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Article

Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.

Cell reports - 10 Jul 2018

Zhang Senyan, Zhou Panpan, Wang Pengfei, Li Yangyang, Jiang Liwei, Jia Wenxu, Wang Han, Fan Angela, Wang Dongli, Shi Xuanling, Fang Xianyang, Hammel Michal, Wang Shuying, Wang Xinquan, Zhang Linqi

Abstract excerpt

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...

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Share to Antibodies, Neutralizing
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Middle East Respiratory Syndrome Coronavirus

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Share to Spike Glycoprotein, Coronavirus

Source

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Identifiers

PMID: 29996104
DOI: 10.1016/j.celrep.2018.06.041
PMCID: PMC7104183

Genes

DPP4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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