CV-N [P51G] was then tested against the previously established glycan attachment site mutants of SARS-CoV-2 (Table ). The pattern of single-site glycan mutants that resisted inhibition included all the residues identified in the WT CV-N experiment (N61D, N122D, N331D, N343D, N603D, N657D; denoted in bold in Table ), but also two additional residues not observed as contributing to resistance in either WT CV-N or GRFT experiments (N282D, N1134D). The overlap of key residues does suggest that CV-N [P51G] is attaching in a similar manner compared to the WT, but the reduced probability of dimer formation suggests that a higher overall concentration is needed to inhibit pseudovirus infection. Initial SPR binding analyses of S1-lectin interactions showed good sensorgram fits to multivalent binding models (Supplemental Figure ), in agreement with the infection inhibition results obtained with different lectin types (Figures and).