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Here, 3 receptor binding domain (RBD) specific monoclonal antibodies (mAbs), 58G6, 510A5 and 13G9, with high neutralizing potency blocking authentic SARS-CoV-2 virus display remarkable efficacy against authentic B.1.351 virus. Surprisingly, structural analysis has revealed that 58G6 and 13G9 both recognize the steric region S\n                    <jats:sup>470\u2013495<\/jats:sup>\n                    on the RBD, overlapping the E484K mutation presented in B.1.351. Also, 58G6 directly binds to another region S\n                    <jats:sup>450\u2013458<\/jats:sup>\n                    in the RBD. Significantly, 58G6 and 510A5 both demonstrate prophylactic efficacy against authentic SARS-CoV-2 and B.1.351 viruses in the transgenic mice expressing human ACE2 (hACE2), protecting weight loss and reducing virus loads. Together, we have evidenced 2 potent neutralizing Abs with unique mechanism targeting authentic SARS-CoV-2 mutants, which can be promising candidates to fulfill the urgent needs for the prolonged COVID-19 pandemic.\n                  <\/jats:p>","DOI":"10.1038\/s41467-021-26539-7","type":"journal-article","created":{"date-parts":[[2021,11,2]],"date-time":"2021-11-02T07:03:37Z","timestamp":1635836617000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":46,"title":["Potent SARS-CoV-2 neutralizing antibodies with protective efficacy against newly emerged mutational 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