Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.
Identifieur interne : 000414 ( new/Analysis ); précédent : 000413; suivant : 000415Emerging 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, Liaison aux protéines, Modèles moléculaires, Polyosides (), Polyosides (métabolisme), Structure quaternaire des protéines.
- MESH :
- génétique : Glycoprotéine de spicule des coronavirus.
- métabolisme : Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Polyosides.
- Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Modèles moléculaires, Polyosides, Structure quaternaire des protéines.
English descriptors
- KwdEn :
- Betacoronavirus (chemistry), Betacoronavirus (genetics), Betacoronavirus (metabolism), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (metabolism), Humans, Models, Molecular, 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.
- Humans, Models, Molecular, 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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Wilce</name><affiliation wicri:level="1"><nlm:affiliation>Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton</wicri:regionArea><wicri:noRegion>Clayton</wicri:noRegion></affiliation></author></analytic><series><title level="j">Emerging microbes & infections</title><idno type="eISSN">2222-1751</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Betacoronavirus (chemistry)</term><term>Betacoronavirus (genetics)</term><term>Betacoronavirus (metabolism)</term><term>Dipeptidyl Peptidase 4 (chemistry)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Humans</term><term>Models, Molecular</term><term>Polysaccharides (chemistry)</term><term>Polysaccharides (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Quaternary</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Dipeptidyl peptidase 4 ()</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (génétique)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Polyosides ()</term><term>Polyosides (métabolisme)</term><term>Structure quaternaire des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Polysaccharides</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Betacoronavirus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Betacoronavirus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Betacoronavirus</term><term>Dipeptidyl Peptidase 4</term><term>Polysaccharides</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dipeptidyl peptidase 4</term><term>Glycoprotéine de spicule des coronavirus</term><term>Polyosides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Structure, Quaternary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dipeptidyl peptidase 4</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Polyosides</term><term>Structure quaternaire des protéines</term></keywords></textClass></profileDesc></teiHeader><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. 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