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mAbs

, том 13 , издание 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}

Скрыть аффилиации авторов Показать аффилиации авторов: 6 аффилиаций

Department of Immunology and Genomic Medicine, National Jewish Health, Denver, CO, USA |

Department of Immunology and Microbiology, School of Medicine, Anschutz Medical Center, University of Colorado, Aurora, CO, USA |

State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agriculture University, Beijing, People’s Republic of China |

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 |

Тип публикации: Journal Article

Дата публикации: 2021-01-01

Taylor & Francis

mAbs

scimago Q1

wos Q1

БС1

SJR: 2.699

CiteScore: 11.7

Impact factor: 7.3

ISSN: 19420862, 19420870

DOI: 10.1080/19420862.2021.1919285

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PubMed ID: 34074219

Immunology

Immunology and Allergy

Краткое описание

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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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.

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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.

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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 - Zhang, Qianqian

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 - Kappler, John W.

AU - Marrack, Philippa C.

AU - Zhang, Gongyi

PY - 2021

DA - 2021/01/01

PB - Taylor & Francis

IS - 1

VL - 13

PMID - 34074219

SN - 1942-0862

SN - 1942-0870

ER -

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@article{2021_Liu,

author = {Haolin Liu and PENGCHENG WEI and Qianqian Zhang 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 John W. Kappler and Philippa C. Marrack and Gongyi Zhang},

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}

}

Издатель

Taylor & Francis

Журнал

mAbs

scimago Q1

wos Q1

БС1

SJR

2.699

CiteScore

11.7

Impact factor

7.3

ISSN

19420862 (Print)

19420870 (Electronic)