Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.
Identifieur interne : 000444 ( PubMed/Corpus ); précédent : 000443; suivant : 000445Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.
Auteurs : Naveen Vankadari ; Jacqueline A. WilceSource :
- Emerging microbes & infections [ 2222-1751 ] ; 2020.
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
Links to Exploration step
pubmed:32178593Le document en format XML
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<author><name sortKey="Vankadari, Naveen" sort="Vankadari, Naveen" uniqKey="Vankadari N" first="Naveen" last="Vankadari">Naveen Vankadari</name>
<affiliation><nlm:affiliation>Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.</nlm:affiliation>
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<author><name sortKey="Wilce, Jacqueline A" sort="Wilce, Jacqueline A" uniqKey="Wilce J" first="Jacqueline A" last="Wilce">Jacqueline A. Wilce</name>
<affiliation><nlm:affiliation>Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.</nlm:affiliation>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.</title>
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<affiliation><nlm:affiliation>Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.</nlm:affiliation>
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<author><name sortKey="Wilce, Jacqueline A" sort="Wilce, Jacqueline A" uniqKey="Wilce J" first="Jacqueline A" last="Wilce">Jacqueline A. Wilce</name>
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<series><title level="j">Emerging microbes & infections</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Betacoronavirus (chemistry)</term>
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<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>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptidyl Peptidase 4</term>
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<term>Spike Glycoprotein, Coronavirus</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Betacoronavirus</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Betacoronavirus</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Spike Glycoprotein, Coronavirus</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>
</front>
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<JournalIssue CitedMedium="Internet"><Volume>9</Volume>
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<Title>Emerging microbes & infections</Title>
<ISOAbbreviation>Emerg Microbes Infect</ISOAbbreviation>
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<ArticleTitle>Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.</ArticleTitle>
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<Abstract><AbstractText>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.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vankadari</LastName>
<ForeName>Naveen</ForeName>
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<AffiliationInfo><Affiliation>Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.</Affiliation>
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<Author ValidYN="Y"><LastName>Wilce</LastName>
<ForeName>Jacqueline A</ForeName>
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<Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber>
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<Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber>
<NameOfSubstance UI="D018819">Dipeptidyl Peptidase 4</NameOfSubstance>
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<SupplMeshList><SupplMeshName Type="Organism" UI="C000656484">severe acute respiratory syndrome coronavirus 2</SupplMeshName>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000073640" MajorTopicYN="N">Betacoronavirus</DescriptorName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">CD26</Keyword>
<Keyword MajorTopicYN="Y">Coronavirus</Keyword>
<Keyword MajorTopicYN="Y">docking</Keyword>
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<Keyword MajorTopicYN="Y">spike glycoprotein</Keyword>
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