© 2018 American Society for Microbiology. Coronavirus spike proteins from different genera are divergent, although they all mediate coronavirus entry into cells by binding to host receptors and fusing viral and cell membranes. Here, we determined the cryo-electron microscopy structure of porcine deltacoronavirus (Pd. CoV) spike protein at 3.3-Å resolution. The trimeric protein contains three receptor-binding S1 subunits that tightly pack into a crown-like structure and three membrane fusion S2 subunits that form a stalk. Each S1 subunit contains two domains, an N-terminal domain (S1-NTD) and C-terminal domain (S1-CTD). Pd. CoV S1-NTD has the same structural fold as alphaand betacoronavirus S1-NTDs as well as host galectins, and it recognizes sugar as its potential receptor. Pd. CoV S1-CTD has the same structural fold as alphacoronavirus S1-CTDs, but its structure differs from that of betacoronavirus S1-CTDs. Pd. CoV S1- CTD binds to an unidentified receptor on host cell surfaces. Pd. CoV S2 is locked in the prefusion conformation by structural restraint of S1 from a different monomeric subunit. Pd. CoV spike possesses several structural features that may facilitate immune evasion by the virus, such as its compact structure, concealed receptorbinding sites, and shielded critical epitopes. Overall, this study reveals that deltacoronavirus spikes are structurally and evolutionally more closely related to alphacoronavirus spikes than to betacoronavirus spikes; it also has implications for the receptor recognition, membrane fusion, and immune evasion by deltacoronaviruses as well as coronaviruses in general.
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