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About:
Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein
Creator
Fan, Angela
Fang, Xianyang
Hammel, Michal
Jia, Wenxu
Jiang, Liwei
Li, Yangyang
Shi, Xuanling
Wang, Dongli
Wang, Han
Wang, Pengfei
Wang, Shuying
Wang, Xinquan
Zhang, Linqi
Zhang, Senyan
Zhou, Panpan
Correspondence,
Zhang,
Linqi, Zhang
Source
Elsevier; Medline; PMC
abstract
The major mechanism of antibody-mediated neutralization of the Middle East respiratory syndrome coronavirus (MERS-CoV) involves competition with the cellular receptor dipeptidyl peptidase 4 (DPP4) for binding to the receptor-binding domain (RBD) of the spike (S) glycoprotein. Here, we report a unique epitope and unusual neutralizing mechanism of the isolated human antibody MERS-4. Structurally, MERS-4 approached the RBD from the outside of the RBD-DPP4 binding interface. Such binding resulted in the folding of the β5-β6 loop toward a shallow groove on the RBD interface critical for accommodating DPP4. The key residues for binding are identified through site-directed mutagenesis. Structural modeling revealed that MERS-4 binds to RBD only in the “up” position in the S trimer. Furthermore, MERS-4 demonstrated synergy with several reported antibodies. These results indicate that MERS-4 neutralizes MERS-CoV by indirect rather than direct competition with DPP4. This mechanism provides a valuable addition for the combined use of antibodies against MERS-CoV infection.
has issue date
2018-07-10
(
xsd:dateTime
)
bibo:doi
10.1016/j.celrep.2018.06.041
bibo:pmid
29996104
has license
no-cc
sha1sum (hex)
600075fe895d0f33445a5d6ab7c225cddae40064
schema:url
https://doi.org/10.1016/j.celrep.2018.06.041
resource representing a document's title
Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein
has PubMed Central identifier
PMC7104183
has PubMed identifier
29996104
schema:publication
Cell Rep
resource representing a document's body
covid:600075fe895d0f33445a5d6ab7c225cddae40064#body_text
is
schema:about
of
named entity 'combined'
named entity 'competition'
named entity 'antibodies'
named entity 'binding'
named entity 'folding'
named entity 'RBD'
named entity 'epitope'
named entity 'Availability'
named entity 'REPORT'
named entity 'MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS'
named entity 'GLYCOPROTEIN'
named entity 'ANTIBODY-MEDIATED NEUTRALIZATION'
named entity 'DPP4'
named entity 'PROVIDES'
named entity 'MERS-COV'
named entity 'UNIQUE'
named entity 'POSITION'
named entity 'MODELING'
named entity 'SHALLOW'
named entity 'STRUCTURAL'
named entity 'MERS'
named entity 'EPITOPE'
named entity 'KEY'
named entity 'GROOVE'
named entity 'RECEPTOR'
named entity 'BINDING'
named entity 'EPITOPE'
named entity 'MERS- COV'
named entity 'UNIQUE'
named entity 'LOOP'
named entity 'DOMAIN'
named entity 'DOMAIN'
named entity 'SOFTWARE'
named entity 'DATA'
named entity 'ARTICLE'
named entity 'STRUCTURAL'
named entity 'MERS-COV'
named entity 'CELLULAR'
named entity 'COMPETITION'
named entity 'HERE'
named entity 'UNUSUAL'
named entity 'ANTIBODIES'
named entity 'INDIRECT'
named entity 'SUMMARY'
named entity 'THESE'
named entity 'RBD'
named entity 'REVEALED'
named entity 'USE OF'
named entity 'REPORTED'
named entity 'COMBINED'
named entity 'INTERFACE'
named entity 'BINDING'
named entity 'SITE-DIRECTED MUTAGENESIS'
named entity 'ABSTRACT'
named entity 'RATHER'
named entity 'CRITICAL'
named entity 'ADDITION'
named entity 'FOLDING'
named entity 'BINDS'
named entity 'RESULTS'
named entity 'DIRECT'
named entity 'INFECTION'
named entity 'ANTIBODY'
named entity 'DIPEPTIDYL PEPTIDASE 4'
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