MersV1, PubMed, Curation, bibRecord, 000485

Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein.

Identifieur interne : 000485 ( PubMed/Curation ); précédent : 000484; suivant : 000486

Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein.

Source :

Nature communications [ 2041-1723 ] ; 2019.

RBID : pubmed:31296843

Descripteurs français

English descriptors

KwdEn :
- Animals, Antibodies, Neutralizing (blood), Antibodies, Neutralizing (immunology), Antibodies, Neutralizing (metabolism), Antibodies, Neutralizing (ultrastructure), Antibodies, Viral (blood), Antibodies, Viral (immunology), Antibodies, Viral (metabolism), Antibodies, Viral (ultrastructure), Cell Line, Tumor, Chlorocebus aethiops, Coronavirus Infections (blood), Coronavirus Infections (immunology), Coronavirus Infections (virology), Crystallography, X-Ray, Dipeptidyl Peptidase 4 (metabolism), Disease Models, Animal, Epitope Mapping, Epitopes (immunology), Female, HEK293 Cells, Humans, Mice, Middle East Respiratory Syndrome Coronavirus (immunology), Middle East Respiratory Syndrome Coronavirus (metabolism), Neutralization Tests, Protein Binding (immunology), Protein Domains (immunology), Recombinant Proteins (immunology), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Recombinant Proteins (ultrastructure), Spike Glycoprotein, Coronavirus (immunology), Spike Glycoprotein, Coronavirus (isolation & purification), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure), Vero Cells, Virus Internalization.
MESH :
- chemical , blood : Antibodies, Neutralizing, Antibodies, Viral.
- chemical , immunology : Antibodies, Neutralizing, Antibodies, Viral, Epitopes, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , isolation & purification : Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Antibodies, Neutralizing, Antibodies, Viral, Dipeptidyl Peptidase 4, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , ultrastructure : Antibodies, Neutralizing, Antibodies, Viral, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- blood : Coronavirus Infections.
- immunology : Coronavirus Infections, Middle East Respiratory Syndrome Coronavirus, Protein Binding, Protein Domains.
- metabolism : Middle East Respiratory Syndrome Coronavirus.
- virology : Coronavirus Infections.
- Animals, Cell Line, Tumor, Chlorocebus aethiops, Crystallography, X-Ray, Disease Models, Animal, Epitope Mapping, Female, HEK293 Cells, Humans, Mice, Neutralization Tests, Vero Cells, Virus Internalization.

Abstract

Most neutralizing antibodies against Middle East respiratory syndrome coronavirus (MERS-CoV) target the receptor-binding domain (RBD) of the spike glycoprotein and block its binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). The epitopes and mechanisms of mAbs targeting non-RBD regions have not been well characterized yet. Here we report the monoclonal antibody 7D10 that binds to the N-terminal domain (NTD) of the spike glycoprotein and inhibits the cell entry of MERS-CoV with high potency. Structure determination and mutagenesis experiments reveal the epitope and critical residues on the NTD for 7D10 binding and neutralization. Further experiments indicate that the neutralization by 7D10 is not solely dependent on the inhibition of DPP4 binding, but also acts after viral cell attachment, inhibiting the pre-fusion to post-fusion conformational change of the spike. These properties give 7D10 a wide neutralization breadth and help explain its synergistic effects with several RBD-targeting antibodies.

DOI: 10.1038/s41467-019-10897-4
PubMed: 31296843

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<author><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name>
<affiliation wicri:level="1"><nlm:affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, 100084, Beijing, China. xinquanwang@mail.tsinghua.edu.cn.</nlm:affiliation>
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<term>Antibodies, Neutralizing (metabolism)</term>
<term>Antibodies, Neutralizing (ultrastructure)</term>
<term>Antibodies, Viral (blood)</term>
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<term>Coronavirus Infections (immunology)</term>
<term>Coronavirus Infections (virology)</term>
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<term>Glycoprotéine de spicule des coronavirus (isolement et purification)</term>
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<term>Glycoprotéine de spicule des coronavirus (ultrastructure)</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Infections à coronavirus</term>
<term>Liaison aux protéines</term>
<term>Protéines recombinantes</term>
<term>Épitopes</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Coronavirus Infections</term>
<term>Middle East Respiratory Syndrome Coronavirus</term>
<term>Protein Binding</term>
<term>Protein Domains</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Anticorps antiviraux</term>
<term>Anticorps neutralisants</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Dipeptidyl peptidase 4</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Anticorps antiviraux</term>
<term>Anticorps neutralisants</term>
<term>Infections à coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Anticorps antiviraux</term>
<term>Anticorps neutralisants</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line, Tumor</term>
<term>Chlorocebus aethiops</term>
<term>Crystallography, X-Ray</term>
<term>Disease Models, Animal</term>
<term>Epitope Mapping</term>
<term>Female</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Mice</term>
<term>Neutralization Tests</term>
<term>Vero Cells</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cartographie épitopique</term>
<term>Cellules HEK293</term>
<term>Cellules Vero</term>
<term>Cristallographie aux rayons X</term>
<term>Femelle</term>
<term>Humains</term>
<term>Lignée cellulaire tumorale</term>
<term>Modèles animaux de maladie humaine</term>
<term>Pénétration virale</term>
<term>Souris</term>
<term>Tests de neutralisation</term>
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<front><div type="abstract" xml:lang="en">Most neutralizing antibodies against Middle East respiratory syndrome coronavirus (MERS-CoV) target the receptor-binding domain (RBD) of the spike glycoprotein and block its binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). The epitopes and mechanisms of mAbs targeting non-RBD regions have not been well characterized yet. Here we report the monoclonal antibody 7D10 that binds to the N-terminal domain (NTD) of the spike glycoprotein and inhibits the cell entry of MERS-CoV with high potency. Structure determination and mutagenesis experiments reveal the epitope and critical residues on the NTD for 7D10 binding and neutralization. Further experiments indicate that the neutralization by 7D10 is not solely dependent on the inhibition of DPP4 binding, but also acts after viral cell attachment, inhibiting the pre-fusion to post-fusion conformational change of the spike. These properties give 7D10 a wide neutralization breadth and help explain its synergistic effects with several RBD-targeting antibodies.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31296843</PMID>
<DateCompleted><Year>2019</Year>
<Month>10</Month>
<Day>25</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>10</Volume>
<Issue>1</Issue>
<PubDate><Year>2019</Year>
<Month>07</Month>
<Day>11</Day>
</PubDate>
</JournalIssue>
<Title>Nature communications</Title>
<ISOAbbreviation>Nat Commun</ISOAbbreviation>
</Journal>
<ArticleTitle>Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein.</ArticleTitle>
<Pagination><MedlinePgn>3068</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41467-019-10897-4</ELocationID>
<Abstract><AbstractText>Most neutralizing antibodies against Middle East respiratory syndrome coronavirus (MERS-CoV) target the receptor-binding domain (RBD) of the spike glycoprotein and block its binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). The epitopes and mechanisms of mAbs targeting non-RBD regions have not been well characterized yet. Here we report the monoclonal antibody 7D10 that binds to the N-terminal domain (NTD) of the spike glycoprotein and inhibits the cell entry of MERS-CoV with high potency. Structure determination and mutagenesis experiments reveal the epitope and critical residues on the NTD for 7D10 binding and neutralization. Further experiments indicate that the neutralization by 7D10 is not solely dependent on the inhibition of DPP4 binding, but also acts after viral cell attachment, inhibiting the pre-fusion to post-fusion conformational change of the spike. These properties give 7D10 a wide neutralization breadth and help explain its synergistic effects with several RBD-targeting antibodies.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Haixia</ForeName>
<Initials>H</Initials>
<Identifier Source="ORCID">0000-0002-9676-6267</Identifier>
<AffiliationInfo><Affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, 100084, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Yingzhu</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDC, 102206, Beijing, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Clinical Laboratory, Peking University Cancer Hospital & Institute, 100142, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Shuyuan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, 100084, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Niu</LastName>
<ForeName>Peihua</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDC, 102206, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qin</LastName>
<ForeName>Kun</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDC, 102206, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jia</LastName>
<ForeName>Wenxu</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Comprehensive AIDS Research Center, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, 100084, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Huang</LastName>
<ForeName>Baoying</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDC, 102206, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Senyan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, 100084, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lan</LastName>
<ForeName>Jun</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, 100084, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Linqi</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Comprehensive AIDS Research Center, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, 100084, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tan</LastName>
<ForeName>Wenjie</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDC, 102206, Beijing, China. tanwj28@163.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Xinquan</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, 100084, Beijing, China. xinquanwang@mail.tsinghua.edu.cn.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Collaborative Innovation Center for Biotherapy, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, West China Medical School, Sichuan University, 610065, Chengdu, China. xinquanwang@mail.tsinghua.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>07</Month>
<Day>11</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nat Commun</MedlineTA>
<NlmUniqueID>101528555</NlmUniqueID>
<ISSNLinking>2041-1723</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D057134">Antibodies, Neutralizing</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000939">Epitopes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber>
<NameOfSubstance UI="C042807">DPP4 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber>
<NameOfSubstance UI="D018819">Dipeptidyl Peptidase 4</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057134" MajorTopicYN="N">Antibodies, Neutralizing</DescriptorName>
<QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName>
<QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName>
<QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018819" MajorTopicYN="N">Dipeptidyl Peptidase 4</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018604" MajorTopicYN="N">Epitope Mapping</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009500" MajorTopicYN="N">Neutralization Tests</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year>
<Month>12</Month>
<Day>10</Day>
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<PubMedPubDate PubStatus="accepted"><Year>2019</Year>
<Month>06</Month>
<Day>05</Day>
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Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein.

Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein.

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