Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 391, Issue 1, Pages 176-181Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.11.027
Keywords
Heparan sulfate; Viral surfing; Herpes simplex virus type-1; Filopodia; Virus; Glycoprotein; Transport
Categories
Funding
- NIH [A1057860, A1081869, A133077]
- Core Grant [EY01792]
- Research to Prevent Blindness, USA
- NATIONAL EYE INSTITUTE [P30EY001792] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI061382, K02AI081869, R01AI057860, R01AI033077] Funding Source: NIH RePORTER
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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 falls to surf and quantum clots 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 (c) 2009 Elsevier Inc. All rights reserved.
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