To investigate whether the binding between DC-SIGN and Gx-psDiMan in solution faithfully replicates binding at the cell surface, we further investigated the ability of GNP-psDiMan to block DC-SIGN-promoted cellular entry of particles pseudotyped with the Ebola virus glycoprotein (EBOVpp). The specific binding between DC-SIGN and the Ebola virus glycoprotein (EBOV-GP) promotes viral attachment and entry into host cells, which ultimately leads to infection. Binding of high affinity Gx-psDiMan to cell surface DC-SIGN should prevent binding of EBOV-GP to DC-SIGN, thereby blocking virus cellular entry and infection. Compared to other antiviral strategies, the use of entry inhibitors to block viral infection can be advantageous, since this can minimize virus developing resistance. Here, HEK293T cells transfected to express full length DC-SIGN and EBOVpp were employed to evaluate the antiviral properties of Gx-psDiMan (x = 5, 13) with 50% or 100% psDiMan content as described previously. The antiviral experiments were performed in DMEM medium supplemented with 10% feta bovine serum (FBS) as described previously. The raw inhibition data (luciferase activities) for each experiments together with negative controls were given in SI, Fig. . The normalized inhibition data (after correction of the background from control viral particles encoding no EBOV-GP gene) were fitted by a modified inhibition model as shown in eq. 6: 14, 48