Summary of paper cited in OP [1]:<p><i>> The most potently neutralizing antibodies to SARS-CoV-2 — including those in clinical use and dominant in polyclonal sera — target the spike RBD. Mutations in the RBD that reduce binding by antibodies have emerged among SARS-CoV-2 variants, highlighting the need for antibodies and vaccines that are robust to viral escape. </i><p><i>> we identify neutralizing antibodies with exceptional sarbecovirus breadth and a corresponding resistance to SARS-CoV-2 escape. One of these antibodies, S2H97, binds with high affinity across all sarbecovirus clades to a cryptic epitope and prophylactically protects hamsters from viral challenge. </i><p><i>> S2H97 exhibits notably tight binding to all RBDs tested, making it, to our knowledge, the broadest pan-sarbecovirus RBD antibody described to date. </i><p><i>> We cannot predict which mutations will next rise to prominence as SARS-CoV-2 continues to evolve, but it seems likely that they will include additional RBM mutations that affect recognition by infection- and vaccine-elicited antibodies. </i><p>This complements a growing body of promising research that will lead to next generation vaccines which should be more resistant to viral evolution. Such research is vital because the current mRNA vaccines induce an immune response that is highly targeted toward the spike protein RBD. Nearly every variant of concern has acquired at least one mutation which confers a degree of immune escape from antibodies targeting the S protein RBD.<p>[1] SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
<a href="https://www.nature.com/articles/s41586-021-03807-6" rel="nofollow">https://www.nature.com/articles/s41586-021-03807-6</a>