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Selection and Application of Human Single Chain Fv Antibody Fragments from a Semi-synthetic Phage Antibody Display Library with Designed CDR3 Regions
Abstract
We have constructed a large (3.6 x 10(8) clones) phage display library of human single chain Fv (scFv) antibody fragments by combining 49 germline VH genes with synthetic heavy chain CDR3 (HCDR3) regions and seven light chains. The HCDR3 regions varied in length between 6 and 15 residues and were designed to contain fully randomized stretches of amino acid residues flanked by regions of limited residue variability that were composed of amino acid residues that frequently occur in natural antibodies. We reasoned that this approach would increase the frequency of functional molecules in our library and, in addition, permit us to efficiently utilize available cloning space. By direct selection on solid phase-bound antigens we obtained phage antibodies with binding activities to 13 different antigens, including Von Willebrand factor, the DNA-binding HMG box of transcription factor TCF-1 and the tumor antigen EGP-2. In addition, we applied a competitive selection procedure to target phage antibodies to the desired portion of a recombinant fusion protein and to select phage antibodies capable of discriminating between the two highly homologous homeobox proteins PBX1a and PBX2. The functional capacity of monoclonal phage antibodies was assessed in immuno-histochemical staining of tissue specimens. Western blotting assays and immunofluorescent analysis of cells by flow cytometry. The results demonstrate that this large human phage antibody library contains a broad assortment of binding specificities that can be applied in a variety of biochemical assays.
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“Due to their central role in antigen recognition and binding, CDR loops undergo the most extensive engineering during development of monoclonal antibody (mAb) therapeutics [36, 37].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [37]
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Vaughan, T. J., Williams, A. J., Pritchard, K., Osbourn, J. K., Pope, A. R., Earnshaw, J. C., McCafferty, J., Hodits, R. A., Wilton, J., & Johnson, K. S. (1996) · Nature Biotechnology · doi:10.1038/nbt0396-309 · Cited by 1,039
Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wölle, J., Plückthun, A., & Virnekäs, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3444 · Cited by 728
“Furthermore, sets of V H genes extended with PCR primers that encode CDR-H3 libraries have been combined with a single V L gene (Nissim et al., 1994), or a limited set of V L genes (De Kruif et al., 1995), or a randomized repertoire of V L genes (Grif®ths et al., 1994).”
BackgroundMethodter Meulen, J., van den Brink, E. N., Poon, L. L. M., Marissen, W. E., Leung, C. S.-W., Cox, F., Cheung, C. Y., Bakker, A. Q., Bogaards, J. A., van Deventer, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030237 · Cited by 599
Self-citationSheets, M. D., Amersdorfer, P., Finnern, R., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6157 · Cited by 438
Recombining germline-derived CDR sequences for creating diverse single-framework antibody libraries
Söderlind, E., Strandberg, L., Jirholt, P., Kobayashi, N., Alexeiva, V., Åberg, A.-M., Nilsson, A., Jansson, B., Ohlin, M., Wingren, C., et al. (2000) · Nature Biotechnology · doi:10.1038/78458 · Cited by 337
Exploiting recombination in single bacteria to make large phage antibody libraries
Sblattero, D., & Bradbury, A. M. (2000) · Nature Biotechnology · doi:10.1038/71958 · Cited by 317
“Discussion Although phage antibody libraries have been used to isolate antibodies against a large number of antigen”
MethodAntibodies from phage antibody libraries
Bradbury, A. M., & Marks, J. D. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.04.007 · Cited by 297
Improving antibody affinity by mimicking somatic hypermutation in vitro
Chowdhury, P. S., & Pastan, I. H. (1999) · Nature Biotechnology · doi:10.1038/9872 · Cited by 256
Strategies for selection of antibodies by phage display
Griffiths, A. D., & Duncan, A. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80092-x · Cited by 250
Rothe, C., Urlinger, S., Löhning, C., Prassler, J., Stark, Y., Jäger, U., Hubner, B., Bardroff, M., Pradel, I., Boß, M., et al. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.018 · Cited by 248
Bakker, A. B. H., van den Oudenrijn, S., Bakker, A. Q., Feller, N., van Meijer, M., Bia, J. A., Jongeneelen, M. A. C., Visser, T., Bijl, N., Geuijen, C. A. W., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1659 · Cited by 247
“antibody phage display library described previously (10) that was rescued”
BackgroundSelf-citationLee, C. V., Liang, W., Dennis, M. S., Eigenbrot, C. W., Sidhu, S. S., & Fuh, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.051 · Cited by 228
Computational approaches to therapeutic antibody design: established methods and emerging trends
Norman, R. A., Ambrosetti, F., Bonvin, A. M. J. J., Colwell, L. J., Kelm, S., Kumar, S., & Krawczyk, K. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbz095 · Cited by 219
“during development of monoclonal antibody (mAb) therapeutics [36, 37].”
BackgroundMaynard, J. A., & Georgiou, G. (2000) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.2.1.339 · Cited by 219
Ravn, U., Gueneau, F., Bærlocher, L., Østerås, M., Desmurs, M., Malinge, P., Magistrelli, G., Farinelli, L., Kosco‐Vilbois, M. H., & Fischer, N. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq789 · Cited by 172
Phage-displayed Antibody Libraries of Synthetic Heavy Chain Complementarity Determining Regions
Sidhu, S. S., Li, B., Chen, Y., Fellouse, F. A., Eigenbrot, C. W., & Fuh, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.050 · Cited by 172
Antibody Engineering for the Development of Therapeutic Antibodies
Kim, S. J., Park, Y.-W., & Hong, H. J. (2005) · Molecules and Cells · doi:10.1016/s1016-8478(23)25245-0 · Cited by 167
Prassler, J., Thiel, S., Pracht, C., et al. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.08.012 · Cited by 165
Ponsel, D., Neugebauer, J. K., Ladetzki-Baehs, K., & Tissot, K. (2011) · Molecules · doi:10.3390/molecules16053675 · Cited by 164
Persic, L., Roberts, A., Wilton, J., Cattaneo, A., Bradbury, A. M., & Hoogenboom, H. R. (1997) · Gene · doi:10.1016/s0378-1119(96)00628-2 · Cited by 163
van den Brink, E. N., ter Meulen, J., Cox, F., Jongeneelen, M. A. C., Thijsse, A., Throsby, M., Marissen, W. E., Rood, P. M. L., Bakker, A. B. H., Gelderblom, H. R., et al. (2005) · Journal of Virology · doi:10.1128/jvi.79.3.1635-1644.2005 · Cited by 156
“libraries and technology, essentially as described previously (8).”
BackgroundSelf-citationSalvatore, G., Beers, R., Margulies, I., Kreitman, R. J., & Pastan, I. H. (2002) · PubMed · Cited by 153
A general method for greatly improving the affinity of antibodies by using combinatorial libraries
Rajpal, A., Beyaz, N., Haber, L., Cappuccilli, G., Yee, H., Bhatt, R. R., Takeuchi, T., Lerner, R. A., & Crea, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503543102 · Cited by 155
A compact phage display human scFv library for selection of antibodies to a wide variety of antigens
Pansri, P., Jaruseranee, N., Rangnoi, K., et al. (2009) · BMC Biotechnology · doi:10.1186/1472-6750-9-6 · Cited by 149
“Amplification using these non-specific primers has been shown to be as efficient as using germline, VH, IgG or IgM, specific primers for the construction of efficient naïve repertoires [13,48].”
Generating improved single-chain Fv molecules for tumor targeting
Adams, G. P., & Schier, R. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00161-1 · Cited by 146
Phage versus Phagemid Libraries for Generation of Human Monoclonal Antibodies
O’Connell, D. J., Becerril, B., Roy‐Burman, A., et al. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00561-2 · Cited by 141
Mating antibody phage display with proteomics
Hust, M. (2003) · Trends in biotechnology · doi:10.1016/j.tibtech.2003.10.011 · Cited by 131
The use of recombinant antibodies in proteomics
Holt, L. J., Enever, C., de Wildt, R. M. T., et al. (2000) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00133-6 · Cited by 130
Rauchenberger, R., Borges, E., Thomassen-Wolf, E., Rom, E., Adar, R., Yaniv, Y., Malka, M., Chumakov, I., Kotzer, S., Resnitzky, D., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303164200 · Cited by 127
By-passing selection: direct screening for antibody-antigen interactions using protein arrays
Holt, L. J. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.15.e72 · Cited by 123
Synthetic antibodies: Concepts, potential and practical considerations
Miersch, S., & Sidhu, S. S. (2012) · Methods · doi:10.1016/j.ymeth.2012.06.012 · Cited by 123
Ho, M., Kreitman, R. J., Onda, M., & Pastan, I. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409783200 · Cited by 114
Geuijen, C. A. W., Tacken, P. J., Wang, L.-C., Klooster, R., van Loo, P. F., Zhou, J., Mondal, A., Liu, Y.-B., Kramer, A., Condamine, T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24767-5 · Cited by 114
Self-citationTowards proteome-wide production of monoclonal antibody by phage display
Liu, B., Huang, L., Sihlbom, C., et al. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5276 · Cited by 110
Geuijen, C. A. W., Nardis, C. D., Maussang, D., Rovers, E., Gallenne, T., Hendriks, L. J. A., Visser, T., Nijhuis, R., Logtenberg, T., de Kruif, J., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.04.003 · Cited by 108
Self-citation[29] Design and use of phage display libraries for the selection of antibodies and enzymes
Viti, F., Nilsson, F. Y., Demartis, S., et al. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)26071-0 · Cited by 108
The use of phage display for the development of tumour targeting agents
Nilsson, F. Y., Tarli, L., Viti, F., & Neri, D. (2000) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(00)00068-5 · Cited by 106
Detection of biological threats. A challenge for directed molecular evolution
Petrenko, V. A., & Sorokulova, I. B. (2004) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2004.04.004 · Cited by 104
Phage antibody display libraries: a powerful antibody discovery platform for immunotherapy
Zhao, A., Tohidkia, M. R., Siegel, D. L., et al. (2014) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2014.958978 · Cited by 103
“The source of V-genes for introducing diversity to this library can be: (a) un-rearranged germline V-genes (Akamatsu et al., 1993; de Kruif et al., 1995; Griffiths et al., 1994; Hoogenboom & Winter, 1992; Nissim et al., 1994), (b) in vivo rearranged V-genes from immune and/or non-immune donors…”
BackgroundBond, C. J., Marsters, J. C., & Sidhu, S. S. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00967-7 · Cited by 101
Kramer, R. A., Marissen, W. E., Goudsmit, J., Visser, T., der Horst, M. C.-V., Bakker, A. Q., de Jong, M., Jongeneelen, M. A. C., Thijsse, S., Backus, H. H. J., et al. (2005) · European Journal of Immunology · doi:10.1002/eji.200526134 · Cited by 97
Self-citationEliminating helper phage from phage display
Chasteen, L., Ayriss, J. E., Pavlik, P., et al. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl772 · Cited by 96
Huls, G. A., Heijnen, I., Cuomo, M. E., Koningsberger, J. C., Wiegman, L., Boel, E. C. H., de Vries, A.-R. V. D. V., Loyson, S. A. J., Helfrich, W., Henegouwen, G. P. V. B., et al. (1999) · Nature Biotechnology · doi:10.1038/7023 · Cited by 95
“A semisynthetic antibody library of human scFv fragments similar to that described previousl”
MethodSelf-citationDiagnostic Probes for Bacillus anthracis Spores Selected from a Landscape Phage Library
Brigati, J. R., Williams, D. D., Sorokulova, I. B., et al. (2004) · Clinical Chemistry · doi:10.1373/clinchem.2004.038018 · Cited by 94
de Kruif, J., & Logtenberg, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7630 · Cited by 93
“…by Ficoll-Hypaque density centrifugation and stained with clone 35 scFv and Fos-linked clone 35 (scFv)2 proteins using the anti-Myc monoclonal antibody and a phycoerythrin-conjugated goat anti-mouse IgG polyclonal antibody as second and third step reagents as described (de Kruif et al., 1995b).”
BackgroundMethodInfluentialSelf-citationvan Ewijk, W., de Kruif, J., Germeraad, W. T. V., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3903 · Cited by 90
Self-citationThe role of phage display in therapeutic antibody discovery
Chan, C. E. Z., Lim, A. P. C., MacAry, P. A., & Hanson, B. J. (2014) · International Immunology · doi:10.1093/intimm/dxu082 · Cited by 87
Isolation and affinity maturation of hapten-specific antibodies
Sheedy, C., MacKenzie, C. R., & Hall, J. C. (2007) · Biotechnology Advances · doi:10.1016/j.biotechadv.2007.02.003 · Cited by 87
Kehoe, J. W., Velappan, N., Walbolt, M., Rasmussen, J., King, D., Lou, J., Knopp, K. A., Pavlik, P., Marks, J. D., Bertozzi, C. R., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600314-mcp200 · Cited by 87
Generation of Recombinant Antibodies
Kipriyanov, S. M., & Little, M. (1999) · Molecular Biotechnology · doi:10.1385/mb:12:2:173 · Cited by 80
Hayden, M. S., Gilliland, L. K., & Ledbetter, J. A. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80136-7 · Cited by 82
Recombinant monoclonal antibody technology
Siegel, D. L. (2002) · Transfusion Clinique et Biologique · doi:10.1016/s1246-7820(01)00210-5 · Cited by 77
Boel, E. C. H., Verlaan, S., Poppelier, M. J. J. G., WESTERDAAL, N. A. C., van Strijp, J. A. G., & Logtenberg, T. (2000) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00170-8 · Cited by 77
Self-citationBeers, R., Chowdhury, P., Bigner, D. D., & Pastan, I. (2000) · PubMed · Cited by 75
Recombinant Antibodies and In Vitro Selection Technologies
Geyer, C. R., McCafferty, J., Dübel, S., Bradbury, A. M., & Sidhu, S. S. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-931-0_2 · Cited by 73
Dunn, I. S. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80060-7 · Cited by 70
Recombinant Antibodies as Therapeutic Agents
Aires‐da‐Silva, F., Côrte‐Real, S., & Gonçalves, J. (2008) · BioDrugs · doi:10.2165/00063030-200822050-00003 · Cited by 68
Creating and engineering human antibodies for immunotherapy
de Haard, H., Henderikx, P., & Hoogenboom, H. R. (1998) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(97)00091-4 · Cited by 65
Katz, B. A. (1997) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.26.1.27 · Cited by 63
“Human Fabs, singlechain antibodies (19, 21, 98), or disulfide-stabilized Fv’s (9) can be isolated with specificities against virtually any targeted antigen, either foreign or self (26, 37), hapten (81), carbohydrate (21, 98), protein, DNA (3), or RNA (72).”
Design of synthetic antibody libraries
Benhar, I. (2007) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.7.5.763 · Cited by 59
Wang, X., Katayama, A., Wang, Y., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-1134 · Cited by 58
Kramer, R. A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gng058 · Cited by 58
“peripheral blood cells (pHEN-BG and pHEN-BT) (5,6).”
BackgroundMethodInfluentialMining human antibody repertoires
Beerli, R. R., & Rader, C. M. (2010) · mAbs · doi:10.4161/mabs.12187 · Cited by 57
Geuijen, C. A. W., Bijl, N., Smit, R., et al. (2004) · European Journal of Cancer · doi:10.1016/j.ejca.2004.10.008 · Cited by 57
Self-citationAntibody-mediated resistance against plant pathogens
Safarnejad, M. R., Jouzani, G. S., Tabatabaie, M., et al. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.08.011 · Cited by 52
Mersmann, M., Schmidt, A., Rippmann, J. F., W�est, T., Brocks, B., Rettig, W. J., Garin‐Chesa, P., Pfizenmaier, K., & Moosmayer, D. (2001) · International Journal of Cancer · doi:10.1002/1097-0215(200102)9999:9999 · Cited by 52
Phage Display Vectors for the In Vitro Generation of Human Antibody Fragments
Hust, M., & DUBEL, S. J. (2005) · Humana Press eBooks · doi:10.1385/1-59259-873-0:071 · Cited by 50
In vivo selection of sFv from phage display libraries
Johns, M. S., George, A. J. T., & Ritter, M. A. (2000) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00152-6 · Cited by 49
Recombinant antibodies by phage display for bioanalytical applications
Guliy, O. I., Евстигнеева, С. С., & Dykman, L. A. (2022) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2022.114909 · Cited by 48
Викторовна, Т. Н., & Витальевна, М. В. (2009) · Acta Naturae · doi:10.32607/20758251-2009-1-3-20-28 · Cited by 57
An overview on application of phage display technique in immunological studies
Rami, A., Behdani, M., Yardehnavi, N., et al. (2017) · Asian Pacific Journal of Tropical Biomedicine · doi:10.1016/j.apjtb.2017.06.001 · Cited by 44
Lim, C. C., Choong, Y. S., & Lim, T. S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081861 · Cited by 44
“6 × 108 DNP, TTX, GBS, SpA, HMG, IgG, Tg, VWF, A2, ICAM-1, δEGP-2, BLT1, PBX1a μM–nM [113] Tomlinson I+J scFv H, 1 VH/1 Vκ 1.”
Construction of a semisynthetic antibody library using trinucleotide oligos
Braunagel, M. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.22.4690 · Cited by 42
Barbas, C. F. (1995) · Nature Medicine · doi:10.1038/nm0895-837 · Cited by 41
Mazor, Y., Blarcom, T. J. V., Carroll, S., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07645.x · Cited by 40
Geuijen, C. A. W., der Horst, M. C.-V., Cox, F., et al. (2005) · Journal of Immunological Methods · doi:10.1016/j.jim.2005.04.016 · Cited by 39
Self-citationGeneration of stable cell clones expressing mixtures of human antibodies
de Kruif, J., Kramer, A., Nijhuis, R., der Zande, V. Z.-V., den Blanken-Smit, R., Clements, C., Visser, T., Keehnen, R., den Hartog, M., Throsby, M., et al. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22763 · Cited by 38
Self-citationMcCafferty, J., & Schofield, D. J. (2015) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2015.01.003 · Cited by 37
Changes in the specificity of antibodies by site-specific mutagenesis followed by random mutagenesis
Miyazaki, C., Iba, Y., Yamada, Y., et al. (1999) · Protein Engineering Design and Selection · doi:10.1093/protein/12.5.407 · Cited by 35
“Since the development of PCR technology and phagedisplay systems, several groups have reported the construction of libraries of phage antibodies (Griffithset al., 1994; de Kruif et al., 1995; Vaughanet al., 1996).”
BackgroundGraus, Y., Verschuuren, J. J. G. M., Degenhardt, A., Vriesman, P. J. C. V. B., Baets, M. H. D., Posner, J. B., Burton, D. R., & Dalmau, J. O. (1998) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00199-9 · Cited by 33
van Esch, W. J. E., Reparon‐Schuijt, C. C., Hamstra, H.-J., van Kooten, C., Logtenberg, T., Breedveld, F. C., & Verweij, C. L. (2003) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.2003.02068.x · Cited by 33
Self-citationNew perspectives on recombinant human antibodies
de Kruif, J., de Vries, A.-R. V. D. V., Clienti, L., et al. (1996) · Immunology Today · doi:10.1016/0167-5699(96)30057-y · Cited by 33
Self-citationA fully human scFv phage display library for rapid antibody fragment reformatting
Li, K., Zettlitz, K. A., Lipianskaya, J., et al. (2015) · Protein Engineering Design and Selection · doi:10.1093/protein/gzv024 · Cited by 32
“ScFvs typically produce well in bacterial systems and are the preferred format for many antibody phage display libraries (de Kruif et al., 1995; Sheets et al., 1998; Okamoto et al., 2004; Wajanarogana et al., 2006).”
BackgroundGennari, F., Mehta, S., Wang, Y., et al. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.073 · Cited by 32
de Kruif, J., Storm, G., van Bloois, L., & Logtenberg, T. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01335-x · Cited by 30
Self-citationA model phage display subtraction method with potential for analysis of differential gene expression
Stausbøl‐Grøn, B., Wind, T., Kjær, S., et al. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00703-x · Cited by 31
Kaleli, N. E., Karadag, M., & Kalyoncu, S. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25685 · Cited by 29
“HCDR3 has therefore been the initial target for introduction of diversity in synthetic libraries as it has been shown in many different prior studies.(31,32) Besides affinity, composition of CDR loops have a significant influence on the specificity and biophysical characteristics of an antibody.”
Velappan, N., Martinez, J. S., Valero, R., et al. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.01.011 · Cited by 30
Selection of antibodies from synthetic antibody libraries
Inbar, N. H., & Benhar, I. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.12.028 · Cited by 31
Wang, X., Campoli, M. R., Ko, E. C., et al. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.08.005 · Cited by 30
Looking for therapeutic antibodies in next generation sequencing repositories
Krawczyk, K., Raybould, M., Kovaltsuk, A., & Deane, C. M. (2019) · doi:10.1101/572958 · Cited by 29
Method for generation of human hyperdiversified antibody fragment library
Mondon, P., Souyris, N., Douchy, L., Crozet, F., Bouayadi, K., & Kharrat, H. (2007) · Biotechnology Journal · doi:10.1002/biot.200600205 · Cited by 29
Recombinant lipid-tagged antibody fragments as functional cell-surface receptors
de Kruif, J., Tijmensen, M., Goldsein, J., et al. (2000) · Nature Medicine · doi:10.1038/72339 · Cited by 29
Self-citationLekkerkerker, A., & Logtenberg, T. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00140-4 · Cited by 29
Self-citationBoel, E. C. H., Bootsma, H. J., de Kruif, J., et al. (1998) · Infection and Immunity · doi:10.1128/iai.66.1.83-88.1998 · Cited by 26
“All sequences are derived from primer CR9A, one of the partially randomized oligonucleotides used to create diversity in CDR3 (8).”
BackgroundMethodInfluentialSelf-citationHust, M., Thie, H., Schirrmann, T., & Dübel, S. (2009) · doi:10.1002/9780470485408.ch8 · Cited by 25
Venet, S., Ravn, U., Buatois, V., Gueneau, F., Calloud, S., Kosco‐Vilbois, M. H., & Fischer, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043471 · Cited by 24
Letchford, J., Cardwell, A., Stewart, K., et al. (2005) · Journal of Immunological Methods · doi:10.1016/j.jim.2005.10.015 · Cited by 24
Directed Evolution of Nucleotide-Based Libraries Using Lambda Exonuclease
Lim, B. N., Choong, Y. S., Ismail, A., et al. (2012) · BioTechniques · doi:10.2144/000113964 · Cited by 22
“CDR regions vary from 3 to 12 amino acids in length (37, 38), depending on their location along the antibody sequence.”
BackgroundMao, H., Graziano, J. J., Chase, T. M. A., Bentley, C. A., Bazirgan, O. A., Reddy, N. P., Song, B. D., & Smider, V. V. (2010) · Nature Biotechnology · doi:10.1038/nbt.1694 · Cited by 22
Metadata
- Authors
- de Kruif, J., Boel, E., & Logtenberg, T.
- Affiliations
- Utrecht University (NL)
- Corresponding author
- Logtenberg, Ton
- ORCID
- Boel, Edwin
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1995-04
- Volume
- 248
- Issue
- 1
- Pages
- 97-105
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2091855294
- Cited by
- 173
- References
- 0
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2019: 5 · 2018: 2 · 2017: 1 · 2015: 3 · 2014: 4 · 2013: 1 · 2012: 7
- FWCI
- 10.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- phage display library, human antibody fragments, competitive selection, von Willebrand factor, PBX2, homeodomain transcription factor, monoclonal antibodies
- MeSH terms
- Amino Acid Sequence, Animals, Haplorhini, Antibodies, Monoclonal, Bacteriophages, Base Sequence, Cell Line, Transformed, Cloning, Molecular, DNA-Binding Proteins, Herpesvirus 4, Human, Fluorescent Antibody Technique, Humans, Immunoglobulin Fragments, Immunoglobulin Fab Fragments, Molecular Sequence Data, Plasmids, Thyroid Gland, Blotting, Western, Gene Library, Receptor-CD3 Complex, Antigen, T-Cell, Sequence Homology, Amino Acid, DNA Primers, Intercellular Adhesion Molecule-1, Macromolecular Substances
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