Herpes simplex virus 1 envelope glycoprotein B and C heparan sulfate binding sites (HSV-1 gB/gC-HS binding sites)

The Herpes simplex virus 1 (HSV-1) envelope glycoproteins B (gB) and C (gC) contain specific binding sites that interact with heparan sulfate (HS) proteoglycans on the surface of host cells (Shukla & Spear, 2001, J Clin Invest). This interaction represents the initial tethering or attachment phase of the viral life cycle, which is essential for concentrating the virions on the host cell membrane before secondary receptors trigger membrane fusion (UniProt P06437, P06473). Glycoprotein C is the primary mediator of this initial attachment, while glycoprotein B provides a secondary attachment mechanism and is crucial for the subsequent fusion of the viral envelope with the host cell membrane. Because this interaction is a prerequisite for infection, these binding sites are significant therapeutic targets for entry inhibitors. Drugs targeting these sites, such as heparan sulfate mimetics or polyanionic compounds like Muparfostat, act by competitively blocking the virus from docking onto the host cell (PubMed PMID: 11601680). Such interventions are explored for the treatment and prevention of HSV-1 related diseases, including orolabial herpes, keratitis, and more severe manifestations like viral encephalitis.

Other names

HSV-1 gB and gC heparin-binding domainsHSV-1 attachment receptorsHeparan sulfate-binding glycoproteins of HSV-1HSV-1 HS-binding sites

Competitive inhibition of viral attachment to host cell heparan sulfate proteoglycans (HSPGs) by mimicking the host receptor or blocking the viral glycoprotein binding domains.