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Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
Nicholas K Hurlburt; Yu-Hsin Wan; Andrew B Stuart; Junli Feng; Andrew T McGuire; Leonidas Stamatatos; Marie Pancera.
Affiliation
  • Nicholas K Hurlburt; Fred Hutchinson Cancer Research Center
  • Yu-Hsin Wan; Fred Hutchinson Cancer Research Center
  • Andrew B Stuart; Fred Hutchinson Cancer Research Center
  • Junli Feng; Fred Hutchinson Cancer Research Center
  • Andrew T McGuire; Fred Hutchinson Cancer Research Center
  • Leonidas Stamatatos; Fred Hutchinson Cancer Research Center
  • Marie Pancera; Fred Hutchinson Cancer Research Center
Preprint in English | bioRxiv | ID: ppbiorxiv-148692
ABSTRACT
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 CV30s epitope overlaps with the human ACE2 receptor binding site thus providing the structural basis for its neutralization by preventing ACE2 binding.
License
cc_by_nc_nd
Full text: Available Collection: Preprints Database: bioRxiv Language: English Year: 2020 Document type: Preprint
Full text: Available Collection: Preprints Database: bioRxiv Language: English Year: 2020 Document type: Preprint
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