{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["De Gasparo R"],"funding":["Swiss National Science Foundation","Howard Hughes Medical Institute","NIAID NIH HHS","NIH HHS"],"pagination":["424-428"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12910678"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["593(7859)"],"pubmed_abstract":["Neutralizing antibodies that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein are among the most promising approaches against COVID-19<sup>1,2</sup>. A bispecific IgG1-like molecule (CoV-X2) has been developed on the basis of C121 and C135, two antibodies derived from donors who had recovered from COVID-19<sup>3</sup>. Here we show that CoV-X2 simultaneously binds two independent sites on the RBD and, unlike its parental antibodies, prevents detectable spike binding to the cellular receptor of the virus, angiotensin-converting enzyme 2 (ACE2). Furthermore, CoV-X2 neutralizes wild-type SARS-CoV-2 and its variants of concern, as well as escape mutants generated by the parental monoclonal antibodies. We also found that in a mouse model of SARS-CoV-2 infection with lung"],"journal":["Nature"],"pubmed_title":["Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice."],"pmcid":["PMC12910678"],"funding_grant_id":["P50 AI150464","P01-AI138398-S1","U01 AI151698","R01 AI078788","2U19AI111825","182270","R37 AI064003"],"pubmed_authors":["Nickl P","Robbiani DF","Nussenzweig MC","Mehn D","Haviernik J","Baldanti F","Mazzola F","Bednar P","Ruzek D","Muecksch F","Prochazka J","Simonelli L","Lorenzi JCC","Strakova P","Honig V","Fortova A","Polakova N","Barnes CO","Bjorkman PJ","Piralla A","Varani L","Tureckova J","Calzolai L","Michalcikova T","Bukova I","Gaiarsa S","Pedotti M","Cassaniti I","Nencka R","Sammartino JC","Hatziioannou T","De Gasparo R","Palus M","Magri D","Mrazkova B","Zudova D","Bianchini F","Percivalle E","Bieniasz PD","Gioria S","Rozman J","Giardina F","Pavlis O","Iatsiuk V","Sedlacek R","Di Girolamo S","Pan-Hammarstrom Q"],"additional_accession":[]},"is_claimable":false,"name":"Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice.","description":"Neutralizing antibodies that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein are among the most promising approaches against COVID-19<sup>1,2</sup>. A bispecific IgG1-like molecule (CoV-X2) has been developed on the basis of C121 and C135, two antibodies derived from donors who had recovered from COVID-19<sup>3</sup>. Here we show that CoV-X2 simultaneously binds two independent sites on the RBD and, unlike its parental antibodies, prevents detectable spike binding to the cellular receptor of the virus, angiotensin-converting enzyme 2 (ACE2). Furthermore, CoV-X2 neutralizes wild-type SARS-CoV-2 and its variants of concern, as well as escape mutants generated by the parental monoclonal antibodies. We also found that in a mouse model of SARS-CoV-2 infection with lung","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2026-07-16T05:15:01.209Z","creation":"2026-07-09T13:09:54.138Z"},"accession":"S-EPMC12910678","cross_references":{"pubmed":["33767445"],"doi":["10.1038/s41586-021-03461-y"]}}