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Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice. 2021
Raoul De Gasparo, and
Mattia Pedotti, and
Luca Simonelli, and
Petr Nickl, and
Frauke Muecksch, and
Irene Cassaniti, and
Elena Percivalle, and
Julio C C Lorenzi, and
Federica Mazzola, and
Davide Magrì, and
Tereza Michalcikova, and
Jan Haviernik, and
Vaclav Honig, and
Blanka Mrazkova, and
Natalie Polakova, and
Andrea Fortova, and
Jolana Tureckova, and
Veronika Iatsiuk, and
Salvatore Di Girolamo, and
Martin Palus, and
Dagmar Zudova, and
Petr Bednar, and
Ivana Bukova, and
Filippo Bianchini, and
Dora Mehn, and
Radim Nencka, and
Petra Strakova, and
Oto Pavlis, and
Jan Rozman, and
Sabrina Gioria, and
Josè Camilla Sammartino, and
Federica Giardina, and
Stefano Gaiarsa, and
Qiang Pan-Hammarström, and
Christopher O Barnes, and
Pamela J Bjorkman, and
Luigi Calzolai, and
Antonio Piralla, and
Fausto Baldanti, and
Michel C Nussenzweig, and
Paul D Bieniasz, and
Theodora Hatziioannou, and
Jan Prochazka, and
Radislav Sedlacek, and
Davide F Robbiani, and
Daniel Ruzek, and
Luca Varani
Institute for Research in Biomedicine, Università della Svizzera italiana (USI), Bellinzona, Switzerland.
Neutralizing antibodies that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein are among the most promising approaches against COVID-191,2. 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-193. 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 inflammation, CoV-X2 protects mice from disease and suppresses viral escape. Thus, the simultaneous targeting of non-overlapping RBD epitopes by IgG-like bispecific antibodies is feasible and effective, and combines the advantages of antibody cocktails with those of single-molecule approaches.
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Sabrina Gioria, and
Josè Camilla Sammartino, and
Federica Giardina, and
Stefano Gaiarsa, and
Qiang Pan-Hammarström, and
Christopher O Barnes, and
Pamela J Bjorkman, and
Luigi Calzolai, and
Antonio Piralla, and
Fausto Baldanti, and
Michel C Nussenzweig, and
Paul D Bieniasz, and
Theodora Hatziioannou, and
Jan Prochazka, and
Radislav Sedlacek, and
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