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,< Jacqueline A. Wilce> Àú | ¾ÆÁø

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2020-07-12
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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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Á¦ 1Æí Äڷγª¹ÙÀÌ·¯½º Á¤ÀÇ
1. Äڷγª¹ÙÀÌ·¯½º°¨¿°Áõ-19(Covid-19) Á¤º¸ 7
2. Äڷγª¹ÙÀÌ·¯½º ºÐ·ù ¹× Ư¼º 9
3. Äڷγª¹ÙÀÌ·¯½º ÀüÀÚÇö¹Ì°æ ÇüÅ 11
4. Äڷγª¹ÙÀÌ·¯½º ±¸Á¶ (Covid-19 Organization) 13
5. Äڷγª19: ȯ°æ¿¡ Áö¼ÓÀûÀÎ ¿µÇâÀ» ¹ÌÄ¥±î? 19
6. Ä¡·á¹ý(Therapeutical Method) 22

Á¦ 2Æí ¿¬±¸³í¹®
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