PMC:7091888 / 21585-22720 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7091888","sourcedb":"PMC","sourceid":"7091888","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7091888","text":"In summary, we have characterized the SARS-CoV-2 RBD protein which exhibits strong binding to its cell-associated and soluble ACE2 receptors with human and bat origin. This RBD protein also demonstrated significantly higher binding affinity to ACE2 than SARS-CoV RBD. SARS-CoV-2 RBD protein could block S protein-mediated SARS-CoV-2 pseudovirus and SARS-CoV pseudovirus entry into their respective ACE2 receptor-expressing target cells, suggesting the potential of SARS-CoV-2 RBD protein as a viral attachment or entry inhibitor against SARS-CoV-2 and SARS-CoV. SARS-CoV RBD-induced antibodies could cross-react with SARS-CoV-2 RBD and cross-neutralize SARS-CoV-2 pseudovirus infection, indicating that SARS-CoV RBD-specific antibodies may be used for treatment of SARS-CoV-2 infection and that either SARS-CoV RBD protein or SARS-CoV-2 RBD protein may be used as a candidate vaccine to induce cross-reactive or cross-neutralizing antibodies for prevention of SARS-CoV-2 or SARS-CoV infection. Taken together, this study provides an essential foundation for the design and development of SARS-CoV-2 RBD-based vaccines and 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