Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation.
Nat Commun
; 11(1): 5413, 2020 10 27.
Article
em En
| MEDLINE
| ID: mdl-33110068
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Anticorpos Neutralizantes
/
Betacoronavirus
/
Afinidade de Anticorpos
Limite:
Humans
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article