PropertyValue
?:abstract
  • 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.
is ?:annotates of
?:creator
?:doi
?:doi
  • 10.1126/science.abd3072
?:journal
  • Science
?:license
  • cc-by
?:pmid
?:pmid
  • 33082294
?:publication_isRelatedTo_Disease
?:source
  • Medline
?:title
  • Neuropilin-1 is a host factor for SARS-CoV-2 infection.
?:type
?:year
  • 2020-10-20

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