Heparan sulfates from bat and human lung and their binding to the spike protein of SARS-CoV-2 virus

Lufeng Yan, Yuefan Song, Ke Xia, Peng He, Fuming Zhang, Shiguo Chen, Robert Pouliot, Daniel J. Weiss, Ritesh Tandon, John T. Bates, Dallas R. Ederer, Dipanwita Mitra, Poonam Sharma, April Davis, Robert J. Linhardt

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) has resulted in a pandemic and continues to spread at an unprecedented rate around the world. Although a vaccine has recently been approved, there are currently few effective therapeutics to fight its associated disease in humans, COVID-19. SARS-CoV-2 and the related severe acute respiratory syndrome (SARS-CoV-1), and Middle East respiratory syndrome (MERS-CoV) result from zoonotic respiratory viruses that have bats as the primary host and an as yet unknown secondary host. While each of these viruses has different protein-based cell-surface receptors, each rely on the glycosaminoglycan, heparan sulfate as a co-receptor. In this study we compare, for the first time, differences and similarities in the structure of heparan sulfate in human and bat lungs. Furthermore, we show that the spike glycoprotein of COVID-19 binds 3.5 times stronger to human lung heparan sulfate than bat lung heparan sulfate.

Original languageEnglish
Article number117797
JournalCarbohydrate Polymers
Volume260
DOIs
StatePublished - 15 May 2021
Externally publishedYes

Keywords

  • Disaccharide composition
  • Heparan sulfate
  • Molecular weight
  • SARS-CoV-2 virus
  • Spike protein RBD

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