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TitlePotent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1 antibodies.
Journal, issue, pagesMAbs, Vol. 13, Issue 1, Page 1922134, Year 2021
Publish dateMay 28, 2021
AuthorsRomain Rouet / Ohan Mazigi / Gregory J Walker / David B Langley / Meghna Sobti / Peter Schofield / Helen Lenthall / Jennifer Jackson / Stephanie Ubiparipovic / Jake Y Henry / Arunasingam Abayasingam / Deborah Burnett / Anthony Kelleher / Robert Brink / Rowena A Bull / Stuart Turville / Alastair G Stewart / Christopher C Goodnow / William D Rawlinson / Daniel Christ /
PubMed AbstractAntibodies 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 ...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.
External linksMAbs / PubMed:34024246 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.69 - 4.6 Å
Structure data

EMDB-23111:
SARS CoV-2 spike trimer
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-23112:
SARS CoV-2 spike trimer + CR3022-B6
Method: EM (single particle) / Resolution: 4.6 Å

EMDB-23113:
SARS CoV-2 spike trimer + CR3014-D1
Method: EM (single particle) / Resolution: 4.4 Å

PDB-7kza:
Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1antibodies
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

PDB-7kzb:
Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1antibodies
Method: X-RAY DIFFRACTION / Resolution: 2.83 Å

PDB-7kzc:
Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1antibodies
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-CL:
Unknown entry / Chloride

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-NA:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-HOH:
WATER / Water

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / COVID19 / SARS-CoV2 / antibody / ANTIVIRAL PROTEIN / VIRAL PROTEIN/Immune System / VIRAL PROTEIN-Immune System complex

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