Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.
Identifieur interne : 000412 ( PubMed/Corpus ); précédent : 000411; suivant : 000413Structural 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. MclellanSource :
- Cell reports [ 2211-1247 ] ; 2019.
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:31553909Le document en format XML
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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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<Title>Cell reports</Title>
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<ArticleTitle>Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD.</ArticleTitle>
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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>
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<ForeName>Nianshuang</ForeName>
<Initials>N</Initials>
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</AffiliationInfo>
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<Keyword MajorTopicYN="N">crystal structure</Keyword>
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