Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 33110068.
- Also identified by DOI 10.1038/s41467-020-19231-9 and PMC identifier 7591918.
- 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
SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2.
Medical subject headings
- Antibodies, Neutralizing
- Antibody Affinity
- Betacoronavirus