Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.
Identifieur interne : 000682 ( 2020/Analysis ); précédent : 000681; suivant : 000683Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.
Auteurs : Naveen Vankadari [Australie] ; Jacqueline A. Wilce [Australie]Source :
- Emerging microbes & infections [ 2222-1751 ] ; 2020.
Descripteurs français
- KwdFr :
- Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (métabolisme), Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à coronavirus (virologie), Liaison aux protéines, Modèles moléculaires, Pandémies, Pneumopathie virale (virologie), Polyosides (), Polyosides (métabolisme), Structure quaternaire des protéines.
- MESH :
- génétique : Glycoprotéine de spicule des coronavirus.
- métabolisme : Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Polyosides.
- virologie : Infections à coronavirus, Pneumopathie virale.
- Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Modèles moléculaires, Pandémies, Polyosides, Structure quaternaire des protéines.
English descriptors
- KwdEn :
- Betacoronavirus (chemistry), Betacoronavirus (genetics), Betacoronavirus (metabolism), Coronavirus Infections (virology), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (metabolism), Humans, Models, Molecular, Pandemics, Pneumonia, Viral (virology), Polysaccharides (chemistry), Polysaccharides (metabolism), Protein Binding, Protein Structure, Quaternary, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism).
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Polysaccharides, Spike Glycoprotein, Coronavirus.
- chemistry : Betacoronavirus.
- genetics : Betacoronavirus, Spike Glycoprotein, Coronavirus.
- metabolism : Betacoronavirus, Dipeptidyl Peptidase 4, Polysaccharides, Spike Glycoprotein, Coronavirus.
- virology : Coronavirus Infections, Pneumonia, Viral.
- Humans, Models, Molecular, Pandemics, Protein Binding, Protein Structure, Quaternary.
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.
DOI: 10.1080/22221751.2020.1739565
PubMed: 32178593
Affiliations:
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pubmed:32178593Le document en format XML
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<term>Dipeptidyl Peptidase 4 (chemistry)</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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