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Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 May 17; Vol. 119 (20), pp. e2120976119. Date of Electronic Publication: 2022 May 12. - Publication Year :
- 2022
-
Abstract
- As the coronavirus disease 2019 (COVID-19) pandemic continues, there is a strong need for highly potent monoclonal antibodies (mAbs) that are resistant against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs). Here, we evaluate the potency of the previously described mAb J08 against these variants using cell-based assays and delve into the molecular details of the binding interaction using cryoelectron microscopy (cryo-EM) and X-ray crystallography. We show that mAb J08 has low nanomolar affinity against most VoCs and binds high on the receptor binding domain (RBD) ridge, away from many VoC mutations. These findings further validate the phase II/III human clinical trial underway using mAb J08 as a monoclonal therapy.
- Subjects :
- Antibody Affinity
COVID-19 therapy
Humans
Neutralization Tests
Antibodies, Monoclonal chemistry
Antibodies, Monoclonal therapeutic use
Antibodies, Neutralizing chemistry
Antibodies, Neutralizing therapeutic use
Antibodies, Viral chemistry
Antibodies, Viral therapeutic use
SARS-CoV-2 immunology
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 119
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 35549549
- Full Text :
- https://doi.org/10.1073/pnas.2120976119