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

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

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Zhang et al. report the structural and functional analysis of the potent MERS-CoV neutralizing antibody MERS-4. MERS-4 recognizes a unique epitope and indirectly disrupts interaction between the receptor binding domain and the receptor DPP4. This mechanism provides a valuable addition for the combined use of antibodies against MERS-CoV infection.

Original languageEnglish
Pages (from-to)441-452
Number of pages12
JournalCell Reports
Volume24
Issue number2
DOIs
Publication statusPublished - 2018 Jul 10

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Zhang, S., Zhou, P., Wang, P., Li, Y., Jiang, L., Jia, W., Wang, H., Fan, A., Wang, D., Shi, X., Fang, X., Hammel, M., Wang, S., Wang, X., & Zhang, L. (2018). Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein. Cell Reports, 24(2), 441-452. https://doi.org/10.1016/j.celrep.2018.06.041