The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Isolation of human monoclonal antibodies by mammalian cell display
Open accessAbstract
Due to their low immunogenicity in patients, humanized or fully human mAbs are becoming increasingly important for the treatment of a growing number of diseases, including cancer, infections, and immune disorders. Here, we describe a technology allowing for the rapid isolation of fully human mAbs. In contrast to previously described methods, B cells specific for an antigen of interest are directly isolated from peripheral blood mononuclear cells (PBMC) of human donors. Recombinant, antigen-specific single-chain Fv (scFv) libraries are generated from this pool of B cells and screened by mammalian cell surface display by using a Sindbis virus expression system. This method allows isolating antigen-specific antibodies by a single round of FACS. The variable regions (VRs) of the heavy chains (HCs) and light chains (LCs) are isolated from positive clones and recombinant fully human antibodies produced as whole IgG or Fab fragments. In this manner, several hypermutated high-affinity antibodies binding the Qβ virus like particle (VLP), a model viral antigen, as well as antibodies specific for nicotine were isolated. All antibodies showed high expression levels in cell culture. The human nicotine-specific mAbs were validated preclinically in a mouse model. Thus, the technology presented here allows for rapid isolation of high-affinity, fully human antibodies with therapeutic potential from human volunteers.
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Traggiai, E., Becker, S., Subbarao, K., Kolesnikova, L., Uematsu, Y., Gismondo, M. R., Murphy, B. R., Rappuoli, R., & Lanzavecchia, A. (2004) · Nature Medicine · doi:10.1038/nm1080 · Cited by 697
Maurer, P., Jennings, G. T., Willers, J., Rohner, F., Lindman, Y., Roubicek, K., Renner, W. A., Müller, P., & Bachmann, M. F. (2005) · European Journal of Immunology · doi:10.1002/eji.200526285 · Cited by 279 · cited 20×
“Characterization of Nicotine-Specific mAb-Nic12.”
BackgroundMethodInfluential
Cited by
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Cheng, Q., Shi, X., Han, M., Smbatyan, G., Lenz, H.-J., & Zhang, Y. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10047 · Cited by 285
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Robinson, M.-P., Ke, N., Lobstein, J., Peterson, C., Szkodny, A., Mansell, T. J., Tuckey, C., Riggs, P. D., Colussi, P. A., Noren, C. J., et al. (2015) · Nature Communications · doi:10.1038/ncomms9072 · Cited by 131
Thoms, F., Jennings, G. T., Maudrich, M., Vogel, M., Haas, S., Zeltins, A., Hofmann-Lehmann, R., Riond, B., Grossmann, J., Hunziker, P., et al. (2019) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2019.01.050 · Cited by 69
Self-citationCystatin F is a biomarker of prion pathogenesis in mice
Nuvolone, M., Schmid, N., Miele, G., Sorce, S., Moos, R., Schori, C., Beerli, R. R., Bauer, M., Saudan, P., Dietmeier, K., et al. (2017) · PLOS ONE · doi:10.1371/journal.pone.0171923 · Cited by 25
Self-citationMonoclonal Antibodies: A Prospective and Retrospective View
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Metadata
- Authors
- Beerli, R. R., Bauer, M., Buser, R. B., Gwerder, M., Muntwiler, S., Maurer, P., Saudan, P., & Bachmann, M. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-09-23
- Volume
- 105
- Issue
- 38
- Pages
- 14336-14341
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W4244541582
- Cited by
- 176
- References
- 2
- FWCI
- 5.73
- Type
- journal article
- Language
- en
- Open access
- green
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- Beerli, R. R., Bauer, M., Buser, R. B., Gwerder, M., Muntwiler, S., Maurer, P., Saudan, P., & Bachmann, M. F. (2008). Isolation of human monoclonal antibodies by mammalian cell display. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0805942105
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