Given the strong affinities (low apparent Kds) of Gx-DiMan in binding to DC-SIGN/R, we anticipated that they should be strong inhibitors in blocking DC-SIGN/R-mediated viral infections, exemplified using the pseudo-Ebola virus. Therefore, Gx-DiMans were tested for their ability to inhibit cell surface DC-SIGN/R promoted entry of the pseudo-Ebola virus using a model cellular infection assay. Here, single cycle murine leukaemia virus (MLV) particles pseudotyped with the Ebola virus glycoprotein (EBOV-GP) and encoding the luciferase gene were used (EBOVpp). As target cells, we employed human embryonic kidney cells, 293T, transfected to express DC-SIGN and DC-SIGNR, as described previously. This well-established cellular assay provides a robust readout (luciferase activity indicating infectious entry) for evaluating antiviral properties of glycoconjugates targeting DC-SIGN/R. Binding of Gx-DiMan to cell surface DC-SIGN/R will block these lectin receptors from binding to EBOV-GP spikes on the virus surface, reducing virus cellular entry and hence luciferase production as shown in SI, Fig. schematically. MLV particles bearing the vesicular stomatitis virus glycoprotein (VSV-G) that does not employ DC-SIGN/R for cell entry were employed as specificity control, while MLV particles encoding luciferase but bearing no viral glycoprotein were used as negative control. All experiments assessing antiviral activity of Gx-DiMan (positive controls)