Binding of the SARS-CoV-2 spike protein to glycans

The pandemic of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a high number of deaths in the world. To combat it, it is necessary to develop a better understanding of how the virus infects host cells. Infection normally starts with the attachment of the virus to cell-surface glycans like heparan sulfate (HS) and sialic acid-containing glycolipids/glycoproteins. In this study, we examined and compared the binding of the subunits and spike (S) proteins of SARS-CoV-2, SARS-CoV, and Middle East respiratory disease (MERS)-CoV to these glycans. Our results revealed that the S proteins and subunits can bind to HS in a sulfation-dependent manner and no binding with sialic acid residues was detected. Overall, this work suggests that HS binding may be a general mechanism for the attachment of these coronaviruses to host cells, and supports the potential importance of HS in infection and in the development of antiviral agents against these viruses. (c) 2021 Science China Press. Published by Elsevier B.V. and Science China Press. All rights reserved.

Automated summary

The study found that the spike proteins and subunits of SARS-CoV-2, SARS-CoV, and MERS-CoV can bind to heparan sulfate (HS) in a sulfation-dependent manner, with no binding to sialic acid residues detected. This suggests that HS binding may be a general mechanism for these coronaviruses to attach to host cells.