Open Access
Open access
mAbs, volume 13, issue 1

501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro

Haolin Liu 1, 2
PENGCHENG WEI 1, 2
Qianqian Zhang 3
Zhongzhou Chen 3
Katja Aviszus 1, 2
Walter DOWNING 4
Shelley Peterson 4
Lyndon Reynoso 5
Gregory P. Downey 6
Stephen K. Frankel 6
Kappler John 1, 2
John W. Kappler 1, 2
Philippa C. Marrack 1, 2
Gongyi Zhang 1, 2
1
 
Department of Immunology and Microbiology, School of Medicine, Anschutz Medical Center, University of Colorado, Aurora, CO, USA
2
 
Department of Immunology and Genomic Medicine, National Jewish Health, Denver, CO, USA
4
 
Department of Nursing, National Jewish Health, Denver, CO, USA
5
 
Department of Pharmacy, National Jewish Health, Denver, CO, USA
6
 
Department of Medicine, National Jewish Health, Denver, CO, USA
Publication typeJournal Article
Publication date2021-01-01
Journal: mAbs
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor5.3
ISSN19420862, 19420870
Immunology
Immunology and Allergy
Abstract
The newly emerging variants of SARS-CoV-2 from South Africa (B.1.351/501Y.V2) and Brazil (P.1/501Y.V3) have led to a higher infection rate and reinfection of COVID-19 patients. We found that the mutations K417N, E484K, and N501Y within the receptor-binding domains (RBDs) of the virus could confer ~2-fold higher binding affinity to the human receptor, angiotensin converting enzyme 2 (ACE2), compared to the wildtype RBD. The mutated version of RBD also completely abolishes the binding of bamlanivimab, a therapeutic antibody, in vitro. Detailed analysis shows that the ~10-fold gain of binding affinity between ACE2 and Y501-RBD, which also exits in the high contagious variant B.1.1.7/501Y.V1 from the United Kingdom, is compromised by additional introduction of the K417/N/T mutation. Mutation of E484K leads to the loss of bamlanivimab binding to RBD, although this mutation does not affect the binding between RBD and ACE2.

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GOST |
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GOST Copy
Liu H. et al. 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro // mAbs. 2021. Vol. 13. No. 1.
GOST all authors (up to 50) Copy
Liu H., WEI P., Zhang Q., Chen Z., Aviszus K., DOWNING W., Peterson S., Reynoso L., Downey G., Frankel S. K., John K., Kappler J. W., Marrack P. C., Zhang G. 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro // mAbs. 2021. Vol. 13. No. 1.
RIS |
Cite this
RIS Copy
TY - JOUR
DO - 10.1080/19420862.2021.1919285
UR - https://doi.org/10.1080/19420862.2021.1919285
TI - 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro
T2 - mAbs
AU - Liu, Haolin
AU - WEI, PENGCHENG
AU - Chen, Zhongzhou
AU - Aviszus, Katja
AU - DOWNING, Walter
AU - Peterson, Shelley
AU - Reynoso, Lyndon
AU - Downey, Gregory P.
AU - Frankel, Stephen K.
AU - John, Kappler
AU - Marrack, Philippa C.
AU - Zhang, Gongyi
AU - Zhang, Qianqian
AU - Kappler, John W.
PY - 2021
DA - 2021/01/01 00:00:00
PB - Taylor & Francis
IS - 1
VL - 13
SN - 1942-0862
SN - 1942-0870
ER -
BibTex
Cite this
BibTex Copy
@article{2021_Liu,
author = {Haolin Liu and PENGCHENG WEI and Zhongzhou Chen and Katja Aviszus and Walter DOWNING and Shelley Peterson and Lyndon Reynoso and Gregory P. Downey and Stephen K. Frankel and Kappler John and Philippa C. Marrack and Gongyi Zhang and Qianqian Zhang and John W. Kappler},
title = {501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro},
journal = {mAbs},
year = {2021},
volume = {13},
publisher = {Taylor & Francis},
month = {jan},
url = {https://doi.org/10.1080/19420862.2021.1919285},
number = {1},
doi = {10.1080/19420862.2021.1919285}
}
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