MersV1, Ncbi, Merge, bibRecord, 001B37

Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.

Identifieur interne : 001B37 ( Ncbi/Merge ); précédent : 001B36; suivant : 001B38

Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.

Auteurs : Jesper Pallesen [États-Unis] ; Nianshuang Wang [États-Unis] ; Kizzmekia S. Corbett [États-Unis] ; Daniel Wrapp [États-Unis] ; Robert N. Kirchdoerfer [États-Unis] ; Hannah L. Turner [États-Unis] ; Christopher A. Cottrell [États-Unis] ; Michelle M. Becker [États-Unis] ; Lingshu Wang [États-Unis] ; Wei Shi [États-Unis] ; Wing-Pui Kong [États-Unis] ; Erica L. Andres [États-Unis] ; Arminja N. Kettenbach [États-Unis] ; Mark R. Denison [États-Unis] ; James D. Chappell [États-Unis] ; Barney S. Graham [États-Unis] ; Andrew B. Ward [États-Unis] ; Jason S. Mclellan [États-Unis]

Source :

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

RBID : pubmed:28807998

Descripteurs français

English descriptors

KwdEn :
- Animals, Antibodies, Neutralizing (immunology), Antibodies, Viral (immunology), Coronaviridae (immunology), Coronavirus Infections (virology), Crystallography, X-Ray (methods), Humans, Immunity, Humoral (immunology), Immunoglobulin G (metabolism), Mice, Inbred BALB C, Middle East Respiratory Syndrome Coronavirus (immunology), Protein Binding, Protein Conformation, Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus (immunology), Structure-Activity Relationship, Vaccination, Viral Vaccines (immunology).
MESH :
- chemical , immunology : Antibodies, Neutralizing, Antibodies, Viral, Spike Glycoprotein, Coronavirus, Viral Vaccines.
- immunology : Coronaviridae, Immunity, Humoral, Middle East Respiratory Syndrome Coronavirus.
- chemical , metabolism : Immunoglobulin G, Receptors, Virus.
- methods : Crystallography, X-Ray.
- virology : Coronavirus Infections.
- Animals, Humans, Mice, Inbred BALB C, Protein Binding, Protein Conformation, Structure-Activity Relationship, Vaccination.

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.

DOI: 10.1073/pnas.1707304114
PubMed: 28807998

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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en">Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.</title>
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<author><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name>
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<author><name sortKey="Corbett, Kizzmekia S" sort="Corbett, Kizzmekia S" uniqKey="Corbett K" first="Kizzmekia S" last="Corbett">Kizzmekia S. Corbett</name>
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<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
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<author><name sortKey="Turner, Hannah L" sort="Turner, Hannah L" uniqKey="Turner H" first="Hannah L" last="Turner">Hannah L. Turner</name>
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<author><name sortKey="Becker, Michelle M" sort="Becker, Michelle M" uniqKey="Becker M" first="Michelle M" last="Becker">Michelle M. Becker</name>
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<placeName><region type="state">Tennessee</region>
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<author><name sortKey="Wang, Lingshu" sort="Wang, Lingshu" uniqKey="Wang L" first="Lingshu" last="Wang">Lingshu Wang</name>
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<author><name sortKey="Shi, Wei" sort="Shi, Wei" uniqKey="Shi W" first="Wei" last="Shi">Wei Shi</name>
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<author><name sortKey="Kong, Wing Pui" sort="Kong, Wing Pui" uniqKey="Kong W" first="Wing-Pui" last="Kong">Wing-Pui Kong</name>
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<placeName><region type="state">Maryland</region>
</placeName>
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<author><name sortKey="Andres, Erica L" sort="Andres, Erica L" uniqKey="Andres E" first="Erica L" last="Andres">Erica L. Andres</name>
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<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Tennessee</region>
</placeName>
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<author><name sortKey="Kettenbach, Arminja N" sort="Kettenbach, Arminja N" uniqKey="Kettenbach A" first="Arminja N" last="Kettenbach">Arminja N. Kettenbach</name>
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<placeName><region type="state">New Hampshire</region>
</placeName>
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</affiliation>
</author>
<author><name sortKey="Denison, Mark R" sort="Denison, Mark R" uniqKey="Denison M" first="Mark R" last="Denison">Mark R. Denison</name>
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<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Tennessee</region>
</placeName>
<wicri:cityArea>Department of Pediatrics, Vanderbilt University Medical Center, Nashville</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Chappell, James D" sort="Chappell, James D" uniqKey="Chappell J" first="James D" last="Chappell">James D. Chappell</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Tennessee</region>
</placeName>
<wicri:cityArea>Department of Pediatrics, Vanderbilt University Medical Center, Nashville</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Graham, Barney S" sort="Graham, Barney S" uniqKey="Graham B" first="Barney S" last="Graham">Barney S. Graham</name>
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<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Maryland</region>
</placeName>
<wicri:cityArea>Viral Pathogenesis Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Ward, Andrew B" sort="Ward, Andrew B" uniqKey="Ward A" first="Andrew B" last="Ward">Andrew B. Ward</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037; Nianshuang.Wang@dartmouth.edu andrew@scripps.edu Jason.S.McLellan@Dartmouth.edu.</nlm:affiliation>
<country wicri:rule="url">États-Unis</country>
<wicri:regionArea>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla</wicri:regionArea>
<wicri:noRegion>La Jolla</wicri:noRegion>
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<author><name sortKey="Mclellan, Jason S" sort="Mclellan, Jason S" uniqKey="Mclellan J" first="Jason S" last="Mclellan">Jason S. Mclellan</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755; Nianshuang.Wang@dartmouth.edu andrew@scripps.edu Jason.S.McLellan@Dartmouth.edu.</nlm:affiliation>
<country wicri:rule="url">États-Unis</country>
<wicri:regionArea>Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover</wicri:regionArea>
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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>Antibodies, Neutralizing (immunology)</term>
<term>Antibodies, Viral (immunology)</term>
<term>Coronaviridae (immunology)</term>
<term>Coronavirus Infections (virology)</term>
<term>Crystallography, X-Ray (methods)</term>
<term>Humans</term>
<term>Immunity, Humoral (immunology)</term>
<term>Immunoglobulin G (metabolism)</term>
<term>Mice, Inbred BALB C</term>
<term>Middle East Respiratory Syndrome Coronavirus (immunology)</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Receptors, Virus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (immunology)</term>
<term>Structure-Activity Relationship</term>
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<term>Viral Vaccines (immunology)</term>
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<term>Coronavirus du syndrome respiratoire du Moyen-Orient (immunologie)</term>
<term>Cristallographie aux rayons X ()</term>
<term>Glycoprotéine de spicule des coronavirus (immunologie)</term>
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<term>Vaccination</term>
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<term>Viral Vaccines</term>
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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.</div>
</front>
</TEI>
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<DateCompleted><Year>2018</Year>
<Month>06</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>02</Month>
<Day>05</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>114</Volume>
<Issue>35</Issue>
<PubDate><Year>2017</Year>
<Month>08</Month>
<Day>29</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>Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.</ArticleTitle>
<Pagination><MedlinePgn>E7348-E7357</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1707304114</ELocationID>
<Abstract><AbstractText>Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pallesen</LastName>
<ForeName>Jesper</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Nianshuang</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755; Nianshuang.Wang@dartmouth.edu andrew@scripps.edu Jason.S.McLellan@Dartmouth.edu.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Corbett</LastName>
<ForeName>Kizzmekia S</ForeName>
<Initials>KS</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wrapp</LastName>
<ForeName>Daniel</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kirchdoerfer</LastName>
<ForeName>Robert N</ForeName>
<Initials>RN</Initials>
<AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Turner</LastName>
<ForeName>Hannah L</ForeName>
<Initials>HL</Initials>
<AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cottrell</LastName>
<ForeName>Christopher A</ForeName>
<Initials>CA</Initials>
<AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Becker</LastName>
<ForeName>Michelle M</ForeName>
<Initials>MM</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Lingshu</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Virology Core, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Wei</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Virology Core, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kong</LastName>
<ForeName>Wing-Pui</ForeName>
<Initials>WP</Initials>
<AffiliationInfo><Affiliation>Virology Core, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Andres</LastName>
<ForeName>Erica L</ForeName>
<Initials>EL</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kettenbach</LastName>
<ForeName>Arminja N</ForeName>
<Initials>AN</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Norris Cotton Cancer Center, Geisel School of Medicine at Dartmouth, Lebanon, NH 03756.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Denison</LastName>
<ForeName>Mark R</ForeName>
<Initials>MR</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chappell</LastName>
<ForeName>James D</ForeName>
<Initials>JD</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Graham</LastName>
<ForeName>Barney S</ForeName>
<Initials>BS</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ward</LastName>
<ForeName>Andrew B</ForeName>
<Initials>AB</Initials>
<AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037; Nianshuang.Wang@dartmouth.edu andrew@scripps.edu Jason.S.McLellan@Dartmouth.edu.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McLellan</LastName>
<ForeName>Jason S</ForeName>
<Initials>JS</Initials>
<Identifier Source="ORCID">0000-0003-3991-542X</Identifier>
<AffiliationInfo><Affiliation>Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755; Nianshuang.Wang@dartmouth.edu andrew@scripps.edu Jason.S.McLellan@Dartmouth.edu.</Affiliation>
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<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
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<Country>United States</Country>
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<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>08</Month>
<Day>14</Day>
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<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
<NlmUniqueID>7505876</NlmUniqueID>
<ISSNLinking>0027-8424</ISSNLinking>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D057134" MajorTopicYN="N">Antibodies, Neutralizing</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
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<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
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<MeshHeading><DescriptorName UI="D003332" MajorTopicYN="N">Coronaviridae</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
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<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
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<MeshHeading><DescriptorName UI="D007074" MajorTopicYN="N">Immunoglobulin G</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D008807" MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
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<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014611" MajorTopicYN="N">Vaccination</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014765" MajorTopicYN="N">Viral Vaccines</DescriptorName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">X-ray crystallography</Keyword>
<Keyword MajorTopicYN="Y">coronavirus</Keyword>
<Keyword MajorTopicYN="Y">cryo-EM</Keyword>
<Keyword MajorTopicYN="Y">neutralizing antibody</Keyword>
<Keyword MajorTopicYN="Y">peplomer</Keyword>
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<CoiStatement>Conflict of interest statement: J.P., N.W., K.S.C., R.N.K., H.L.T., C.A.C., B.S.G., A.B.W., and J.S.M. are inventors on US patent application no. 62/412,703, entitled “Prefusion Coronavirus Spike Proteins and Their Use.” L.W., W.S., W.-P.K., and B.S.G. are inventors on US patent application no. PCT/US2016/019395, entitled “Middle East Respiratory Syndrome Coronavirus Immunogens, Antibodies and Their Use.”</CoiStatement>
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Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.

Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.

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