A role for heparan sulfate in viral surfing.
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.
Oh
Myung-Jin
MJ
Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, IL 60612, USA.
Akhtar
Jihan
J
Desai
Prashant
P
Shukla
Deepak
D
D002462:Cell Membrane / Q000821:virology; D006497:Heparan Sulfate / Q000502:physiology*; D018259:Herpesvirus 1, Human / Q000235:genetics / Q000502:physiology*; D006801:Humans; D009154:Mutation; D011554:Pseudopodia / Q000821:virology*; D045663:Quantum Dots; D014759:Viral Envelope Proteins / Q000235:genetics / Q000502:physiology*; D053585:Virus Attachment; D053586:Virus Internalization
D006497:Heparan Sulfate; D014759:Viral Envelope Proteins; C040495:glycoprotein B, Simplexvirus