Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26

Naveen Vankadari, Jacqueline A. Wilce

Research output: Contribution to journalLetterResearchpeer-review

488 Citations (Scopus)

Abstract

The recent outbreak of pneumonia-causing COVID-19 in China is an urgent global public health issue with an increase in mortality and morbidity. Here we report our modelled homo-trimer structure of COVID-19 spike glycoprotein in both closed (ligand-free) and open (ligand-bound) conformation, which is involved in host cell adhesion. We also predict the unique N- and O-linked glycosylation sites of spike glycoprotein that distinguish it from the SARS and underlines shielding and camouflage of COVID-19 from the host the defence system. Furthermore, our study also highlights the key finding that the S1 domain of COVID-19 spike glycoprotein potentially interacts with the human CD26, a key immunoregulatory factor for hijacking and virulence. These findings accentuate the unique features of COVID-19 and assist in the development of new therapeutics.

Original languageEnglish
Pages (from-to)601-604
Number of pages4
JournalEmerging Microbes & Infections
Volume9
Issue number1
DOIs
Publication statusPublished - 17 Mar 2020

Keywords

  • CD26
  • Coronavirus
  • docking
  • glycosylation
  • spike glycoprotein

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