Holmes et al. (1981) showed that a corona virus, mouse hepatitis virus, MHV, had a glycoprotein E1 glycosylated normally in the presence of tunicamycin. This indicated that E1 bore O-linked instead of N-linked glycans. The “peplomeric glycoprotein E2 was not detectable upon tunicamycin treatment,” indicating its synthesis was interdicted or its degradation was facilitated by lack of N-linked glycosylation and was improperly processed (Holmes et al. 1981). E2 may be analogous to the S-spike glycoprotein. Viral particles were produced with tunicamycin treatment but were noninfective, lacking E2, which was required for attachment to viral receptors on cells, probably analogous ACE2 by today’s knowledge. At that time, no drug was known to inhibit O-glycosylation, such as α-benzyl-GalNAc, in use today. Because of these observations, either N-linked or O-linked glycosylation interference may potentially interdict SARS-Cov2 infectivity.