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Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice
- 1.
SYSNO ASEP 0544120 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice Author(s) De Gasparo, R. (CH)
Pedotti, M. (CH)
Simonelli, L. (CH)
Nickl, Petr (UMG-J)
Muecksch, F. (US)
Cassaniti, I. (IT)
Percivalle, E. (IT)
Lorenzi, J.C.C. (US)
Mazzola, F. (CH)
Magri, D. (IT)
Michalčíková, Tereza (UMG-J)
Haviernik, J. (CZ)
Hönig, Václav (BC-A) RID, ORCID
Mrázková, Blanka (UMG-J)
Poláková, Natálie (UMG-J)
Fořtová, A. (CZ)
Turečková, Jolana (UMG-J) RID
Iatsiuk, Veronika (UMG-J)
Di Girolamo, S. (CH)
Palus, Martin (BC-A) RID, ORCID
Zudová, Dagmar (UMG-J)
Bednář, P. (CZ)
Buková, Ivana (UMG-J)
Bianchini, F. (CH)
Mehn, D. (IT)
Nencka, Radim (UOCHB-X) RID, ORCID
Straková, P. (CZ)
Pavlis, O. (CZ)
Rozman, Jan (UMG-J)
Gioria, S. (IT)
Sammartino, J.C. (IT)
Giardina, F. (IT)
Gaiarsa, S. (IT)
Pan-Hammarstrom, Q. (SE)
Barnes, C.O. (US)
Bjorkman, P.J. (US)
Calzolai, L. (IT)
Piralla, A. (IT)
Baldanti, F. (IT)
Nussenzweig, M.C. (US)
Bieniasz, P.D. (US)
Hatziioannou, T. (US)
Procházka, Jan (UMG-J) ORCID
Sedláček, Radislav (UMG-J) RID
Robbiani, D.F. (CH)
Růžek, Daniel (BC-A) RID, ORCID
Varani, L. (CH)Number of authors 47 Source Title Nature. - : Palgrave Macmillan - ISSN 0028-0836
Roč. 593, č. 7859 (2021), s. 424-428Number of pages 5 s. Publication form Online - E Language eng - English Country GB - United Kingdom Keywords virus ; infection ; mutations ; domain Subject RIV EB - Genetics ; Molecular Biology OECD category Virology Subject RIV - cooperation Biology Centre (since 2006) - Microbiology, Virology R&D Projects LM2018126 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED2.1.00/19.0395 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA20-14325S GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support UMG-J - RVO:68378050 ; UOCHB-X - RVO:61388963 ; BC-A - RVO:60077344 UT WOS 000640199100001 EID SCOPUS 85103180392 DOI 10.1038/s41586-021-03461-y Annotation 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(1,2). 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-19(3). 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. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2022 Electronic address https://www.nature.com/articles/s41586-021-03461-y
Number of the records: 1