| Literature DB >> 34329642 |
Shane Miersch1, Zhijie Li2, Reza Saberianfar1, Mart Ustav3, James Brett Case4, Levi Blazer1, Chao Chen1, Wei Ye1, Alevtina Pavlenco1, Maryna Gorelik1, Julia Garcia Perez1, Suryasree Subramania1, Serena Singh1, Lynda Ploder1, Safder Ganaie4, Rita E Chen5, Daisy W Leung4, Pier Paolo Pandolfi6, Giuseppe Novelli7, Giulia Matusali8, Francesca Colavita8, Maria R Capobianchi8, Suresh Jain9, J B Gupta9, Gaya K Amarasinghe10, Michael S Diamond11, James Rini12, Sachdev S Sidhu13.
Abstract
Neutralizing antibodies (nAbs) hold promise as therapeutics against COVID-19. Here, we describe protein engineering and modular design principles that have led to the development of synthetic bivalent and tetravalent nAbs against SARS-CoV-2. The best nAb targets the host receptor binding site of the viral S-protein and tetravalent versions block entry with a potency exceeding bivalent nAbs by an order of magnitude. Structural studies show that both the bivalent and tetravalent nAbs can make multivalent interactions with a single S-protein trimer, consistent with the avidity and potency of these molecules. Significantly, we show that the tetravalent nAbs show increased tolerance to potential virus escape mutants and an emerging variant of concern. Bivalent and tetravalent nAbs can be produced at large-scale and are as stable and specific as approved antibody drugs. Our results provide a general framework for enhancing antiviral therapies against COVID-19 and related viral threats, and our strategy can be applied to virtually any antibody drug.Entities:
Keywords: RBD-binding; anti-viral; neutralizing; synthetic; tetravalent
Year: 2021 PMID: 34329642 DOI: 10.1016/j.jmb.2021.167177
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469