Scientists unlock virus-fighting power with synthetic nanobody platform Nanobodies ViralInfections Biologics AntiSARSCoV2 Nanobodies Biomedicine PNASNews
By Tarun Sai LomteJun 8 2023Reviewed by Benedette Cuffari, M.Sc. In a recent study published in the Proceedings of the National Academy of Sciences, researchers developed a fully synthetic platform for nanobody generation.
Nanobodies recognize targets through a single variable heavy domain. Nanobodies can target epitopes inaccessible to bulkier antibodies, which require variable light and heavy domains to form the paratope. Nanobodies are commonly obtained by immunizing camelids; however, yeast- and phage-based synthetic platforms have also been used for de novo discovery.
Nanobodies were well displayed on the surface, with around 67% of the library showing surface display. The library was then validated using the receptor-binding domain of the SARS-CoV-2 spike protein as the test antigen. The library was screened for RBD binders in three rounds of magnetic-activated cell sorting and five rounds of fluorescence-activated cell sorting .
Subsequently, the number of enriched nanobodies and their target RBD epitopes were determined. A yeast competition assay was used to assess epitope specificity using three SARS-CoV-2 antibodies, including CR3022 , CC12.1 , and CC6.30 . Six nanobodies competed with CC6.30 and CR3022, whereas the remaining four competed with all three antibodies. Overall, 45 nanobodies were selected for further validation. Of these, twenty-four nanobodies were binned to the class 4, CR3022-competitive epitope , and 21 were binned to the class 2, CC6.30-competitive epitope .
Nanobodies with RBD-specific binding and monodisperse size-exclusion profiles were formatted into bsNb4-Ig with LM18 as the light chain and class 2/4 nanobody as the heavy chain. Thirteen of the 23 Nb-C4/LM18 bsNb4-Igs and 16 of the 20 Nb-C2/LM18 bsNb4-Igs had 10- to 470-fold improved neutralization than LM18-Fc fusion construct.
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