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Binding of the SARS-CoV-2 Spike Protein to Glycans
Wei Hao; Bo Ma; Ziheng Li; Xiaoyu Wang; Xiaopan Gao; Yaohao Li; Bo Qin; Shiying Shang; Sheng Cui; Zhongping Tan.
Affiliation
  • Wei Hao; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Bo Ma; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Ziheng Li; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Xiaoyu Wang; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Xiaopan Gao; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Yaohao Li; University of Colorado
  • Bo Qin; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Shiying Shang; School of Pharmaceutical Sciences, Tsinghua University
  • Sheng Cui; Chinese Academy of Medical Sciences and Peking Union Medical College
  • Zhongping Tan; Chinese Academy of Medical Sciences and Peking Union Medical College
Preprint in En | PREPRINT-BIORXIV | ID: ppbiorxiv-100537
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ABSTRACT
The pandemic of 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 oligosaccharides. In this study, we examined and compared the binding of the subunits and spike (S) proteins of SARS-CoV-2 and SARS-CoV, MERS-CoV to these glycans. Our results revealed that the S proteins and subunits can bind to HS in a sulfation-dependent manner, the length of HS is not a critical factor for the binding, 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.Competing Interest StatementThe authors have declared no competing interest.View Full Text
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Full text: 1 Collection: 09-preprints Database: PREPRINT-BIORXIV Language: En Year: 2020 Document type: Preprint
Full text: 1 Collection: 09-preprints Database: PREPRINT-BIORXIV Language: En Year: 2020 Document type: Preprint