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Potent neutralization of clinical isolates of SARS-CoV-2 D614 and G614 variants by a monomeric, sub-nanomolar affinity nanobody by Valenzuela Nieto, Guillermo (author);Jara, Ronald (author);Watterson, Daniel (author);Modhiran, Naphak (author);Amarilla, Alberto A. (author);Himelreichs, Johanna (author);Khromykh, Alexander A. (author);Salinas-Rebolledo, Constanza (author);Pinto, Teresa (author);Cheuquemilla, Yorka (author);Margolles, Yago (author);López González del Rey, Natalia (author);Miranda-Chacon, Zaray (author);Cuevas, Alexei (author);Berking, Anne (author);Deride, Camila (author);González-Moraga, Sebastián (author);Mancilla, Héctor (author);Maturana, Daniel (author);Langer, Andreas (author);Toledo, Juan Pablo (author);Müller, Ananda (author);Uberti, Benjamín (author);Krall, Paola (author);Ehrenfeld, Pamela (author);Blesa, Javier (author);Chana-Cuevas, Pedro (author);Rehren, German (author);Schwefel, David (author);Fernandez, Luis Ángel (author);Rojas-Fernandez, Alejandro (author) is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Potent neutralization of clinical isolates of SARS-CoV-2 D614 and G614 variants by a monomeric, sub-nanomolar affinity nanobody about?

## Abstract Despite unprecedented global efforts to rapidly develop SARS-CoV-2 treatments, in order to reduce the burden placed on health systems, the situation remains critical. Effective diagnosis, treatment, and prophylactic measures are urgently required to meet global demand: recombinant antibodies fulfill these requirements and have marked clinical potential. Here, we describe the fast-tracked development of an alpaca Nanobody specific for the receptor-binding-domain (RBD) of the SARS-CoV-2 Spike protein with potential therapeutic applicability. We present a rapid method for nanobody isolation that includes an optimized immunization regimen coupled with VHH library E. coli surface display, which allows single-step selection of Nanobodies using a simple density gradient centrifugation of the bacterial library. The selected single and monomeric Nanobody, W25, binds to the SARS-CoV-2 S RBD with sub-nanomolar affinity and efficiently competes with ACE-2 receptor binding. Furthermore, W25 potently neutralizes SARS-CoV-2 wild type and the D614G variant with IC50 values in the nanomolar range, demonstrating its potential as antiviral agent.

Who reads Potent neutralization of clinical isolates of SARS-CoV-2 D614 and G614 variants by a monomeric, sub-nanomolar affinity nanobody?

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Author
Valenzuela Nieto, Guillermo (author);Jara, Ronald (author);Watterson, Daniel (author);Modhiran, Naphak (author);Amarilla, Alberto A. (author);Himelreichs, Johanna (author);Khromykh, Alexander A. (author);Salinas-Rebolledo, Constanza (author);Pinto, Teresa (author);Cheuquemilla, Yorka (author);Margolles, Yago (author);López González del Rey, Natalia (author);Miranda-Chacon, Zaray (author);Cuevas, Alexei (author);Berking, Anne (author);Deride, Camila (author);González-Moraga, Sebastián (author);Mancilla, Héctor (author);Maturana, Daniel (author);Langer, Andreas (author);Toledo, Juan Pablo (author);Müller, Ananda (author);Uberti, Benjamín (author);Krall, Paola (author);Ehrenfeld, Pamela (author);Blesa, Javier (author);Chana-Cuevas, Pedro (author);Rehren, German (author);Schwefel, David (author);Fernandez, Luis Ángel (author);Rojas-Fernandez, Alejandro (author)
Publisher
Springer Science and Business Media LLC
Published
2021
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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