MersV1, PubMed, Corpus, bibRecord, 000412

Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.

Identifieur interne : 000412 ( PubMed/Corpus ); précédent : 000411; suivant : 000413

Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.

Auteurs : Nianshuang Wang ; Osnat Rosen ; Lingshu Wang ; Hannah L. Turner ; Laura J. Stevens ; Kizzmekia S. Corbett ; Charles A. Bowman ; Jesper Pallesen ; Wei Shi ; Yi Zhang ; Kwanyee Leung ; Robert N. Kirchdoerfer ; Michelle M. Becker ; Mark R. Denison ; James D. Chappell ; Andrew B. Ward ; Barney S. Graham ; Jason S. Mclellan

Source :

Cell reports [ 2211-1247 ] ; 2019.

RBID : pubmed:31553909

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) emerged into the human population in 2012 and has caused substantial morbidity and mortality. Potently neutralizing antibodies targeting the receptor-binding domain (RBD) on MERS-CoV spike (S) protein have been characterized, but much less is known about antibodies targeting non-RBD epitopes. Here, we report the structural and functional characterization of G2, a neutralizing antibody targeting the MERS-CoV S1 N-terminal domain (S1-NTD). Structures of G2 alone and in complex with the MERS-CoV S1-NTD define a site of vulnerability comprising two loops, each of which contain a residue mutated in G2-escape variants. Cell-surface binding studies and in vitro competition experiments demonstrate that G2 strongly disrupts the attachment of MERS-CoV S to its receptor, dipeptidyl peptidase-4 (DPP4), with the inhibition requiring the native trimeric S conformation. These results advance our understanding of antibody-mediated neutralization of coronaviruses and should facilitate the development of immunotherapeutics and vaccines against MERS-CoV.

DOI: 10.1016/j.celrep.2019.08.052
PubMed: 31553909

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pubmed:31553909

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<sourceDesc><biblStruct><analytic><title xml:lang="en">Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.</title>
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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="Pallesen, Jesper" sort="Pallesen, Jesper" uniqKey="Pallesen J" first="Jesper" last="Pallesen">Jesper Pallesen</name>
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<author><name sortKey="Shi, Wei" sort="Shi, Wei" uniqKey="Shi W" first="Wei" last="Shi">Wei Shi</name>
<affiliation><nlm:affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Zhang, Yi" sort="Zhang, Yi" uniqKey="Zhang Y" first="Yi" last="Zhang">Yi Zhang</name>
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<author><name sortKey="Leung, Kwanyee" sort="Leung, Kwanyee" uniqKey="Leung K" first="Kwanyee" last="Leung">Kwanyee Leung</name>
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<author><name sortKey="Kirchdoerfer, Robert N" sort="Kirchdoerfer, Robert N" uniqKey="Kirchdoerfer R" first="Robert N" last="Kirchdoerfer">Robert N. Kirchdoerfer</name>
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</affiliation>
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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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<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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<author><name sortKey="Chappell, James D" sort="Chappell, James D" uniqKey="Chappell J" first="James D" last="Chappell">James D. Chappell</name>
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<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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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) emerged into the human population in 2012 and has caused substantial morbidity and mortality. Potently neutralizing antibodies targeting the receptor-binding domain (RBD) on MERS-CoV spike (S) protein have been characterized, but much less is known about antibodies targeting non-RBD epitopes. Here, we report the structural and functional characterization of G2, a neutralizing antibody targeting the MERS-CoV S1 N-terminal domain (S1-NTD). Structures of G2 alone and in complex with the MERS-CoV S1-NTD define a site of vulnerability comprising two loops, each of which contain a residue mutated in G2-escape variants. Cell-surface binding studies and in vitro competition experiments demonstrate that G2 strongly disrupts the attachment of MERS-CoV S to its receptor, dipeptidyl peptidase-4 (DPP4), with the inhibition requiring the native trimeric S conformation. These results advance our understanding of antibody-mediated neutralization of coronaviruses and should facilitate the development of immunotherapeutics and vaccines against MERS-CoV.</div>
</front>
</TEI>
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<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>02</Day>
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<Issue>13</Issue>
<PubDate><Year>2019</Year>
<Month>Sep</Month>
<Day>24</Day>
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<Title>Cell reports</Title>
<ISOAbbreviation>Cell Rep</ISOAbbreviation>
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<ArticleTitle>Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.</ArticleTitle>
<Pagination><MedlinePgn>3395-3405.e6</MedlinePgn>
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<Abstract><AbstractText>Middle East respiratory syndrome coronavirus (MERS-CoV) emerged into the human population in 2012 and has caused substantial morbidity and mortality. Potently neutralizing antibodies targeting the receptor-binding domain (RBD) on MERS-CoV spike (S) protein have been characterized, but much less is known about antibodies targeting non-RBD epitopes. Here, we report the structural and functional characterization of G2, a neutralizing antibody targeting the MERS-CoV S1 N-terminal domain (S1-NTD). Structures of G2 alone and in complex with the MERS-CoV S1-NTD define a site of vulnerability comprising two loops, each of which contain a residue mutated in G2-escape variants. Cell-surface binding studies and in vitro competition experiments demonstrate that G2 strongly disrupts the attachment of MERS-CoV S to its receptor, dipeptidyl peptidase-4 (DPP4), with the inhibition requiring the native trimeric S conformation. These results advance our understanding of antibody-mediated neutralization of coronaviruses and should facilitate the development of immunotherapeutics and vaccines against MERS-CoV.</AbstractText>
<CopyrightInformation>Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Nianshuang</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rosen</LastName>
<ForeName>Osnat</ForeName>
<Initials>O</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Lingshu</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</Affiliation>
</AffiliationInfo>
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<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, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Stevens</LastName>
<ForeName>Laura J</ForeName>
<Initials>LJ</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Corbett</LastName>
<ForeName>Kizzmekia S</ForeName>
<Initials>KS</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bowman</LastName>
<ForeName>Charles A</ForeName>
<Initials>CA</Initials>
<AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.</Affiliation>
</AffiliationInfo>
</Author>
<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, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Wei</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Yi</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Leung</LastName>
<ForeName>Kwanyee</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</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, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Becker</LastName>
<ForeName>Michelle M</ForeName>
<Initials>MM</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Denison</LastName>
<ForeName>Mark R</ForeName>
<Initials>MR</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA; Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chappell</LastName>
<ForeName>James D</ForeName>
<Initials>JD</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.</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, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Graham</LastName>
<ForeName>Barney S</ForeName>
<Initials>BS</Initials>
<AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McLellan</LastName>
<ForeName>Jason S</ForeName>
<Initials>JS</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: jmclellan@austin.utexas.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
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<Acronym>RC</Acronym>
<Agency>CCR NIH HHS</Agency>
<Country>United States</Country>
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<Grant><GrantID>HHSN261200800001E</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
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<Grant><GrantID>R01 AI127521</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">DPP4</Keyword>
<Keyword MajorTopicYN="N">MERS-CoV</Keyword>
<Keyword MajorTopicYN="N">coronavirus</Keyword>
<Keyword MajorTopicYN="N">crystal structure</Keyword>
<Keyword MajorTopicYN="N">electron microscopy</Keyword>
<Keyword MajorTopicYN="N">membrane fusion</Keyword>
<Keyword MajorTopicYN="N">receptor-binding</Keyword>
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<Day>06</Day>
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<Month>08</Month>
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Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.

Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.

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