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The receptor binding domain of the new Middle East respiratory syndrome coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies.

Identifieur interne : 001832 ( Main/Exploration ); précédent : 001831; suivant : 001833

The receptor binding domain of the new Middle East respiratory syndrome coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies.

Auteurs : Huihui Mou [Pays-Bas] ; V Stalin Raj ; Frank J M. Van Kuppeveld ; Peter J M. Rottier ; Bart L. Haagmans ; Berend Jan Bosch

Source :

RBID : pubmed:23785207

Descripteurs français

English descriptors

Abstract

The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor-expressing cells and soluble DPP4. Antibodies to this domain--much less so those to the preceding N-terminal region--efficiently neutralize MERS-CoV infection.

DOI: 10.1128/JVI.01277-13
PubMed: 23785207


Affiliations:


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Le document en format XML

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<term>Coronavirus (immunology)</term>
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<front>
<div type="abstract" xml:lang="en">The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor-expressing cells and soluble DPP4. Antibodies to this domain--much less so those to the preceding N-terminal region--efficiently neutralize MERS-CoV infection.</div>
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