MersV1, PubMed, Checkpoint, bibRecord, 000C69

Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein.

Identifieur interne : 000C69 ( PubMed/Checkpoint ); précédent : 000C68; suivant : 000C70

Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein.

Auteurs : Wentao Li [Pays-Bas] ; Ruben J G. Hulswit [Pays-Bas] ; Ivy Widjaja [Pays-Bas] ; V Stalin Raj [Pays-Bas] ; Ryan Mcbride [États-Unis] ; Wenjie Peng [États-Unis] ; W. Widagdo [Pays-Bas] ; M Alejandra Tortorici [France] ; Brenda Van Dieren [Pays-Bas] ; Yifei Lang [Pays-Bas] ; Jan W M. Van Lent [Pays-Bas] ; James C. Paulson [États-Unis] ; Cornelis A M. De Haan [Pays-Bas] ; Raoul J. De Groot [Pays-Bas] ; Frank J M. Van Kuppeveld [Pays-Bas] ; Bart L. Haagmans [Pays-Bas] ; Berend-Jan Bosch [Pays-Bas]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2017.

RBID : pubmed:28923942

Descripteurs français

KwdFr :
- Acides sialiques (métabolisme), Animaux, Attachement viral, Chameaux, Coronavirus du syndrome respiratoire du Moyen-Orient (pathogénicité), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à coronavirus (métabolisme), Infections à coronavirus (virologie), Mucines, Polyosides (métabolisme), Récepteurs viraux (métabolisme).
MESH :
- génétique : Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus.
- métabolisme : Acides sialiques, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Infections à coronavirus, Polyosides, Récepteurs viraux.
- pathogénicité : Coronavirus du syndrome respiratoire du Moyen-Orient.
- virologie : Infections à coronavirus.
- Animaux, Attachement viral, Chameaux, Humains, Mucines.

English descriptors

KwdEn :
- Animals, Camelus, Coronavirus Infections (metabolism), Coronavirus Infections (virology), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Humans, Middle East Respiratory Syndrome Coronavirus (pathogenicity), Mucins, Polysaccharides (metabolism), Receptors, Virus (metabolism), Sialic Acids (metabolism), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Virus Attachment.
MESH :
- chemical , genetics : Dipeptidyl Peptidase 4, Spike Glycoprotein, Coronavirus.
- metabolism : Coronavirus Infections, Dipeptidyl Peptidase 4, Polysaccharides, Receptors, Virus, Sialic Acids, Spike Glycoprotein, Coronavirus.
- pathogenicity : Middle East Respiratory Syndrome Coronavirus.
- virology : Coronavirus Infections.
- Animals, Camelus, Humans, Mucins, Virus Attachment.

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) targets the epithelial cells of the respiratory tract both in humans and in its natural host, the dromedary camel. Virion attachment to host cells is mediated by 20-nm-long homotrimers of spike envelope protein S. The N-terminal subunit of each S protomer, called S1, folds into four distinct domains designated S1^A through S1^D Binding of MERS-CoV to the cell surface entry receptor dipeptidyl peptidase 4 (DPP4) occurs via S1^B We now demonstrate that in addition to DPP4, MERS-CoV binds to sialic acid (Sia). Initially demonstrated by hemagglutination assay with human erythrocytes and intact virus, MERS-CoV Sia-binding activity was assigned to S subdomain S1^A When multivalently displayed on nanoparticles, S1 or S1^A bound to human erythrocytes and to human mucin in a strictly Sia-dependent fashion. Glycan array analysis revealed a preference for α2,3-linked Sias over α2,6-linked Sias, which correlates with the differential distribution of α2,3-linked Sias and the predominant sites of MERS-CoV replication in the upper and lower respiratory tracts of camels and humans, respectively. Binding is hampered by Sia modifications such as 5-N-glycolylation and (7,)9-O-acetylation. Depletion of cell surface Sia by neuraminidase treatment inhibited MERS-CoV entry of Calu-3 human airway cells, thus providing direct evidence that virus-Sia interactions may aid in virion attachment. The combined observations lead us to propose that high-specificity, low-affinity attachment of MERS-CoV to sialoglycans during the preattachment or early attachment phase may form another determinant governing the host range and tissue tropism of this zoonotic pathogen.

DOI: 10.1073/pnas.1712592114
PubMed: 28923942

Affiliations:

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<author><name sortKey="Lang, Yifei" sort="Lang, Yifei" uniqKey="Lang Y" first="Yifei" last="Lang">Yifei Lang</name>
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<author><name sortKey="Van Lent, Jan W M" sort="Van Lent, Jan W M" uniqKey="Van Lent J" first="Jan W M" last="Van Lent">Jan W M. Van Lent</name>
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<affiliation wicri:level="2"><nlm:affiliation>Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
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<affiliation wicri:level="4"><nlm:affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</nlm:affiliation>
<country xml:lang="fr">Pays-Bas</country>
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<country wicri:rule="url">Pays-Bas</country>
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</affiliation>
</author>
<author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend-Jan" last="Bosch">Berend-Jan Bosch</name>
<affiliation wicri:level="4"><nlm:affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands; b.haagmans@erasmusmc.nl b.j.bosch@uu.nl.</nlm:affiliation>
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<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
<idno type="eISSN">1091-6490</idno>
<imprint><date when="2017" type="published">2017</date>
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<term>Camelus</term>
<term>Coronavirus Infections (metabolism)</term>
<term>Coronavirus Infections (virology)</term>
<term>Dipeptidyl Peptidase 4 (genetics)</term>
<term>Dipeptidyl Peptidase 4 (metabolism)</term>
<term>Humans</term>
<term>Middle East Respiratory Syndrome Coronavirus (pathogenicity)</term>
<term>Mucins</term>
<term>Polysaccharides (metabolism)</term>
<term>Receptors, Virus (metabolism)</term>
<term>Sialic Acids (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (genetics)</term>
<term>Spike Glycoprotein, Coronavirus (metabolism)</term>
<term>Virus Attachment</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides sialiques (métabolisme)</term>
<term>Animaux</term>
<term>Attachement viral</term>
<term>Chameaux</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient (pathogénicité)</term>
<term>Dipeptidyl peptidase 4 (génétique)</term>
<term>Dipeptidyl peptidase 4 (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus (génétique)</term>
<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
<term>Humains</term>
<term>Infections à coronavirus (métabolisme)</term>
<term>Infections à coronavirus (virologie)</term>
<term>Mucines</term>
<term>Polyosides (métabolisme)</term>
<term>Récepteurs viraux (métabolisme)</term>
</keywords>
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<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
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<term>Glycoprotéine de spicule des coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus Infections</term>
<term>Dipeptidyl Peptidase 4</term>
<term>Polysaccharides</term>
<term>Receptors, Virus</term>
<term>Sialic Acids</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Dipeptidyl peptidase 4</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Infections à coronavirus</term>
<term>Polyosides</term>
<term>Récepteurs viraux</term>
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</keywords>
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</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term>
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<term>Humans</term>
<term>Mucins</term>
<term>Virus Attachment</term>
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<term>Attachement viral</term>
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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) targets the epithelial cells of the respiratory tract both in humans and in its natural host, the dromedary camel. Virion attachment to host cells is mediated by 20-nm-long homotrimers of spike envelope protein S. The N-terminal subunit of each S protomer, called S1, folds into four distinct domains designated S1<sup>A</sup>
 through S1<sup>D</sup>
 Binding of MERS-CoV to the cell surface entry receptor dipeptidyl peptidase 4 (DPP4) occurs via S1<sup>B</sup>
 We now demonstrate that in addition to DPP4, MERS-CoV binds to sialic acid (Sia). Initially demonstrated by hemagglutination assay with human erythrocytes and intact virus, MERS-CoV Sia-binding activity was assigned to S subdomain S1<sup>A</sup>
 When multivalently displayed on nanoparticles, S1 or S1<sup>A</sup>
 bound to human erythrocytes and to human mucin in a strictly Sia-dependent fashion. Glycan array analysis revealed a preference for α2,3-linked Sias over α2,6-linked Sias, which correlates with the differential distribution of α2,3-linked Sias and the predominant sites of MERS-CoV replication in the upper and lower respiratory tracts of camels and humans, respectively. Binding is hampered by Sia modifications such as 5-<i>N</i>
-glycolylation and (7,)9-<i>O</i>
-acetylation. Depletion of cell surface Sia by neuraminidase treatment inhibited MERS-CoV entry of Calu-3 human airway cells, thus providing direct evidence that virus-Sia interactions may aid in virion attachment. The combined observations lead us to propose that high-specificity, low-affinity attachment of MERS-CoV to sialoglycans during the preattachment or early attachment phase may form another determinant governing the host range and tissue tropism of this zoonotic pathogen.</div>
</front>
</TEI>
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<DateCompleted><Year>2018</Year>
<Month>06</Month>
<Day>26</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>114</Volume>
<Issue>40</Issue>
<PubDate><Year>2017</Year>
<Month>10</Month>
<Day>03</Day>
</PubDate>
</JournalIssue>
<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation>
</Journal>
<ArticleTitle>Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein.</ArticleTitle>
<Pagination><MedlinePgn>E8508-E8517</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1712592114</ELocationID>
<Abstract><AbstractText>Middle East respiratory syndrome coronavirus (MERS-CoV) targets the epithelial cells of the respiratory tract both in humans and in its natural host, the dromedary camel. Virion attachment to host cells is mediated by 20-nm-long homotrimers of spike envelope protein S. The N-terminal subunit of each S protomer, called S1, folds into four distinct domains designated S1<sup>A</sup>
 through S1<sup>D</sup>
 Binding of MERS-CoV to the cell surface entry receptor dipeptidyl peptidase 4 (DPP4) occurs via S1<sup>B</sup>
 We now demonstrate that in addition to DPP4, MERS-CoV binds to sialic acid (Sia). Initially demonstrated by hemagglutination assay with human erythrocytes and intact virus, MERS-CoV Sia-binding activity was assigned to S subdomain S1<sup>A</sup>
 When multivalently displayed on nanoparticles, S1 or S1<sup>A</sup>
 bound to human erythrocytes and to human mucin in a strictly Sia-dependent fashion. Glycan array analysis revealed a preference for α2,3-linked Sias over α2,6-linked Sias, which correlates with the differential distribution of α2,3-linked Sias and the predominant sites of MERS-CoV replication in the upper and lower respiratory tracts of camels and humans, respectively. Binding is hampered by Sia modifications such as 5-<i>N</i>
-glycolylation and (7,)9-<i>O</i>
-acetylation. Depletion of cell surface Sia by neuraminidase treatment inhibited MERS-CoV entry of Calu-3 human airway cells, thus providing direct evidence that virus-Sia interactions may aid in virion attachment. The combined observations lead us to propose that high-specificity, low-affinity attachment of MERS-CoV to sialoglycans during the preattachment or early attachment phase may form another determinant governing the host range and tissue tropism of this zoonotic pathogen.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Wentao</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hulswit</LastName>
<ForeName>Ruben J G</ForeName>
<Initials>RJG</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Widjaja</LastName>
<ForeName>Ivy</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Raj</LastName>
<ForeName>V Stalin</ForeName>
<Initials>VS</Initials>
<Identifier Source="ORCID">0000-0003-2250-8481</Identifier>
<AffiliationInfo><Affiliation>Department of Viroscience, Erasmus Medical Center, 3015 CN Rotterdam, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McBride</LastName>
<ForeName>Ryan</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Peng</LastName>
<ForeName>Wenjie</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Widagdo</LastName>
<ForeName>W</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Department of Viroscience, Erasmus Medical Center, 3015 CN Rotterdam, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tortorici</LastName>
<ForeName>M Alejandra</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Institut Pasteur, Unité de Virologie Structurale, 75015 Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>CNRS UMR 3569 Virologie, 75015 Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van Dieren</LastName>
<ForeName>Brenda</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lang</LastName>
<ForeName>Yifei</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van Lent</LastName>
<ForeName>Jan W M</ForeName>
<Initials>JWM</Initials>
<AffiliationInfo><Affiliation>Laboratory of Virology, Department of Plant Sciences, Wageningen University, 6708 PB Wageningen, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Paulson</LastName>
<ForeName>James C</ForeName>
<Initials>JC</Initials>
<AffiliationInfo><Affiliation>Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>de Haan</LastName>
<ForeName>Cornelis A M</ForeName>
<Initials>CAM</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>de Groot</LastName>
<ForeName>Raoul J</ForeName>
<Initials>RJ</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van Kuppeveld</LastName>
<ForeName>Frank J M</ForeName>
<Initials>FJM</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Haagmans</LastName>
<ForeName>Bart L</ForeName>
<Initials>BL</Initials>
<AffiliationInfo><Affiliation>Department of Viroscience, Erasmus Medical Center, 3015 CN Rotterdam, The Netherlands; b.haagmans@erasmusmc.nl b.j.bosch@uu.nl.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bosch</LastName>
<ForeName>Berend-Jan</ForeName>
<Initials>BJ</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands; b.haagmans@erasmusmc.nl b.j.bosch@uu.nl.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 AI114730</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>09</Month>
<Day>18</Day>
</ArticleDate>
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<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
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<ISSNLinking>0027-8424</ISSNLinking>
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<NameOfSubstance UI="D009077">Mucins</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002162" MajorTopicYN="N">Camelus</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018819" MajorTopicYN="N">Dipeptidyl Peptidase 4</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009077" MajorTopicYN="N">Mucins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012794" MajorTopicYN="N">Sialic Acids</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053585" MajorTopicYN="N">Virus Attachment</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">MERS-CoV</Keyword>
<Keyword MajorTopicYN="Y">attachment</Keyword>
<Keyword MajorTopicYN="Y">receptor</Keyword>
<Keyword MajorTopicYN="Y">sialic acid</Keyword>
<Keyword MajorTopicYN="Y">spike</Keyword>
</KeywordList>
<CoiStatement>The authors declare no conflict of interest.</CoiStatement>
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Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein.

Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein.

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