The indication that positions N61, N122 & N603 could be involved with CV-N binding is strengthened by reports showing that these sites often bear high-mannose oligosaccharides (1). It is surprising, however, that the RBD glycan attachment sites (N331 & N343) were implicated in pseudovirus sensitivity to CV-N as these two sites are known to bear predominantly complex oligosaccharides (1). CV-N's oligosaccharide specificity and antiviral activity has been extensively studied (>200 publications) and CV-N has always been reported to bind exclusively to high-mannose oligosaccharides, not complex oligosaccharides . The results here are a potential indicator of more global changes in Spike structure and glycosylation may have resulted from the mutation of oligosaccharide attachment sites, including possible cooperative effects between glycan sites. For example, RBD glycans have recently been reported to not be binding sites for CV-N (Muñoz-Basagoiti et al. PNAS, 2023, in press), and CV-N and GRFT binding were shown not to interfere with ACE2 binding .