SARS-CoV-2 Spike Protein Interacts with Multiple Innate Immune Receptors
Gao, C.; Zeng, J.; Jia, N.; Stavenhagen, K.; Matsumoto, Y.; Zhang, H.; Li, J.; Hume, A. J.; Muehlberger, E.; van Die, I.; Kwan, J.; Tantisira, K.; Emili, A.; Cummings, R. D.
Show abstract
The spike (S) glycoprotein in the envelope of SARS-CoV-2 is densely glycosylated but the functions of its glycosylation are unknown. Here we demonstrate that S is recognized in a glycan-dependent manner by multiple innate immune receptors including the mannose receptor MR/CD206, DC-SIGN/CD209, L-SIGN/CD209L, and MGL/CLEC10A/CD301. Single-cell RNA sequencing analyses indicate that such receptors are highly expressed in innate immune cells in tissues susceptible to SARS-CoV-2 infection. Binding of the above receptors to S is characterized by affinities in the picomolar range and consistent with S glycosylation analysis demonstrating a variety of N- and O-glycans as receptor ligands. These results indicate multiple routes for SARS-CoV-2 to interact with human cells and suggest alternative strategies for therapeutic intervention.
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