Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody
Abstract
The MERS-CoV is an emerging virus, which already infected more than 1,300 humans with high (~36%) mortality. Here, we show that m336, an exceptionally potent human anti-MERS-CoV antibody, is almost germline with only one somatic mutation in the heavy chain. The structure of Fab m336 in complex with the MERS-CoV receptor-binding domain reveals that its IGHV1-69-derived heavy chain provides more than 85% binding surface and that its epitope almost completely overlaps with the receptor-binding site. Analysis of antibodies from 69 healthy humans suggests an important role of the V(D)J recombination-generated junctional and allele-specific residues for achieving high affinity of binding at such low levels of somatic hypermutation. Our results also have important implications for development of vaccine immunogens based on the newly identified m336 epitope as well as for elucidation of mechanisms of neutralization by m336-like antibodies and their elicitation in vivo.
- Authors:
-
- Fudan Univ., Shanghai (China). Shanghai Medical College
- National Inst. of Health (NIH), Frederick, MD (United States). National Cancer Inst.
- New York Blood Center, New York, NY (United States). Lindsley F. Kimball Research Inst.
- National Inst. of Health (NIH), Bethesda, MD (United States). National Inst. of Allergy and Infectious Diseases
- Fudan Univ., Shanghai (China). Shanghai Medical College; National Inst. of Health (NIH), Frederick, MD (United States). National Cancer Inst.
- Fudan Univ., Shanghai (China). Shanghai Medical College; New York Blood Center, New York, NY (United States). Lindsley F. Kimball Research Inst.
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1214653
- Grant/Contract Number:
- W-31-109-ENG-38
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 6; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES
Citation Formats
Ying, Tianlei, Prabakaran, Ponraj, Du, Lanying, Shi, Wei, Feng, Yang, Wang, Yanping, Wang, Lingshu, Li, Wei, Jiang, Shibo, Dimitrov, Dimiter S., and Zhou, Tongqing. Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. United States: N. p., 2015.
Web. doi:10.1038/ncomms9223.
Ying, Tianlei, Prabakaran, Ponraj, Du, Lanying, Shi, Wei, Feng, Yang, Wang, Yanping, Wang, Lingshu, Li, Wei, Jiang, Shibo, Dimitrov, Dimiter S., & Zhou, Tongqing. Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. United States. https://doi.org/10.1038/ncomms9223
Ying, Tianlei, Prabakaran, Ponraj, Du, Lanying, Shi, Wei, Feng, Yang, Wang, Yanping, Wang, Lingshu, Li, Wei, Jiang, Shibo, Dimitrov, Dimiter S., and Zhou, Tongqing. Tue .
"Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody". United States. https://doi.org/10.1038/ncomms9223. https://www.osti.gov/servlets/purl/1214653.
@article{osti_1214653,
title = {Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody},
author = {Ying, Tianlei and Prabakaran, Ponraj and Du, Lanying and Shi, Wei and Feng, Yang and Wang, Yanping and Wang, Lingshu and Li, Wei and Jiang, Shibo and Dimitrov, Dimiter S. and Zhou, Tongqing},
abstractNote = {The MERS-CoV is an emerging virus, which already infected more than 1,300 humans with high (~36%) mortality. Here, we show that m336, an exceptionally potent human anti-MERS-CoV antibody, is almost germline with only one somatic mutation in the heavy chain. The structure of Fab m336 in complex with the MERS-CoV receptor-binding domain reveals that its IGHV1-69-derived heavy chain provides more than 85% binding surface and that its epitope almost completely overlaps with the receptor-binding site. Analysis of antibodies from 69 healthy humans suggests an important role of the V(D)J recombination-generated junctional and allele-specific residues for achieving high affinity of binding at such low levels of somatic hypermutation. Our results also have important implications for development of vaccine immunogens based on the newly identified m336 epitope as well as for elucidation of mechanisms of neutralization by m336-like antibodies and their elicitation in vivo.},
doi = {10.1038/ncomms9223},
journal = {Nature Communications},
number = ,
volume = 6,
place = {United States},
year = {Tue Sep 15 00:00:00 EDT 2015},
month = {Tue Sep 15 00:00:00 EDT 2015}
}
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journal, November 2016
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Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains
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Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
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Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
journal, July 2019
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Development of a Phage Display Panning Strategy Utilizing Crude Antigens: Isolation of MERS-CoV Nucleoprotein human antibodies
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Passive Transfer of A Germline-like Neutralizing Human Monoclonal Antibody Protects Transgenic Mice Against Lethal Middle East Respiratory Syndrome Coronavirus Infection
journal, August 2016
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Update on therapeutic options for Middle East Respiratory Syndrome Coronavirus (MERS-CoV)
journal, December 2016
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Antibodies and vaccines against Middle East respiratory syndrome coronavirus
journal, January 2019
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Ultrapotent Human Neutralizing Antibody Repertoires Against Middle East Respiratory Syndrome Coronavirus From a Recovered Patient
journal, May 2018
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Characterization and bioactivity of self-assembled anti-angiogenic chondroitin sulphate-ES2-AF nanoparticle conjugate
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Toward Developing a Preventive MERS-CoV Vaccine—Report from a Workshop Organized by the Saudi Arabia Ministry of Health and the International Vaccine Institute, Riyadh, Saudi Arabia, November 14–15, 2015
journal, August 2016
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Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
journal, November 2019
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A Human DPP4-Knockin Mouse’s Susceptibility to Infection by Authentic and Pseudotyped MERS-CoV
journal, August 2018
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Combining a Fusion Inhibitory Peptide Targeting the MERS-CoV S2 Protein HR1 Domain and a Neutralizing Antibody Specific for the S1 Protein Receptor-Binding Domain (RBD) Showed Potent Synergism against Pseudotyped MERS-CoV with or without Mutations in RBD
journal, January 2019
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Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
journal, January 2019
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Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody
text, January 2020
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