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© The severe acute respiratory syndrome coronavirus 2 (SARS–CoV–2) entry into cells is a complex process that involves (1) recognition of the host entry receptor, angiotensin–converting enzyme 2 (ACE2), by the SARS–CoV–2 spike protein receptor binding domain (RBD), and (2) the subsequent fusion of the viral and cell membranes. Our long–term immune–defense is the production of antibodies (Abs) that recognize the SARS–CoV–2 RBD and successfully block viral infection. Thus, to understand immunity against SARS–CoV–2, a comprehensive molecular understanding of how human SARS–CoV–2 Abs recognize the RBD is needed. Here, we report the sequence–specific backbone assignment of the SARS–CoV–2 RBD and, furthermore, demonstrate that biomolecular NMR spectroscopy chemical shift perturbation (CSP) mapping successfully and rapidly identifies the molecular epitopes of RBD–specific mAbs. By incorporating NMR–based CSP mapping with other molecular techniques to define RBD–mAb interactions and then correlating these data with neutralization efficacy, structure–based approaches for developing improved vaccines and COVID–19 mAb–based therapies will be greatly accelerated.
