Author: Chunyun Sun; Long Chen; Ji Yang; Chunxia Luo; Yanjing Zhang; Jing Li; Jiahui Yang; Jie Zhang; Liangzhi Xie
Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development Document date: 2020_2_20
ID: nhq0oq8y_38
Snippet: Since SARS-CoV-2 and SARS-CoV are both coronaviruses with over 70% sequence homology and share the same human receptor ACE2, analyzing SARS-CoV's antibodies' cross-reactivity to SARS-CoV-2 may provide useful information on whether neutralizing epitopes were conserved on the two coronaviruses. Two rabbit polyclonal antibodies produced with SARS-CoV S1 and RBD proteins had potent binding and neutralizing activities to SARS-CoV but only modest cross.....
Document: Since SARS-CoV-2 and SARS-CoV are both coronaviruses with over 70% sequence homology and share the same human receptor ACE2, analyzing SARS-CoV's antibodies' cross-reactivity to SARS-CoV-2 may provide useful information on whether neutralizing epitopes were conserved on the two coronaviruses. Two rabbit polyclonal antibodies produced with SARS-CoV S1 and RBD proteins had potent binding and neutralizing activities to SARS-CoV but only modest cross-binding and cross-neutralizing activities to the new SARS-CoV-2 virus. Four highly potent ACE2 blocking SARS-CoV monoclonal antibodies showed binding affinities to SARS-CoV S1 protein in the range of 0.2 nM to 8.7 pM, and very high neutralizing activities to SARS-CoV. As low as 0.2 ug/mL nAb can lead to 100% neutralization of SARS-CoV PSV. However, virtually no cross-binding or cross neutralizing activities against the novel SARS-CoV-2 virus were detected with the four ACE2 blocking monoclonal antibodies.
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