Author: Hurlburt, Nicholas K.; Wan, Yu-Hsin; Stuart, Andrew B.; Feng, Junli; McGuire, Andrew T.; Stamatatos, Leonidas; Pancera, Marie
Title: Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation Cord-id: o8uadujh Document date: 2020_6_12
ID: o8uadujh
Snippet: 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.
Document: 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.
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