Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.
Naveen VankadariJacqueline A WilcePublished in: Emerging microbes & infections (2020)
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.
Keyphrases
- coronavirus disease
- sars cov
- public health
- respiratory syndrome coronavirus
- endothelial cells
- cell adhesion
- escherichia coli
- pseudomonas aeruginosa
- staphylococcus aureus
- small molecule
- coronary artery disease
- acute respiratory distress syndrome
- binding protein
- extracorporeal membrane oxygenation
- biofilm formation