Breadth of function. The abundant glycan modifications on the exposed SARS-CoV-2 Spike surface have been found by sequence comparisons to be highly conserved in homologous amino acid positions in the known virus variants . On this basis, it may be proposed that multivalent targeting of key glycans on SARS-CoV-2 Spike improves the chances of avoiding facile mutational escape by the virus. Indeed, the substantial breadth of lectin antiviral effects observed in this current work and elsewhere for variants of SARS-CoV-2 supports this expectation. Furthermore, the antiviral effects observed with a fully infectious coronavirus that is not in the SARS-CoV-2 line argues for a potential broad spectrum anti-coronavirus activity as has been previously reported for GRFT in an investigation of its activity against SARS-CoV-1 . As several single glycan-attachment site mutants identified in the current work reduced their lectin sensitivity, the possibility that mutational escape to a lectin treatment could occur. However, importantly, the single site variants that were found in the current study to cause loss of lectin antagonism also have greatly reduced infectivity. Thus, it is highly unlikely that such mutants would survive, thereby mitigating against lectin escape via single-site glycan mutations.