Binding of HSV-1 to permissive cells occurs through viral glycoproteins on the viral envelope interacting with specific receptors on the cell surface, triggering fusion of the plasma membrane with the outer envelope. Five of these glycoproteins are known to be involved in virion binding to the cell surface: gB, gC, gD and the heterodimer gH-L. Of the five, only gC is dispensable for allowing productive infection as deletion of gB, gD or gH-L results in an entry-defective phenotype [2] [3] . gD is known to bind independently to HvEM, nectin-1 and nectin-2, whereas gH interacts with the avb3 integrin, with the paired immunoglobulin-like receptor, PILRa, acting as a receptor for gB [2] [4] [5] .