Author: Daly, James L; Simonetti, Boris; Klein, Katja; Chen, Kai-En; Williamson, Maia Kavanagh; Antón-Plágaro, Carlos; Shoemark, Deborah K; Simón-Gracia, Lorena; Bauer, Michael; Hollandi, Reka; Greber, Urs F; Horvath, Peter; Sessions, Richard B; Helenius, Ari; Hiscox, Julian A; Teesalu, Tambet; Matthews, David A; Davidson, Andrew D; Collins, Brett M; Cullen, Peter J; Yamauchi, Yohei
Title: Neuropilin-1 is a host factor for SARS-CoV-2 infection. Cord-id: 0g4naq14 Document date: 2020_10_20
ID: 0g4naq14
Snippet: SARS-CoV-2, the causative agent of COVID-19, uses the viral Spike (S) protein for host cell attachment and entry. The host protease furin cleaves the full-length precursor S glycoprotein into two associated polypeptides: S1 and S2. Cleavage of S generates a polybasic Arg-Arg-Ala-Arg C-terminal sequence on S1, which conforms to a C-end rule (CendR) motif that binds to cell surface Neuropilin-1 (NRP1) and Neuropilin-2 (NRP2) receptors. Here, we used X-ray crystallography and biochemical approaches
Document: SARS-CoV-2, the causative agent of COVID-19, uses the viral Spike (S) protein for host cell attachment and entry. The host protease furin cleaves the full-length precursor S glycoprotein into two associated polypeptides: S1 and S2. Cleavage of S generates a polybasic Arg-Arg-Ala-Arg C-terminal sequence on S1, which conforms to a C-end rule (CendR) motif that binds to cell surface Neuropilin-1 (NRP1) and Neuropilin-2 (NRP2) receptors. Here, we used X-ray crystallography and biochemical approaches to show that the S1 CendR motif directly bound NRP1. Blocking this interaction using RNAi or selective inhibitors reduced SARS-CoV-2 entry and infectivity in cell culture. NRP1 thus serves as a host factor for SARS-CoV-2 infection and may potentially provide a therapeutic target for COVID-19.
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