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

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...

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Published inEmerging microbes & infections Vol. 9; no. 1; pp. 601 - 604
Main Authors Vankadari, Naveen, Wilce, Jacqueline A.
Format Journal Article
LanguageEnglish
Published London Taylor & Francis 01.01.2020
Taylor & Francis Ltd
Taylor & Francis Group
Subjects
CD26
Coronavirus
Coronaviruses
COVID-19
docking
DPP4
Glycoproteins
glycosylation
Letter
Ligands
spike glycoprotein
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Summary: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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Supplemental data for this article can be accessed https://doi.org/10.1080/22221751.2020.1739565
ISSN:2222-1751
2222-1751
DOI:10.1080/22221751.2020.1739565