Herpes simplex virus 1 cell entry receptor (HSV-1 cell entry receptor)

Herpes simplex virus 1 cell entry receptors are a heterogeneous group of host cell surface molecules exploited by HSV-1 for initial attachment, viral envelope fusion, and subsequent infection. Key receptors include nectin-1 (a cell adhesion molecule of the immunoglobulin superfamily), HVEM (herpesvirus entry mediator, a member of the TNF receptor family), 3-O-sulfated heparan sulfate (a glycosaminoglycan modification recognized by viral glycoprotein D), and, for certain viral envelope glycoproteins, integrins (αvβ6, αvβ8)[1][2][3][4][6]. Viral glycoprotein D (gD) specifically engages nectin-1, HVEM, or 3-O-sulfated heparan sulfate, triggering a conformational change that enables other viral glycoproteins (gB, gH, gL) to mediate fusion or endocytosis. These receptors are considered valid therapeutic targets for novel antiviral agents and are under investigation in research settings. However, current clinical therapies do not directly target host cell entry mechanisms. Their expression is cell type–dependent, influencing tissue tropism and clinical manifestation of HSV-1 infection[5].

Other names

HSV-1 entry receptorherpes simplex virus 1 entry receptor

Viral attachment blockade: Inhibitor binds viral glycoproteins or host entry receptor, preventing initial HSV binding.\nFusion inhibition: Interference with glycoprotein–receptor interactions that enable membrane fusion, entry, and cell-to-cell spread.