Herpes simplex virus type 2 fusion machinery (HSV-2 fusion machinery) (HSV-2 fusion machinery)

The Herpes simplex virus type 2 (HSV-2) fusion machinery is a multi-protein complex essential for the virus to enter host cells and spread between them (Atanasiu et al., 2010). This machinery is composed of four essential glycoproteins: glycoprotein D (gD), glycoprotein B (gB), and the heterodimer formed by glycoproteins H and L (gH/gL) (Eisenberg et al., 2012). The entry process is initiated by gD binding to specific host cell receptors, such as Nectin-1 or Herpesvirus Entry Mediator (HVEM), which triggers a cascade of conformational changes (Heldwein & Krummenacher, 2008). These changes are transmitted through the gH/gL complex to gB, the primary fusogen, which then inserts into the host membrane to facilitate pore formation and viral genome delivery (Atanasiu et al., 2010). Because these proteins are critical for the viral life cycle and are exposed on the virion surface, they serve as the primary targets for neutralizing antibodies and entry-inhibiting therapeutics (Chowdhury et al., 2021). Targeting these proteins aims to prevent the initial infection of epithelial cells and the subsequent colonization of sensory neurons where the virus establishes latency (Huang et al., 2019). Therapeutic agents like the monoclonal antibody UB-621 specifically target gD to block receptor binding and prevent viral entry (Huang et al., 2019). Other approaches include small molecules like docosanol, which interfere with the fusion process, and vaccines designed to elicit antibodies against the gD and gB components (ClinicalTrials.gov, 2024).

Other names

HSV-2 entry machineryHSV-2 gB/gD/gH/gL complexHerpes simplex virus 2 envelope glycoproteins

Inhibition of viral-host membrane fusion by blocking glycoprotein-receptor interactions or preventing conformational changes in the fusion protein complex.