Herpes simplex virus fusion machinery (HSV fusion machinery)

The Herpes simplex virus (HSV) fusion machinery is a coordinated multi-protein complex consisting of glycoproteins gB, gD, and the gH/gL heterodimer, which are essential for viral entry and cell-to-cell spread (Campadelli-Fiume et al., 2012, Reviews in Medical Virology). The process is initiated when gD binds to host cell receptors such as Nectin-1 or Herpesvirus Entry Mediator (HVEM), triggering a signal through gH/gL to the fusogen gB (Spear, 2004, Cellular Microbiology). This machinery also mediates late-stage fusion events, leading to the formation of syncytia, which are multinucleated giant cells that facilitate direct viral transmission between adjacent cells while shielding the virus from the host immune system. Glycoprotein processing, including complex glycosylation in the host Golgi apparatus, is critical for the stability and functional competence of these proteins. Therapeutic agents like docosanol (n-docosanol) are believed to inhibit this machinery by interfering with the fusion between the viral envelope and the host plasma membrane (Pope et al., 1998, Antiviral Research). Unlike nucleoside analogs that target DNA replication, inhibitors of the fusion machinery provide a mechanism to block the earliest stages of infection and limit the spread of the virus within tissues.

Other names

HSV entry complexHSV glycoproteins (gB, gD, gH/gL)Syncytium-inducing proteinsHerpes simplex virus envelope glycoproteins

Inhibition of the fusion between the viral envelope and the host cell plasma membrane, and prevention of syncytia formation between infected and uninfected cells.