Nature Microbiology, volume 6, issue 10, pages 1233-1244
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Jinhui Dong
1
,
Seth J. Zost
1
,
Allison J Greaney
2, 3
,
Tyler N Starr
3
,
Adam S Dingens
3
,
Elaine C. Chen
4
,
Rita E. Chen
5, 6
,
James B. Case
5
,
Rachel E. Sutton
1
,
Pavlo Gilchuk
1
,
Jessica Rodriguez
1
,
Erica Armstrong
1
,
Christopher Gainza
1
,
Rachel S. Nargi
1
,
Elad Binshtein
1
,
Xuping Xie
7
,
Xianwen Zhang
7
,
Pei Shi
7
,
James Logue
8
,
Stuart Weston
8
,
Marisa McGrath
8
,
Matthew Frieman
8
,
Tyler Brady
9
,
Kevin M Tuffy
9
,
Helen Bright
9
,
Yueh-Ming Loo
9
,
Patrick M Mctamney
9
,
Mark T Esser
9
,
Robert H. Carnahan
1, 10
,
Michael S. Diamond
5, 6, 11, 12
,
Jesse D Bloom
2, 3, 13
,
James Crowe
1, 4, 10
6
7
Department of Biochemistry & Molecular Biology, The University of Texas Medical Branch at Galveston, Galveston, USA
|
9
Microbial Sciences, AstraZeneca, Gaithersburg, USA
|
Publication type: Journal Article
Publication date: 2021-09-21
Cell Biology
Genetics
Microbiology (medical)
Microbiology
Applied Microbiology and Biotechnology
Immunology
Abstract
Understanding the molecular basis for immune recognition of SARS-CoV-2 spike glycoprotein antigenic sites will inform the development of improved therapeutics. We determined the structures of two human monoclonal antibodies–AZD8895 and AZD1061–which form the basis of the investigational antibody cocktail AZD7442, in complex with the receptor-binding domain (RBD) of SARS-CoV-2 to define the genetic and structural basis of neutralization. AZD8895 forms an ‘aromatic cage’ at the heavy/light chain interface using germ line-encoded residues in complementarity-determining regions (CDRs) 2 and 3 of the heavy chain and CDRs 1 and 3 of the light chain. These structural features explain why highly similar antibodies (public clonotypes) have been isolated from multiple individuals. AZD1061 has an unusually long LCDR1; the HCDR3 makes interactions with the opposite face of the RBD from that of AZD8895. Using deep mutational scanning and neutralization escape selection experiments, we comprehensively mapped the crucial binding residues of both antibodies and identified positions of concern with regards to virus escape from antibody-mediated neutralization. Both AZD8895 and AZD1061 have strong neutralizing activity against SARS-CoV-2 and variants of concern with antigenic substitutions in the RBD. We conclude that germ line-encoded antibody features enable recognition of the SARS-CoV-2 spike RBD and demonstrate the utility of the cocktail AZD7442 in neutralizing emerging variant viruses. Structural analysis of two human monoclonal antibodies that conform the antibody cocktail AZD7442, in complex with the RBD of SARS-CoV-2, reveal strong neutralization of SARS-CoV-2 variants of concern.
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Citations by publishers
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Cold Spring Harbor Laboratory
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47 publications, 20.52%
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Wiley
6 publications, 2.62%
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5 publications, 2.18%
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4 publications, 1.75%
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NEJM Group
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- We do not take into account publications without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Dong J. et al. Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail // Nature Microbiology. 2021. Vol. 6. No. 10. pp. 1233-1244.
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Dong J., Zost S. J., Greaney A. J., Starr T. N., Dingens A. S., Chen E. C., Chen R. E., Case J. B., Sutton R. E., Gilchuk P., Rodriguez J., Armstrong E., Gainza C., Nargi R. S., Binshtein E., Xie X., Zhang X., Shi P., Logue J., Weston S., McGrath M., Frieman M., Brady T., Tuffy K. M., Bright H., Loo Y., Mctamney P. M., Esser M. T., Carnahan R. H., Diamond M. S., Bloom J. D., Crowe J. Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail // Nature Microbiology. 2021. Vol. 6. No. 10. pp. 1233-1244.
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TY - JOUR
DO - 10.1038/s41564-021-00972-2
UR - https://doi.org/10.1038/s41564-021-00972-2
TI - Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
T2 - Nature Microbiology
AU - Dong, Jinhui
AU - Zost, Seth J.
AU - Greaney, Allison J
AU - Starr, Tyler N
AU - Dingens, Adam S
AU - Chen, Elaine C.
AU - Chen, Rita E.
AU - Case, James B.
AU - Sutton, Rachel E.
AU - Gilchuk, Pavlo
AU - Rodriguez, Jessica
AU - Armstrong, Erica
AU - Gainza, Christopher
AU - Nargi, Rachel S.
AU - Binshtein, Elad
AU - Xie, Xuping
AU - Zhang, Xianwen
AU - Shi, Pei
AU - Logue, James
AU - Weston, Stuart
AU - McGrath, Marisa
AU - Frieman, Matthew
AU - Brady, Tyler
AU - Tuffy, Kevin M
AU - Bright, Helen
AU - Loo, Yueh-Ming
AU - Mctamney, Patrick M
AU - Esser, Mark T
AU - Carnahan, Robert H.
AU - Diamond, Michael S.
AU - Bloom, Jesse D
AU - Crowe, James
PY - 2021
DA - 2021/09/21 00:00:00
PB - Springer Nature
SP - 1233-1244
IS - 10
VL - 6
SN - 2058-5276
ER -
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@article{2021_Dong,
author = {Jinhui Dong and Seth J. Zost and Allison J Greaney and Tyler N Starr and Adam S Dingens and Elaine C. Chen and Rita E. Chen and James B. Case and Rachel E. Sutton and Pavlo Gilchuk and Jessica Rodriguez and Erica Armstrong and Christopher Gainza and Rachel S. Nargi and Elad Binshtein and Xuping Xie and Xianwen Zhang and Pei Shi and James Logue and Stuart Weston and Marisa McGrath and Matthew Frieman and Tyler Brady and Kevin M Tuffy and Helen Bright and Yueh-Ming Loo and Patrick M Mctamney and Mark T Esser and Robert H. Carnahan and Michael S. Diamond and Jesse D Bloom and James Crowe},
title = {Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail},
journal = {Nature Microbiology},
year = {2021},
volume = {6},
publisher = {Springer Nature},
month = {sep},
url = {https://doi.org/10.1038/s41564-021-00972-2},
number = {10},
pages = {1233--1244},
doi = {10.1038/s41564-021-00972-2}
}
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Dong, Jinhui, et al. “Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail.” Nature Microbiology, vol. 6, no. 10, Sep. 2021, pp. 1233-1244. https://doi.org/10.1038/s41564-021-00972-2.