Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein

Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein

Antibodies that target the N-terminal domain (NTD) of the MERS-CoV spike remain poorly characterized. Here, Zhou et al. report the structural and functional analysis of the NTD-targeting mAb 7D10 and show that it synergizes with antibodies targeting the receptor-binding domain against different MERS...

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Main Authors: Haixia Zhou, Yingzhu Chen, Shuyuan Zhang, Peihua Niu, Kun Qin, Wenxu Jia, Baoying Huang, Senyan Zhang, Jun Lan, Linqi Zhang, Wenjie Tan, Xinquan Wang
Format: Article
Language:English
Published: Nature Publishing Group 2019-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-10897-4
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spelling doaj-8a133a47d4394d95889e6dc384e4b3852021-05-11T12:37:31ZengNature Publishing GroupNature Communications2041-17232019-07-0110111310.1038/s41467-019-10897-4Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoproteinHaixia Zhou0Yingzhu Chen1Shuyuan Zhang2Peihua Niu3Kun Qin4Wenxu Jia5Baoying Huang6Senyan Zhang7Jun Lan8Linqi Zhang9Wenjie Tan10Xinquan Wang11The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua UniversityKey Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDCThe Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua UniversityKey Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDCKey Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDCComprehensive AIDS Research Center, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Department of Basic Medical Sciences, School of Medicine, Tsinghua UniversityKey Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDCThe Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua UniversityThe Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua UniversityComprehensive AIDS Research Center, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Department of Basic Medical Sciences, School of Medicine, Tsinghua UniversityKey Laboratory of Medical Virology, National Health and Family Planning Commission, National Institute for Viral Disease Control and Prevention, China CDCThe Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua UniversityAntibodies that target the N-terminal domain (NTD) of the MERS-CoV spike remain poorly characterized. Here, Zhou et al. report the structural and functional analysis of the NTD-targeting mAb 7D10 and show that it synergizes with antibodies targeting the receptor-binding domain against different MERS-CoV strains.https://doi.org/10.1038/s41467-019-10897-4
collection DOAJ
language English
format Article
sources DOAJ
author Haixia Zhou
Yingzhu Chen
Shuyuan Zhang
Peihua Niu
Kun Qin
Wenxu Jia
Baoying Huang
Senyan Zhang
Jun Lan
Linqi Zhang
Wenjie Tan
Xinquan Wang
spellingShingle Haixia Zhou
Yingzhu Chen
Shuyuan Zhang
Peihua Niu
Kun Qin
Wenxu Jia
Baoying Huang
Senyan Zhang
Jun Lan
Linqi Zhang
Wenjie Tan
Xinquan Wang
Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
Nature Communications
author_facet Haixia Zhou
Yingzhu Chen
Shuyuan Zhang
Peihua Niu
Kun Qin
Wenxu Jia
Baoying Huang
Senyan Zhang
Jun Lan
Linqi Zhang
Wenjie Tan
Xinquan Wang
author_sort Haixia Zhou
title Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
title_short Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
title_full Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
title_fullStr Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
title_full_unstemmed Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
title_sort structural definition of a neutralization epitope on the n-terminal domain of mers-cov spike glycoprotein
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-07-01
description Antibodies that target the N-terminal domain (NTD) of the MERS-CoV spike remain poorly characterized. Here, Zhou et al. report the structural and functional analysis of the NTD-targeting mAb 7D10 and show that it synergizes with antibodies targeting the receptor-binding domain against different MERS-CoV strains.
url https://doi.org/10.1038/s41467-019-10897-4
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