These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26.