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New variants have affected\n                    antibody interaction with the surface spike protein. We defined the domain\n                    specificities and measured hexa-proline stabilized spike protein (HexaPro)\n                    binding kinetics of a large panel of antibodies sourced by the Coronavirus\n                    Immunotherapeutics Consortium. Epitope binning analysis of antibodies competing\n                    for HexaPro binding separated the fine specificities of the majority of\n                    antibodies to four regions: top, outer, mesa\/valley, or cryptic site of receptor\n                    binding domain (RBD). Most of the top-RBD-specific antibodies showed\n                    &gt;3-fold loss of binding and authentic-virus neutralization activity for\n                    the B.1.351 variant. Remarkably, among RBD mesa\/valley-specific or\n                    cryptic-site-specific antibodies, 55% showed &gt;3-fold stronger affinities,\n                    and at least 60% maintained neutralization activity for the B.1.351 variant.\n                    These data also highlighted the diversity of SARS-CoV-2-specific antibodies that\n                    retain high spike affinities and antiviral functions across variants.<\/jats:p>\n          <jats:sec>\n            <jats:title>IMPORTANCE<\/jats:title>\n            <jats:p>Multiple SARS-CoV-2 variants of concern have emerged and caused a significant\n                        number of infections and deaths worldwide. These variants of concern contain\n                        mutations that might significantly affect antigen-targeting by antibodies.\n                        It is therefore important to further understand how antibody binding and\n                        neutralization are affected by the mutations in SARS-CoV-2 variants. We\n                        highlighted how antibody epitope specificity can influence antibody binding\n                        to SARS-CoV-2 spike protein variants and neutralization of SARS-CoV-2\n                        variants. We showed that weakened spike binding and neutralization of Beta\n                        (B.1.351) and Omicron (BA.1) variants compared to wildtype are not universal\n                        among the panel of antibodies and identified antibodies of a specific\n                        binding footprint exhibiting consistent enhancement of spike binding and\n                        retained neutralization to Beta variant. These data and analysis can inform\n                        how antigen-targeting by antibodies might evolve during a pandemic and\n                        prepare for potential future sarbecovirus outbreaks.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1128\/jvi.01070-23","type":"journal-article","created":{"date-parts":[[2023,11,29]],"date-time":"2023-11-29T09:01:27Z","timestamp":1701248487000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Cryptic-site-specific antibodies to the SARS-CoV-2 receptor binding                    domain can retain functional binding affinity to spike variants"],"prefix":"10.1128","volume":"97","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-0582-3863","authenticated-orcid":false,"given":"Kan","family":"Li","sequence":"first","affiliation":[{"name":"Center for Human Systems Immunology, Duke University","place":["Durham, USA"]},{"name":"Department of Surgery, Duke University","place":["Durham, USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard H. 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