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Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation.
Hurlburt, Nicholas K; Wan, Yu-Hsin; Stuart, Andrew B; Feng, Junli; McGuire, Andrew T; Stamatatos, Leonidas; Pancera, Marie.
Afiliação
  • Hurlburt NK; Fred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA, USA.
  • Wan YH; Fred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA, USA.
  • Stuart AB; Fred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA, USA.
  • Feng J; Fred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA, USA.
  • McGuire AT; Fred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA, USA.
  • Stamatatos L; University of Washington, Department of Global Health, Seattle, WA, USA.
  • Pancera M; Fred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA, USA.
bioRxiv ; 2020 Jun 12.
Article em En | MEDLINE | ID: mdl-32577631
SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determined 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 (RBD). The structure reveals CV30's epitope overlaps with the human ACE2 receptor binding site thus providing the structural basis for its neutralization by preventing ACE2 binding.

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: BioRxiv Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: BioRxiv Ano de publicação: 2020 Tipo de documento: Article