Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35549549.
- Also identified by DOI 10.1073/pnas.2120976119 and PMC identifier 9171815.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Antibodies, Monoclonal
- Antibodies, Neutralizing
- Antibodies, Viral
- SARS-CoV-2