Author: Gao, Chao; Zeng, Junwei; Jia, Nan; Stavenhagen, Kathrin; Matsumoto, Yasuyuki; Zhang, Hua; Li, Jiang; Hume, Adam J.; Mühlberger, Elke; van Die, Irma; Kwan, Julian; Tantisira, Kelan; Emili, Andrew; Cummings, Richard D.
Title: SARS-CoV-2 Spike Protein Interacts with Multiple Innate Immune Receptors Cord-id: mfjb49pa Document date: 2020_7_30
ID: mfjb49pa
Snippet: 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
Document: 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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