Kohler, G. & Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495–497 (1975).
Li, J. et al. Human antibodies for immunotherapy development generated via a human B cell hybridoma technology. Proc. Natl Acad. Sci. USA 103, 3557–3562 (2006).
Fishwild, D. M. et al. High-avidity human IgG kappa monoclonal antibodies from a novel strain of minilocus transgenic mice. Nat. Biotechnol. 14, 845–851 (1996).
Winter, G., Griffiths, A. D., Hawkins, R. E. & Hoogenboom, H. R. Making antibodies by phage display technology. Annu Rev. Immunol. 12, 433–455 (1994).
Lipovsek, D. & Pluckthun, A. In-vitro protein evolution by ribosome display and mRNA display. J. Immunol. Methods 290, 51–67 (2004).
Daugherty, P. S., Chen, G., Olsen, M. J., Iverson, B. L. & Georgiou, G. Antibody affinity maturation using bacterial surface display. Protein Eng. 11, 825–832 (1998).
Harvey, B. R. et al. Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries. Proc. Natl Acad. Sci. USA 101, 9193–9198 (2004).
Hoogenboom, H. R. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23, 1105–1116 (2005).
Boder, E. T. & Wittrup, K. D. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 15, 553–557 (1997).
Mazor, Y., Van Blarcom, T., Mabry, R., Iverson, B. L. & Georgiou, G. Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli. Nat. Biotechnol. 25, 563–565 (2007).
Mazor, Y., Van Blarcom, T., Iverson, B. L. & Georgiou, G. E-clonal antibodies: selection of full-length IgG antibodies using bacterial periplasmic display. Nat. Protoc. 3, 1766–1777 (2008).
Mazor, Y., Van Blarcom, T., Carroll, S. & Georgiou, G. Selection of full-length IgGs by tandem display on filamentous phage particles and Escherichia coli fluorescence-activated cell sorting screening. FEBS J. 277, 2291–2303 (2010).
Rakestraw, J. A., Aird, D., Aha, P. M., Baynes, B. M. & Lipovsek, D. Secretion-and-capture cell-surface display for selection of target-binding proteins. Protein Eng. Des. Sel. 24, 525–530 (2011).
Rhiel, L. et al. REAL-Select: full-length antibody display and library screening by surface capture on yeast cells. PLoS ONE 9, e114887 (2014).
Shaheen, H. H. et al. A dual-mode surface display system for the maturation and production of monoclonal antibodies in glyco-engineered Pichia pastoris. PLoS ONE 8, e70190 (2013).
Zhou, C., Jacobsen, F. W., Cai, L., Chen, Q. & Shen, W. D. Development of a novel mammalian cell surface antibody display platform. MAbs 2, 508–518 (2010).
Georgiou, G. Analysis of large libraries of protein mutants using flow cytometry. Adv. Protein Chem. 55, 293–315 (2000).
Lee, P. A., Tullman-Ercek, D. & Georgiou, G. The bacterial twin-arginine translocation pathway. Annu. Rev. Microbiol. 60, 373–395 (2006).
Robinson, M. P. et al. Efficient expression of full-length antibodies in the cytoplasm of engineered bacteria. Nat. Commun. 6, 8072 (2015).
Lobstein, J. et al. SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm. Micro. Cell Fact. 11, 56 (2012).
DeLisa, M. P., Tullman, D. & Georgiou, G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl Acad. Sci. USA 100, 6115–6120 (2003).
Fisher, A. C., Kim, W. & DeLisa, M. P. Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway. Protein Sci. 15, 449–458 (2006).
Stanley, N. R. et al. Behaviour of topological marker proteins targeted to the Tat protein transport pathway. Mol. Microbiol. 43, 1005–1021 (2002).
Hicks, M. G., Lee, P. A., Georgiou, G., Berks, B. C. & Palmer, T. Positive selection for loss-of-function tat mutations identifies critical residues required for TatA activity. J. Bacteriol. 187, 2920–2925 (2005).
Lee, H. C., Portnoff, A. D., Rocco, M. A. & DeLisa, M. P. An engineered genetic selection for ternary protein complexes inspired by a natural three-component hitchhiker mechanism. Sci. Rep. 4, 7570 (2014).
Rodrigue, A., Chanal, A., Beck, K., Muller, M. & Wu, L. F. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway. J. Biol. Chem. 274, 13223–13228 (1999).
Waraho, D. & DeLisa, M. P. Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism. Proc. Natl Acad. Sci. USA 106, 3692–3697 (2009).
Otrelo-Cardoso, A. R. et al. Structural data on the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli: SAXS and preliminary X-ray crystallography analysis. Int. J. Mol. Sci. 15, 2223–2236 (2014).
Rayner, L. E. et al. The solution structures of two human IgG1 antibodies show conformational stability and accommodate their C1q and FcgammaR ligands. J. Biol. Chem. 290, 8420–8438 (2015).
Jermutus, L., Honegger, A., Schwesinger, F., Hanes, J. & Pluckthun, A. Tailoring in vitro evolution for protein affinity or stability. Proc. Natl Acad. Sci. USA 98, 75–80 (2001).
Fujiwara, K. et al. A single-chain antibody/epitope system for functional analysis of protein-protein interactions. Biochemistry 41, 12729–12738 (2002).
der Maur, A. A. et al. Direct in vivo screening of intrabody libraries constructed on a highly stable single-chain framework. J. Biol. Chem. 277, 45075–45085 (2002).
Cristobal, S., de Gier, J. W., Nielsen, H. & von Heijne, G. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18, 2982–2990 (1999).
Xu, J. L. & Davis, M. M. Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities. Immunity 13, 37–45 (2000).
Ye, J., Ma, N., Madden, T. L. & Ostell, J. M. IgBLAST: an immunoglobulin variable domain sequence analysis tool. Nucleic Acids Res. 41, W34–W40 (2013).
Niman, H. L. et al. Generation of protein-reactive antibodies by short peptides is an event of high frequency: implications for the structural basis of immune recognition. Proc. Natl Acad. Sci. USA 80, 4949–4953 (1983).
Waraho-Zhmayev, D., Meksiriporn, B., Portnoff, A. D. & DeLisa, M. P. Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selection. Protein Eng. Des. Sel. 27, 351–358 (2014).
Meksiriporn, B. et al. A survival selection strategy for engineering synthetic binding proteins that specifically recognize post-translationally phosphorylated proteins. Nat. Commun. 10, 1830 (2019).
Koch, H., Grafe, N., Schiess, R. & Pluckthun, A. Direct selection of antibodies from complex libraries with the protein fragment complementation assay. J. Mol. Biol. 357, 427–441 (2006).
Mossner, E., Koch, H. & Pluckthun, A. Fast selection of antibodies without antigen purification: adaptation of the protein fragment complementation assay to select antigen-antibody pairs. J. Mol. Biol. 308, 115–122 (2001).
Lofdahl, P. A., Nord, O., Janzon, L. & Nygren, P. A. Selection of TNF-alpha binding affibody molecules using a beta-lactamase protein fragment complementation assay. N. Biotechnol. 26, 251–259 (2009).
Lofdahl, P. A. & Nygren, P. A. Affinity maturation of a TNFalpha-binding affibody molecule by Darwinian survival selection. Biotechnol. Appl. Biochem. 55, 111–120 (2010).
Secco, P. et al. Antibody library selection by the {beta}-lactamase protein fragment complementation assay. Protein Eng. Des. Sel. 22, 149–158 (2009).
Lee, C. V., Sidhu, S. S. & Fuh, G. Bivalent antibody phage display mimics natural immunoglobulin. J. Immunol. Methods 284, 119–132 (2004).
Sazinsky, S. L. et al. Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors. Proc. Natl Acad. Sci. USA 105, 20167–20172 (2008).
Jung, S. T. et al. Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells. Proc. Natl Acad. Sci. USA 107, 604–609 (2010).
El Debs, B., Utharala, R., Balyasnikova, I. V., Griffiths, A. D. & Merten, C. A. Functional single-cell hybridoma screening using droplet-based microfluidics. Proc. Natl Acad. Sci. USA 109, 11570–11575 (2012).
Koster, S. et al. Drop-based microfluidic devices for encapsulation of single cells. Lab Chip 8, 1110–1115 (2008).
Akbari, S. & Pirbodaghi, T. A droplet-based heterogeneous immunoassay for screening single cells secreting antigen-specific antibodies. Lab Chip 14, 3275–3280 (2014).
Fang, Y., Chu, T. H., Ackerman, M. E. & Griswold, K. E. Going native: Direct high throughput screening of secreted full-length IgG antibodies against cell membrane proteins. MAbs 9, 1253–1261 (2017).
Mettler Izquierdo, S. et al. High-efficiency antibody discovery achieved with multiplexed microscopy. Microscopy 65, 341–352 (2016).
Powell, K. T. & Weaver, J. C. Gel microdroplets and flow cytometry: rapid determination of antibody secretion by individual cells within a cell population. Biotechnology 8, 333–337 (1990).
Guzman, L. M., Belin, D., Carson, M. J. & Beckwith, J. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121–4130 (1995).
Cox, E. C. et al. Antibody-mediated endocytosis of polysialic acid enables intracellular delivery and cytotoxicity of a glycan-directed antibody-drug conjugate. Cancer Res. 79, 1810–1821 (2019).
- SEO Powered Content & PR Distribution. Get Amplified Today.
- EVM Finance. Unified Interface for Decentralized Finance. Access Here.
- Quantum Media Group. IR/PR Amplified. Access Here.
- PlatoAiStream. Web3 Data Intelligence. Knowledge Amplified. Access Here.
- Source: https://www.nature.com/articles/s41467-023-39178-x
