Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1 antibodies
Antibodies against coronavirus spike protein potently protect against infection and disease, but whether such protection can be extended to variant coronaviruses is unclear. This is exemplified by a set of iconic and well-characterized monoclonal antibodies developed after the 2003 SARS outbreak, in...
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Taylor & Francis Group,
2021-01-01T00:00:00Z.
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| 042 | |a dc | ||
| 100 | 1 | 0 | |a Romain Rouet |e author |
| 700 | 1 | 0 | |a Ohan Mazigi |e author |
| 700 | 1 | 0 | |a Gregory J. Walker |e author |
| 700 | 1 | 0 | |a David B. Langley |e author |
| 700 | 1 | 0 | |a Meghna Sobti |e author |
| 700 | 1 | 0 | |a Peter Schofield |e author |
| 700 | 1 | 0 | |a Helen Lenthall |e author |
| 700 | 1 | 0 | |a Jennifer Jackson |e author |
| 700 | 1 | 0 | |a Stephanie Ubiparipovic |e author |
| 700 | 1 | 0 | |a Jake Y. Henry |e author |
| 700 | 1 | 0 | |a Arunasingam Abayasingam |e author |
| 700 | 1 | 0 | |a Deborah Burnett |e author |
| 700 | 1 | 0 | |a Anthony Kelleher |e author |
| 700 | 1 | 0 | |a Robert Brink |e author |
| 700 | 1 | 0 | |a Rowena A. Bull |e author |
| 700 | 1 | 0 | |a Stuart Turville |e author |
| 700 | 1 | 0 | |a Alastair G. Stewart |e author |
| 700 | 1 | 0 | |a Christopher C. Goodnow |e author |
| 700 | 1 | 0 | |a William D. Rawlinson |e author |
| 700 | 1 | 0 | |a Daniel Christ |e author |
| 245 | 0 | 0 | |a Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1 antibodies |
| 260 | |b Taylor & Francis Group, |c 2021-01-01T00:00:00Z. | ||
| 500 | |a 10.1080/19420862.2021.1922134 | ||
| 500 | |a 1942-0870 | ||
| 500 | |a 1942-0862 | ||
| 520 | |a Antibodies against coronavirus spike protein potently protect against infection and disease, but whether such protection can be extended to variant coronaviruses is unclear. This is exemplified by a set of iconic and well-characterized monoclonal antibodies developed after the 2003 SARS outbreak, including mAbs m396, CR3022, CR3014 and 80R, which potently neutralize SARS-CoV-1, but not SARS-CoV-2. Here, we explore antibody engineering strategies to change and broaden their specificity, enabling nanomolar binding and potent neutralization of SARS-CoV-2. Intriguingly, while many of the matured clones maintained specificity of the parental antibody, new specificities were also observed, which was further confirmed by X-ray crystallography and cryo-electron microscopy, indicating that a limited set of VH antibody domains can give rise to variants targeting diverse epitopes, when paired with a diverse VL repertoire. Our findings open up over 15 years of antibody development efforts against SARS-CoV-1 to the SARS-CoV-2 field and outline general principles for the maturation of antibody specificity against emerging viruses. | ||
| 546 | |a EN | ||
| 690 | |a Monoclonal antibodies | ||
| 690 | |a antibody maturation | ||
| 690 | |a antibody engineering | ||
| 690 | |a phage display | ||
| 690 | |a SARS-CoV-2 | ||
| 690 | |a structural studies | ||
| 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/10.1080/19420862.2021.1922134 | |
| 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/cad1878f11e24fe7a3dee032090722d6 |z Connect to this object online. |