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.
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Emerging Microbes
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1. Äڷγª¹ÙÀÌ·¯½º°¨¿°Áõ-19(Covid-19) Á¤º¸ 7
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3. Äڷγª¹ÙÀÌ·¯½º ÀüÀÚÇö¹Ì°æ ÇüÅ 11
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6. Ä¡·á¹ý(Therapeutical Method) 22
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Emerging WuHan (COVID-19) coronavirus: glycan shield and structure
prediction of spike glycoprotein and its interaction with human CD26
1. Abstract 23
2. Introduction 23
3. Acknowledgements 26
4. Disclosure statement 26
5. References 26