Pleiotropic viral TF and gC enhance FXa- and FVIIa-mediated infection by activating cellular PAR2. TF, gC, and proPL on the HSV1 surface initiate coagulation.^14,16,17  Binding of HSV1 to the host cell (eg, via gC-heparan sulfate proteoglycan, HSP), positions FVIIa and FXa proximal to PARs, where viral TF and gC combine with FVIIa and FXa, presumably in a quaternary complex, to enhance infection optimally by stimulating PAR2. A novel gC-FXa binary combination and known TF-FXa and TF-FVIIa also enhance PAR2-mediated infection. In contrast, independently of TF or gC on the virus, thrombin increases HSV1 infection through PAR1 (not shown). Therefore, HSV1 exploits multiple hemostatic functions of TF and gC to augment infection of cells.