Herpes simplex virus type 1 (HSV-1) virion and attachment proteins (HSV-1)

Herpes simplex virus type 1 (HSV-1) is a highly prevalent human pathogen that causes primary and recurrent infections, most commonly manifesting as oral cold sores. The HSV-1 virion is a complex structure consisting of a double-stranded DNA genome, an icosahedral capsid, a proteinaceous tegument, and a lipid envelope containing at least 12 glycoproteins. The attachment and entry process is a multi-step mechanism involving the binding of viral glycoproteins gC and gB to host heparan sulfate proteoglycans, followed by gD binding to specific entry receptors such as Nectin-1 or Herpesvirus Entry Mediator (HVEM) (NIH: HSV-1 Entry Mechanisms, 2021). This interaction triggers a conformational change in the gH/gL complex, which activates the fusion protein gB to merge the viral envelope with the host cell membrane (UniProt: P06437). Therapeutic strategies targeting this process, such as the over-the-counter drug docosanol, aim to prevent the virus from entering host cells, thereby limiting viral replication and spread (PubChem: CID 12620). Understanding these molecular interactions is crucial for developing next-generation antivirals and vaccines to combat HSV-1 related diseases, including keratitis and encephalitis (StatPearls: Herpes Simplex Virus, 2023).

Other names

Human alphaherpesvirus 1HSV-1Herpes simplex virus 1

Inhibition of the fusion between the viral envelope and the host cell membrane, and blocking the interaction between viral glycoproteins (gB, gC, gD, gH/gL) and host cell surface receptors such as heparan sulfate proteoglycans, Nectin-1, and HVEM (StatPearls: Herpes Simplex Virus, 2023; NIH: HSV-1 Entry Mechanisms, 2021).