The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
A robust pipeline for rapid production of versatile nanobody repertoires
Open accessAbstract
Nanobodies are single-domain antibodies derived from the variable regions of Camelidae atypical immunoglobulins. They show promise as high-affinity reagents for research, diagnostics and therapeutics owing to their high specificity, small size (∼15 kDa) and straightforward bacterial expression. However, identification of repertoires with sufficiently high affinity has proven time consuming and difficult, hampering nanobody implementation. Our approach generates large repertoires of readily expressible recombinant nanobodies with high affinities and specificities against a given antigen. We demonstrate the efficacy of this approach through the production of large repertoires of nanobodies against two antigens, GFP and mCherry, with Kd values into the subnanomolar range. After mapping diverse epitopes on GFP, we were also able to design ultrahigh-affinity dimeric nanobodies with Kd values as low as ∼30 pM. The approach presented here is well suited for the routine production of high-affinity capture reagents for various biomedical applications.
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Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241
Nanobodies: natural single-domain antibodies
Muyldermans, S. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-063011-092449 · Cited by 2,304
Properties, production, and applications of camelid single-domain antibody fragments
Harmsen, M. M., & De Haard, H. J. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1142-2 · Cited by 809
Fluorescent Proteins as Proteomic Probes
Cristea, I. M., Williams, R., Chait, B. T., & Rout, M. P. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500227-mcp200 · Cited by 251
Self-citation
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Roybal, K. T., Williams, J. Z., Morsut, L., Rupp, L. J., Kolinko, I., Choe, J. H., Walker, W. J., McNally, K. A., & Lim, W. A. (2016) · Cell · doi:10.1016/j.cell.2016.09.011 · Cited by 721
Programming self-organizing multicellular structures with synthetic cell-cell signaling
Toda, S., Blauch, L. R., Tang, S. K. Y., Morsut, L., & Lim, W. A. (2018) · Science · doi:10.1126/science.aat0271 · Cited by 470
Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape
Koenig, P.-A., Das, H., Liu, H., Kümmerer, B. M., Gohr, F. N., Jenster, L.-M., Schiffelers, L. D. J., Tesfamariam, Y. M., Uchima, M., Wuerth, J. D., et al. (2021) · Science · doi:10.1126/science.abe6230 · Cited by 396
Treweek, J. B., Chan, K. Y., Flytzanis, N. C., Yang, B., Deverman, B. E., Greenbaum, A., Lignell, A., Xiao, C., Cai, L., Ladinsky, M. S., et al. (2015) · Nature Protocols · doi:10.1038/nprot.2015.122 · Cited by 258
Pham, T. C., Jayasinghe, M. K., Pham, T. T., Yang, Y., Wei, L., Usman, W. M., Chen, H., Pirisinu, M., Gong, J., Kim, S., et al. (2021) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12057 · Cited by 250
Metadata
- Authors
- Fridy, P. C., Li, Y., Keegan, S., Thompson, M. K., Nudelman, I., Scheid, J. F., Oeffinger, M., Nussenzweig, M. C., Fenyö, D., Chait, B. T., & Rout, M. P.
- Venue
- Nature Methods
- Published
- 2014-11-02
- Volume
- 11
- Issue
- 12
- Pages
- 1253-1260
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2087904752
- Cited by
- 499
- References
- 5
- FWCI
- 18.76
- Type
- journal article
- Language
- en
- Open access
- green
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