GTPase, Cdc42. We also demonstrate that interaction between a highly conserved herpesvirus envelope glycoprotein B (gB) and HS is required for surfing. A HSV-1 mutant that lacks gB fails to surf and quantum dots conjugated with gB demonstrate surfing-like movements. Our data demonstrates a novel use of a common receptor, HS, which could also be exploited by multiple viruses and quite possibly, many additional ligands for transport along the plasma membrane.
Original language | English (US) |
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Pages (from-to) | 176-181 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 391 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1 2010 |
Keywords
- Filopodia
- Glycoprotein
- Heparan sulfate
- Herpes simplex virus type-1
- Transport
- Viral surfing
- Virus
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology