Herpes simplex virus 1 entry receptors

Host cell receptors for HSV-1 entry are a diverse group of cell surface molecules that facilitate the multi-step process of Herpes Simplex Virus type 1 (HSV-1) infection. The process begins with the attachment of viral glycoproteins gB and gC to heparan sulfate proteoglycans (HSPGs) on the host cell surface [1, 9]. This is followed by the binding of viral glycoprotein D (gD) to one of several specific entry receptors, including Nectin-1 (also known as Poliovirus receptor-related protein 1), Herpesvirus entry mediator (HVEM, a member of the TNF receptor superfamily), or 3-O-sulfated heparan sulfate [2, 3, 7]. These interactions trigger a conformational change in gD that recruits the core fusion machinery (gB and the gH/gL complex), leading to the fusion of the viral envelope with the host plasma membrane or endosomal membrane [1, 12]. Different receptors are utilized depending on the cell type; for example, Nectin-1 is the primary receptor for epithelial and neuronal cells, while HVEM is critical for entry into T lymphocytes [3, 12]. Targeting these receptors or their interactions with viral glycoproteins is a key area of antiviral research, with drugs like docosanol acting as fusion inhibitors and various experimental peptides and small molecules designed to block attachment or receptor binding [4, 10, 18].

Other names

Host cell receptors for HSV-1 entryHSV-1 entry receptorsgD receptorsNectin-1 (PVRL1, HveC)Herpesvirus entry mediator (HVEM, TNFRSF14, HveA)3-O-sulfated heparan sulfate (3-OS HS)Heparan sulfate proteoglycans (HSPG)Nectin-2 (PVRL2, HveB)Paired immunoglobulin-like type 2 receptor alpha (PILRα)Non-muscle myosin heavy chain IIA (NMHC-IIA)Myelin-associated glycoprotein (MAG)

Inhibition of viral-host membrane fusion, blocking of viral attachment to cell surface proteoglycans, and downregulation of receptor expression.