Anja Schlör, Stefan Hirschberg, Ghada Ben Amor, Toni Luise Meister, Prerna Arora, Stefan Pöhlmann, Markus Hoffmann, Stephanie Pfänder, Omar Kamal Eddin, Julian Kamhieh-Milz, Katja Hanack
- Introduction: The ongoing COVID-19 pandemic situation caused by SARS-CoV-2 and variants of concern such as B.1.617.2 (Delta) and recently, B.1.1.529 (Omicron) is posing multiple challenges to humanity. The rapid evolution of the virus requires adaptation of diagnostic and therapeutic applications.
Objectives: In this study, we describe camelid heavy-chain-only antibodies (hcAb) as useful tools for novel in vitro diagnostic assays and for therapeutic applications due to their neutralizing capacity.
Methods: Five antibody candidates were selected out of a naïve camelid library by phage display and expressed as full length IgG2 antibodies. The antibodies were characterized by Western blot, enzyme-linked immunosorbent assays, surface plasmon resonance with regard to their specificity to the recombinant SARS-CoV-2 Spike protein and to SARS-CoV-2 virus-like particles. Neutralization assays were performed with authentic SARS-CoV-2 and pseudotyped viruses (wildtype and Omicron).
Results: All antibodies efficiently detect recombinantIntroduction: The ongoing COVID-19 pandemic situation caused by SARS-CoV-2 and variants of concern such as B.1.617.2 (Delta) and recently, B.1.1.529 (Omicron) is posing multiple challenges to humanity. The rapid evolution of the virus requires adaptation of diagnostic and therapeutic applications.
Objectives: In this study, we describe camelid heavy-chain-only antibodies (hcAb) as useful tools for novel in vitro diagnostic assays and for therapeutic applications due to their neutralizing capacity.
Methods: Five antibody candidates were selected out of a naïve camelid library by phage display and expressed as full length IgG2 antibodies. The antibodies were characterized by Western blot, enzyme-linked immunosorbent assays, surface plasmon resonance with regard to their specificity to the recombinant SARS-CoV-2 Spike protein and to SARS-CoV-2 virus-like particles. Neutralization assays were performed with authentic SARS-CoV-2 and pseudotyped viruses (wildtype and Omicron).
Results: All antibodies efficiently detect recombinant SARS-CoV-2 Spike protein and SARS-CoV-2 virus-like particles in different ELISA setups. The best combination was shown with hcAb B10 as catcher antibody and HRP-conjugated hcAb A7.2 as the detection antibody. Further, four out of five antibodies potently neutralized authentic wildtype SARS-CoV-2 and particles pseudotyped with the SARS-CoV-2 Spike proteins of the wildtype and Omicron variant, sublineage BA.1 at concentrations between 0.1 and 0.35 ng/mL (ND50).
Conclusion: Collectively, we report novel camelid hcAbs suitable for diagnostics and potential therapy.…
MetadatenAuthor details: | Anja SchlörORCiD, Stefan HirschbergORCiD, Ghada Ben Amor, Toni Luise MeisterORCiDGND, Prerna AroraORCiDGND, Stefan PöhlmannORCiDGND, Markus HoffmannORCiD, Stephanie PfänderORCiDGND, Omar Kamal Eddin, Julian Kamhieh-MilzORCiDGND, Katja HanackORCiDGND |
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DOI: | https://doi.org/10.3389/fimmu.2022.930975 |
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ISSN: | 1664-3224 |
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Title of parent work (English): | Frontiers in Immunology |
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Publisher: | Frontiers Media SA |
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Place of publishing: | Lausanne, Schweiz |
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Further contributing person(s): | Ingo Drexler, Oral Alpan, Elizabeth De Gaspari |
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Publication type: | Article |
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Language: | English |
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Date of first publication: | 2022/09/14 |
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Publication year: | 2022 |
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Release date: | 2022/12/07 |
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Tag: | Omicron; SARS-CoV-2; camelid heavy-chain-only antibodies; nanobodies; neutralization; single domain antibodies |
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Number of pages: | 14 |
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First page: | 1 |
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Last Page: | 14 |
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Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
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| Extern / Extern |
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DDC classification: | 6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit |
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Peer review: | Referiert |
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Grantor: | Publikationsfonds der Universität Potsdam |
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Publishing method: | Open Access / Gold Open-Access |
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License (German): | CC-BY - Namensnennung 4.0 International |
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External remark: | Zweitveröffentlichung in der Schriftenreihe Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe ; 1280 |
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