501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro
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...
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Taylor & Francis Group,
2021-01-01T00:00:00Z.
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001 | doaj_8fedadc2ee61424d849e04c78d26f524 | ||
042 | |a dc | ||
100 | 1 | 0 | |a Haolin Liu |e author |
700 | 1 | 0 | |a Pengcheng Wei |e author |
700 | 1 | 0 | |a Qianqian Zhang |e author |
700 | 1 | 0 | |a Zhongzhou Chen |e author |
700 | 1 | 0 | |a Katja Aviszus |e author |
700 | 1 | 0 | |a Walter Downing |e author |
700 | 1 | 0 | |a Shelley Peterson |e author |
700 | 1 | 0 | |a Lyndon Reynoso |e author |
700 | 1 | 0 | |a Gregory P. Downey |e author |
700 | 1 | 0 | |a Stephen K. Frankel |e author |
700 | 1 | 0 | |a John Kappler |e author |
700 | 1 | 0 | |a Philippa Marrack |e author |
700 | 1 | 0 | |a Gongyi Zhang |e author |
245 | 0 | 0 | |a 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro |
260 | |b Taylor & Francis Group, |c 2021-01-01T00:00:00Z. | ||
500 | |a 10.1080/19420862.2021.1919285 | ||
500 | |a 1942-0870 | ||
500 | |a 1942-0862 | ||
520 | |a 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. | ||
546 | |a EN | ||
690 | |a SARS-COV-2 | ||
690 | |a COVID-19 | ||
690 | |a B.1.1.7/501Y.V1 | ||
690 | |a B.1.351/501Y.V2 | ||
690 | |a P.1/501Y.V3 | ||
690 | |a ACE2 | ||
690 | |a Therapeutics. Pharmacology | ||
690 | |a RM1-950 | ||
690 | |a Immunologic diseases. Allergy | ||
690 | |a RC581-607 | ||
655 | 7 | |a article |2 local | |
786 | 0 | |n mAbs, Vol 13, Iss 1 (2021) | |
787 | 0 | |n https://www.tandfonline.com/doi/10.1080/19420862.2021.1919285 | |
787 | 0 | |n https://doaj.org/toc/1942-0862 | |
787 | 0 | |n https://doaj.org/toc/1942-0870 | |
856 | 4 | 1 | |u https://doaj.org/article/8fedadc2ee61424d849e04c78d26f524 |z Connect to this object online. |