Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody

Proc Natl Acad Sci U S A. 2022 May 17;119(20):e2120976119. doi: 10.1073/pnas.2120976119. Epub 2022 May 12.

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.

Keywords: SARS-CoV-2; cryoelectron microscopy; monoclonal therapy; neutralizing antibody; variants of concern.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal* / chemistry
  • Antibodies, Monoclonal* / therapeutic use
  • Antibodies, Neutralizing* / chemistry
  • Antibodies, Neutralizing* / therapeutic use
  • Antibodies, Viral* / chemistry
  • Antibodies, Viral* / therapeutic use
  • Antibody Affinity
  • COVID-19 / therapy
  • Humans
  • Neutralization Tests
  • SARS-CoV-2* / immunology

Substances

  • Antibodies, Monoclonal
  • Antibodies, Neutralizing
  • Antibodies, Viral

Supplementary concepts

  • SARS-CoV-2 variants