In order to further validate the cluster hypothesis for optimal CV-N pseudovirus activity, we examined a predominantly monomeric CV-N [P51G] mutant for its ability to inhibit pseudovirus. Wild Type CV-N has two mannose-binding domains and the ability to form metastable dimers (up to 40% by mass in literature , resulting in up to 4 mannose-binding domains per dimer . We observed a similar 33% dimer content for the CV-N used in this study by measuring Western Blot band intensities with ImageJ, In contrast, the [P51G] mutation has been shown to hinder dimer formation, resulting in a strong preference for the monomeric form of CV-N (≤3% dimeric ), with only two mannose-binding domains per functional unit . CV-N [P51G] was evaluated first against WT SARS-CoV-2 (Figure ). Compared to WT CV-N, the CV-N [P51G] was a poorer inhibitor of WT SARS-CoV-2 by an order of magnitude (WT CV-N 45.96±26.17 nM, CV-N [P51G] 394.7±118.5 nM), arguing that dimer formation is a significant contributor to the potency of CV-N inhibition of SARS-CoV-2.