Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Abstract

Significance The SARS-CoV-2 virus infects cells by docking the spike protein at its surface to a receptor protein exposed on human cells. Both receptor and spike are covered by sugars. With molecular dynamics simulations, we show that sugars attached to the N90 site of the human receptor interfere with binding to the virus, explaining reports of increased susceptibility to infection if N90 glycosylation is lost. By contrast, sugars at the human receptor N322 site strengthen the binding to spike by latching onto a site on spike that is targeted also by neutralizing antibodies. By characterizing the contrasting roles of sugars in the interaction between virus and host cells, we aid in the targeted development of neutralizing antibodies and SARS-CoV-2 fusion inhibitors.

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Cited by papers we hold 3

• Computational epitope map of SARS-CoV-2 spike protein · 2021
  No notice
• The flexibility of ACE2 in the context of SARS-CoV-2 infection · 2021
  No notice
• The glycosylation in SARS-CoV-2 and its receptor ACE2 · 2021
  No notice

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