Herpesvirus envelope glycoprotein-heparan sulfate proteoglycan interface (HSV gB/gC-HSPG interface)

The herpesvirus envelope glycoprotein-heparan sulfate proteoglycan interface is the primary site for the initial attachment of herpesviruses, such as Herpes Simplex Virus (HSV), to host cells. This interaction typically involves viral glycoproteins gC and gB binding to the glycosaminoglycan chains of host cell surface heparan sulfate proteoglycans (HSPGs) [1][2]. This tethering step is crucial for concentrating the virus on the cell surface and facilitating subsequent interactions with entry receptors like nectin-1 or HVEM, leading to membrane fusion [3]. Because this interface is essential for the initiation of infection, it serves as a significant therapeutic target for entry inhibitors [4]. Drugs targeting this interface, such as heparin mimetics or polyanionic compounds, work by competitively binding to the viral glycoproteins, thereby preventing the virus from docking onto the host cell [5].

Other names

Herpesvirus attachment complexgC-HSPG interactiongB-HSPG interactionViral glycoprotein-proteoglycan interfaceHerpesvirus envelope glycoproteins at the host proteoglycan attachment interface

Competitive inhibition of viral attachment to host cell surface heparan sulfate proteoglycans.