A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity.

Mack, M; Riethmüller, G; Kufer, P

doi:10.1073/pnas.92.15.7021

Cited by 351Monoclonal and Polyclonal Antibodies ResearchToxin Mechanisms and ImmunotoxinsProtein purification and stability

A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity.

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Mack, M, Riethmüller, G, Kufer, P·1995·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.92.15.7021PMC PMC41463

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Abstract

Construction of a bispecific single-chain antibody derivative is described that consists of two different single-chain Fv fragments joined through a Gly-Ser linker. One specificity of the two Fv fragments is directed against the CD3 antigen of human T cells and the other is directed against the epithelial 17-1A antigen; the latter had been found in a clinical trial to be a suitable target for antibody therapy of minimal residual colorectal cancer. The construct could be expressed in CHO cells as a fully functional protein, while its periplasmic expression in Escherichia coli resulted in a nonfunctional protein only. The antigen-binding properties of the bispecific single-chain antibody are indistinguishable from those of the corresponding univalent single-chain Fv fragments. By redirecting human peripheral T lymphocytes against 17-1A-positive tumor cells, the bispecific antibody proved to be highly cytotoxic at nanomolar concentrations as demonstrated by 51Cr release assay on various cell lines. The described bispecific construct has a molecular mass of 60 kDa and can be easily purified by its C-terminal histidine tail on a Ni-NTA chromatography column. As bispecific antibodies have already been shown to be effective in vivo in experimental tumor systems as well as in phase-one clinical trials, the small CD3/17-1A-bispecific antibody may be more efficacious than intact antibodies against minimal residual cancer cells.

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This new kind of bispecific antibody proved highly cytotoxic at nanomolar concentrations against various cell lines, using unstimulated human PBMCs in the absence of co-signaling.
“This new kind of bsAb proved to be highly cytotoxic at nanomolar concentrations against various cell lines, using unstimulated human PBMCs in the absence of co-signaling. 44”
From Bispecific antibodies for cancer therapy: The light at the end of the tunnel? (2009) · cites this paper as [44]

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A new method for predicting signal sequence cleavage sites
von HEIJNE, G. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.11.4683 · Cited by 4,554 · see citing works
Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
Pelletier, J., & Sonenberg, N. (1988) · Nature · doi:10.1038/334320a0 · Cited by 1,953 · see citing works
pEF-BOS, a powerful mammalian expression vector
Mizushima, S., & Nagata, S. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.17.5322 · Cited by 1,632 · see citing works
Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.
Huston, J. S., Levinson, D., Mudgett-Hunter, M., Tai, M. S., Novotný, J., Margolies, M. N., Ridge, R. J., Bruccoleri, R. E., Haber, E., & Crea, R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.16.5879 · Cited by 1,594 · see citing works
Single-Chain Antigen-Binding Proteins
Bird, R. E., Hardman, K. D., Jacobson, J. W., Johnson, S., Kaufman, B. M., Lee, S., Lee, T. T., Pope, S. H., Riordan, G. S., & Whitlow, M. D. (1988) · Science · doi:10.1126/science.3140379 · Cited by 1,509 · see citing works
"Diabodies": small bivalent and bispecific antibody fragments.
Holliger, P., Prospero, T. D., & Winter, G. P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6444 · Cited by 879 · see citing works
Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms.
Yokota, T., Milenic, D. E., Whitlow, M. D., & Schlom, J. (1992) · PubMed · Cited by 819 · see citing works
Cloning immunoglobulin variable domains for expression by the polymerase chain reaction.
Orlandi, R., Güssow, D., Jones, P. T., & Winter, G. P. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3833 · Cited by 707 · see citing works
Randomised trial of monoclonal antibody for adjuvant therapy of resected Dukes' C colorectal carcinoma
Riethmüller, G., Gruber, R., Schneider-Gädicke, E., Schlimok, G., Witte, J., Raab, R., Pichlmayr, R., Pichlmaier, H., Schmiegel, W., Buggisch, P., et al. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92398-1 · Cited by 633 · see citing works
Self-citation
Hybrid antibodies can target sites for attack by T cells
Staerz, U. D., Kanagawa, O., & Bevan, M. J. (1985) · Nature · doi:10.1038/314628a0 · Cited by 492 · see citing works
A comparison of strategies to stabilize immunoglobulin Fv-fragments
Glockshuber, R., Malia, M., Pfitzinger, I., & Plückthun, A. (1990) · Biochemistry · doi:10.1021/bi00458a002 · Cited by 473 · see citing works
Specific targeting of cytotoxic T cells by anti-T3 linked to anti-target cell antibody
Perez, P., Hoffman, R. W., Shaw, S., Bluestone, J. A., & Segal, D. M. (1985) · Nature · doi:10.1038/316354a0 · Cited by 337 · see citing works
Preliminary trial of specific targeting therapy against malignant glioma
Nitta, T., Yagita∥, H., Okumura, K., Sato, K., & Ishii, S. (1990) · The Lancet · doi:10.1016/0140-6736(90)90205-j · Cited by 235 · see citing works
The epithelial cell surface antigen 17–1A, a target for antibody‐mediated tumor therapy: Its biochemical nature, tissue distribution and recognition by different monoclonal antibodies
Göitlinger, H. G., Funke, I., Johnson, J. P., Gokel, J. M., & Riethmüller, G. (1986) · International Journal of Cancer · doi:10.1002/ijc.2910380109 · Cited by 233 · see citing works
Self-citation
A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.
Brinkmann, U., Reiter, Y., Jung, S. H., Lee, B., & Pastan, I. H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7538 · Cited by 223 · see citing works
Formation of a bispecific antibody by the use of leucine zippers
Kostelny, S. A., Cole, M. S., & Tso, J. Y. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.5.1547 · Cited by 211 · see citing works
Hybrid hybridoma producing a bispecific monoclonal antibody that can focus effector T-cell activity.
Staerz, U. D., & Bevan, M. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.5.1453 · Cited by 208 · see citing works
The use of hybrid hybridomas to target human cytotoxic T lymphocytes
Lanzavecchia, A., & Scheidegger, D. (1987) · European Journal of Immunology · doi:10.1002/eji.1830170118 · Cited by 198 · see citing works
[42] Selection and coamplification of heterologous genes in mammalian cells
Kaufman, R. J. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85044-o · Cited by 182 · see citing works
Molecular cloning of cDNA for the carcinoma-associated antigen GA733-2.
Szala, S., Froehlich, M., Scollon, M., Kasai, Y., Steplewski, Z., Koprowski, H., & Linnenbach, A. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.9.3542 · Cited by 173 · see citing works
Cure of Xenografted Human Tumors by Bispecific Monoclonal Antibodies and Human T Cells
Renner, C., Jung, W. E., Şahin, U., Denfeld, R. W., Pohl, C., Trümper, L. H. P., Hartmann, F., Diehl, V., van Lier, R. A. W., & Pfreundschuh, M. G. (1994) · Science · doi:10.1126/science.8171337 · Cited by 156 · see citing works
[34] Expression of functional antibody Fv and Fab fragments in Escherichia coli
Plückthun, A., & Skerra, A. (1989) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(89)78036-8 · Cited by 140 · see citing works
Construction, expression, and activity of a bivalent bispecific single-chain antibody.
Mallender, W. D., & Voss, E. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42334-9 · Cited by 122 · see citing works
Adoptive immunotherapy of ovarian carcinoma with bs-MAb-targeted lymphocytes: a multicenter study.
Bolhuis, R. L. H., Lamers, C. H., Goey, S. H., Eggermont, A. M. M., Trimbos, J. B. M. Z., Stoter, G., Lanzavecchia, A., Re, E. D., Miotti, S., & Raspagliesi, F. (1992) · PubMed · Cited by 108 · see citing works
Efficient tumor cell lysis mediated by a bispecific single chain antibody expressed in Escherichia coli.
Gruber, M., Schodin, B. A., Wilson, E. R., & Kranz, D. M. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.11.5368 · Cited by 98 · see citing works
Adhesion receptors in lymphocyte activation
Collins, T. L., Kassner, P. D., Bierer, B. E., & Burakoff, S. J. (1994) · Current Opinion in Immunology · doi:10.1016/0952-7915(94)90117-1 · Cited by 88 · see citing works
Human T cells targeted with anti-T3 cross-linked to antitumor antibody prevent tumor growth in nude mice.
Titus, J. A., Garrido, M. A., Hecht, T. T., Winkler, D. F., Wunderlich, J. R., & Segal, D. M. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.138.11.4018 · Cited by 85 · see citing works
Human T-lymphocytes targeted against an established human ovarian carcinoma with a bispecific F(ab')2 antibody prolong host survival in a murine xenograft model.
Mezzanzanica, D., Garrido, M. A., Neblock, D. S., Daddona, P. E., Andrew, S. M., Zurawski, V. R., Segal, D. M., & Wunderlich, J. R. (1991) · PubMed · Cited by 69 · see citing works
Bispecific anti-idiotype/anti-CD3 antibody therapy of murine B cell lymphoma
Weiner, G. J., & Hillstrom, J. R. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.11.4035 · Cited by 67 · see citing works
Bispecific single chain molecules (Janusins) target cytotoxic lymphocytes on HIV infected cells.
Traunecker, A., Lanzavecchia, A., & Karjalainen, K. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04932.x · Cited by 67 · see citing works
The role of T cell activation in anti-CD3 x antitumor bispecific antibody therapy.
Weiner, G. J., Kostelny, S. A., Hillstrom, J. R., Cole, M. S., Link, B. K., Wang, S. L., & Tso, J. Y. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.5.2385 · Cited by 64 · see citing works
Target cell‐induced T cell activation with bi‐ and trispecific antibody fragments
Jung, G., Freimann, U., von Marschall, Z., Reisfeld, R. A., & Wilmanns, W. (1991) · European Journal of Immunology · doi:10.1002/eji.1830211020 · Cited by 61 · see citing works
Treatment of mice bearing BCL1 lymphoma with bispecific antibodies
Brissinck, J., Demanet, C., Moser, M. A., Léo, O., & Thielemans, K. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.11.4019 · Cited by 56 · see citing works
Cell-mediated cytotoxic mechanisms
Squier, M. K. T., & Cohen, J. (1994) · Current Opinion in Immunology · doi:10.1016/0952-7915(94)90126-0 · Cited by 52 · see citing works
Targeted cytotoxic cells in human peripheral blood lymphocytes.
Garrido, M. A., Perez, P., Titus, J. A., Valdayo, M. J., Winkler, D. F., Barbieri, S. A., Wunderlich, J. R., & Segal, D. M. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.8.2891 · Cited by 49 · see citing works
Human peripheral blood lymphocytes targeted with bispecific antibodies release cytokines that are essential for inhibiting tumor growth
Qian, J. H., Titus, J. A., Andrew, S. M., Mezzanzanica, D., Garrido, M. A., Wunderlich, J. R., & Segal, D. M. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.146.9.3250 · Cited by 49 · see citing works
Trispecific F(ab’)3 derivatives that use cooperative signaling via the TCR/CD3 complex and CD2 to activate and redirect resting cytotoxic T cells
Tutt, A. N. J., Stevenson, G. T., & Glennie, M. J. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.1.60 · Cited by 44 · see citing works
Cytokine Release in an Ovarian Carcinoma Patient Following Intravenous Administration of Bispecific Antibody OC/TR F(ab')2
Tibben, J. G., Boerman, O. C., Claessens, R. A. M. J., Corstens, F. H. M., van Deuren, M., Mulder, P., van der Meer, J. W. M., Keijser, K. G. G., & Massuger, L. F. A. G. (1993) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/85.12.1003 · Cited by 27 · see citing works
Bispecific IgG and IL-2 therapy of a syngeneic B-cell lymphoma in immunocompetent mice.
Weiner, G. J. (1992) · PubMed · Cited by 9 · see citing works

Flagged first, then by citations

Research works printed but not linked: 6

[9]Staerz, U. D. & Bevan, M. J. (1986) Proc. Natl. Acad. Sci. USA 83, 1453–1457.
[13]Hollinger, P., Prospero, T. & Winter, G. (1993) Proc. Natl. Acad. Sci. USA 90, 6444–6448.
[16]Huston, J. S., Levinson, D., Mudgett-Hunter, M., Tai, M.-S., Novotny, J., Margolies, M. N., Ridge, R. J., Bruccoleri, R. E., Haber, E., Crea, R. & Oppermann, H. (1988) Proc. Natl. Acad. Sci. USA 85, 5879–5883.
[18]Orlandi, R., Güssow, D. H., Jones, P. T. & Winter, G. (1989) Proc. Natl. Acad. Sci. USA 86, 3833–3837.
[25]Szala, S., Froehlich, M., Scollon, M., Kasai, Y., Steplewski, Z., Koprowsky, H. & Linnebach, A. J. (1990) Proc. Natl. Acad. Sci. USA 87, 3542–3564.
[30]Brinkmann, U., Reiter, Y., Jung, S., Lee, B. & Pastan, I. (1993) Proc. Natl. Acad. Sci. USA 90, 7538–7542.

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Self-citation
Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10
Klein, J. S., Gnanapragasam, P. N. P., Galimidi, R. P., Foglesong, C. P., West, A. P., & Björkman, P. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811427106 · Cited by 156 · see citing works
Insight to drug delivery aspects for colorectal cancer
Gulbake, A. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i2.582 · Cited by 152 · see citing works
Efficient elimination of chronic lymphocytic leukaemia B cells by autologous T cells with a bispecific anti-CD19/anti-CD3 single-chain antibody construct
Löffler, A., Gruen, M., Wuchter, C., Schriever, F., Kufer, P., Dreier, T., Hanakam, F., Baeuerle, P. A., Bommert, K., Karawajew, L., et al. (2003) · Leukemia · doi:10.1038/sj.leu.2402890 · Cited by 150 · see citing works
Self-citation
Treatment of Refractory Hodgkin's Disease With an Anti-CD16/CD30 Bispecific Antibody
Hartmann, F., Renner, C., Jung, W., Deisting, C., Juwana, M., Eichentopf, B., Kloft, M., & Pfreundschuh, M. (1997) · Blood · doi:10.1182/blood.v89.6.2042 · Cited by 149 · see citing works
Targeting of adenoviral vectors through a bispecific single-chain antibody
Haisma, H. J., Grill, J., Curiel, D. T., Hoogeland, S., van Beusechem, V. W., Pinedo, H. M., & Gerritsen, W. R. (2000) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7700198 · Cited by 147 · see citing works
Developments and Challenges for mAb-Based Therapeutics
Goswami, S., Wang, W., Arakawa, T., & Ohtake, S. (2013) · Antibodies · doi:10.3390/antib2030452 · Cited by 144 · see citing works
The coming of age of engineered multivalent antibodies
Nuñez‐Prado, N., Compte, M., Harwood, S. L., Álvarez-Méndez, A., Lykkemark, S., Sanz, L., & Álvarez‐Vallina, L. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.02.013 · Cited by 136 · see citing works
Bispecific T-Cell Redirection versus Chimeric Antigen Receptor (CAR)-T Cells as Approaches to Kill Cancer Cells
Strohl, W. R., & Naso, M. F. (2019) · Antibodies · doi:10.3390/antib8030041 · Cited by 136 · see citing works
Multiple Active States and Oligomerization of CCR5 Revealed by Functional Properties of Monoclonal Antibodies
Blanpain, C., Vanderwinden, J., Cihak, J., Wittamer, V., Poul, E. L., Issafras, H., Stangassinger, M., Vassart, G., Marullo, S., Schlöndorff, D., et al. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-03-0129 · Cited by 135 · see citing works
Self-citation
Pediatric posttransplant relapsed/refractory B-precursor acute lymphoblastic leukemia shows durable remission by therapy with the T-cell engaging bispecific antibody blinatumomab
Schlegel, P., Lang, P., Zugmaier, G., Ebinger, M., Kreyenberg, H., Witte, K., Feucht, J., Pfeiffer, M. M., Teltschik, H., Kyzirakos, C., et al. (2014) · Haematologica · doi:10.3324/haematol.2013.100073 · Cited by 133 · see citing works
A tetravalent bispecific TandAb (CD19/CD3), AFM11, efficiently recruits T cells for the potent lysis of CD19 + tumor cells
Reusch, U., Duell, J., Ellwanger, K., Herbrecht, C., Knackmuss, S. H. J., Fucek, I., Eser, M., McAleese, F., Molkenthin, V., Gall, F. L., et al. (2015) · mAbs · doi:10.1080/19420862.2015.1029216 · Cited by 132 · see citing works
Immunology and immunotherapy of colorectal cancer
Dalerba, P. D., Maccalli, C., Casati, C., Castelli, C., & Parmiani, G. (2003) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(02)00159-2 · Cited by 129 · see citing works
Simultaneous targeting of CD44 and EpCAM with a bispecific aptamer effectively inhibits intraperitoneal ovarian cancer growth
Zheng, J., Zhao, S., Yu, X., Huang, S., & Liu, H. Y. (2017) · Theranostics · doi:10.7150/thno.17826 · Cited by 120 · see citing works
Blinatumomab, a Bi-Specific Anti-CD19/CD3 BiTE® Antibody for the Treatment of Acute Lymphoblastic Leukemia: Perspectives and Current Pediatric Applications
Hoffman, L. M., & Gore, L. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00063 · Cited by 116 · see citing works
Expression and characterization of bispecific single‐chain Fv fragments produced in transgenic plants
Fischer, R., Schumann, D., Zimmermann, S., Drossard, J., Sack, M., & Schillberg, S. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00435.x · Cited by 116 · see citing works
Bispecific Minibodies Targeting HER2/neu and CD16 Exhibit Improved Tumor Lysis When Placed in a Divalent Tumor Antigen Binding Format
Shahied, L., Tang, Y., Alpaugh, R. K., Somer, R. A., Greenspon, D., & Weiner, L. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407888200 · Cited by 117 · see citing works
Bispecific Immunomodulatory Antibodies for Cancer Immunotherapy
Blanco, B., Domínguez-Alonso, C., & Álvarez‐Vallina, L. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-3770 · Cited by 116 · see citing works
Multivalency: the hallmark of antibodies used for optimization of tumor targeting by design
Deyev, S. M., & Lebedenko, E. N. (2008) · BioEssays · doi:10.1002/bies.20805 · Cited by 109 · see citing works
Bispecific antibodies and CAR-T cells: dueling immunotherapies for large B-cell lymphomas
Trabolsi, A., Arumov, A., & Schatz, J. (2024) · Blood Cancer Journal · doi:10.1038/s41408-024-00997-w · Cited by 114 · see citing works
Fc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds
Liu, H.-Y., Saxena, A., Sidhu, S., & Wu, D.-H. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00038 · Cited by 109 · see citing works
Targeted BiTE Expression by an Oncolytic Vector Augments Therapeutic Efficacy Against Solid Tumors
Speck, T., Heidbuechel, J. P. W., Veinalde, R., Jaeger, D., Kalle, C. V., Ball, C. R., Ungerechts, G., & Engeland, C. E. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-2651 · Cited by 105 · see citing works
CD19-/CD3-bispecific antibody of the BiTE class is far superior to tandem diabody with respect to redirected tumor cell lysis
Mølhøj, M., Crommer, S., Brischwein, K., Rau, D., Sriskandarajah, M., Hoffmann, P., Kufer, P., Hofmeister, R., & Baeuerle, P. A. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.09.032 · Cited by 104 · see citing works
Self-citation
Translation and Clinical Development of Bispecific T‐cell Engaging Antibodies for Cancer Treatment
Yuraszeck, T. M., Kasichayanula, S., & Benjamin, J. (2017) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.651 · Cited by 100 · see citing works
Novel TCR-based biologics: mobilising T cells to warm ‘cold’ tumours
Lowe, K. L., Cole, D. K., Kenefeck, R., OKelly, I., Lepore, M., & Jakobsen, B. K. (2019) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2019.06.001 · Cited by 94 · see citing works
Leucine Zipper Dimerized Bivalent and Bispecific scFv Antibodies from a Semi-synthetic Antibody Phage Display Library
de Kruif, J., & Logtenberg, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7630 · Cited by 93 · see citing works
A novel asymmetrical anti-HER2/CD3 bispecific antibody exhibits potent cytotoxicity for HER2-positive tumor cells
Yu, S., Zhang, J., Yan, Y., Yao, X., Fang, L., Xiong, H., Liu, Y., Chu, Q., Zhou, P., & Wu, K. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1354-1 · Cited by 92 · see citing works
A sensitivity scale for targeting T cells with chimeric antigen receptors (CARs) and bispecific T-cell Engagers (BiTEs)
Stone, J. D., Aggen, D. H., Schietinger, A., Schreiber, H. W., & Kranz, D. M. (2012) · OncoImmunology · doi:10.4161/onci.20592 · Cited by 92 · see citing works
Immunoglobulin Fc Heterodimer Platform Technology: From Design to Applications in Therapeutic Antibodies and Proteins
Ha, J.-H., Kim, J.-E., & Kim, Y. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00394 · Cited by 92 · see citing works
Therapeutic Window of MuS110, a Single-Chain Antibody Construct Bispecific for Murine EpCAM and Murine CD3
Amann, M., Brischwein, K., Lutterbuese, P., Parr, L., Petersen, L., Lorenczewski, G., Krinner, E., Bruckmeier, S., Lippold, S., Kischel, R., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2182 · Cited by 90 · see citing works
Self-citation
Antibodies and gene therapy: teaching old ‘magic bullets’ new tricks
Sanz, L., Blanco, B., & Álvarez‐Vallina, L. (2003) · Trends in Immunology · doi:10.1016/j.it.2003.12.001 · Cited by 90 · see citing works
Food groups and risk of oral and pharyngeal cancer
Levi, F., Pasche, C., Vecchia, C. L., Lucchini, F., Franceschi, S., & Monnier, P. (1998) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19980831)77:5 · Cited by 228 · see citing works
Solubility, Stability, and Avidity of Recombinant Antibody Fragments Expressed in Microorganisms
Kang, T. H., & Seong, B. L. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01927 · Cited by 89 · see citing works
Fifty years of monoclonals: the past, present and future of antibody therapeutics
Chan, A. C., Martyn, G. D., & Carter, P. J. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01207-9 · Cited by 96 · see citing works
New approaches to antibody therapy
Weiner, L. M., & Adams, G. P. (2000) · Oncogene · doi:10.1038/sj.onc.1204000 · Cited by 89 · see citing works
Bispecific antibodies engage T cells for antitumor immunotherapy
Choi, B. D., Cai, M., Bigner, D. D., Mehta, A. I., Kuan, C.-T., & Sampson, J. H. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.572874 · Cited by 88 · see citing works
Signal transduction therapy of cancer
Levitzki, A., & Klein, S. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.04.001 · Cited by 85 · see citing works
Symmetry breaking: bispecific antibodies, the beginnings, and 50 years on.
Riethmüller, G. (2012) · Europe PMC (PubMed Central) · Cited by 85 · see citing works
Self-citation
A Bispecific Diabody That Mediates Natural Killer Cell Cytotoxicity Against Xenotransplantated Human Hodgkin’s Tumors
Arndt, M. A. E., Krauß, J., Kipriyanov, S. M., Pfreundschuh, M. G., & Little, M. (1999) · Blood · doi:10.1182/blood.v94.8.2562.420k20_2562_2568 · Cited by 85 · see citing works
Current trends and challenges in the downstream purification of bispecific antibodies
Chen, S. W., & Zhang, W. (2021) · Antibody Therapeutics · doi:10.1093/abt/tbab007 · Cited by 84 · see citing works
Bispecific and bifunctional single chain recombinant antibodies
Kriangkum, J., Xu, B., Nagata, L. P., Fulton, R. E., & Suresh, M. R. (2001) · Biomolecular Engineering · doi:10.1016/s1389-0344(01)00083-1 · Cited by 83 · see citing works
Tumor-Antigen–Binding Bispecific Antibodies for Cancer Treatment
Weidle, U. H., Kontermann, R. E., & Brinkmann, U. (2014) · Seminars in Oncology · doi:10.1053/j.seminoncol.2014.08.004 · Cited by 83 · see citing works
ATTACK, a novel bispecific T cell-recruiting antibody with trivalent EGFR binding and monovalent CD3 binding for cancer immunotherapy
Harwood, S. L., Álvarez‐Cienfuegos, A., Nuñez‐Prado, N., Compte, M., Hernández‐Pérez, S., Merino, N., Bonet, J., Navarro, R., Henegouwen, P. M. P. V. B. E., Lykkemark, S., et al. (2017) · OncoImmunology · doi:10.1080/2162402x.2017.1377874 · Cited by 83 · see citing works
Bispecific antibody platforms for cancer immunotherapy
Lameris, R., de Bruin, R. C. G., Schneiders, F. L., Henegouwen, P. M. P. V. B. E., Verheul, H. M. W., de Gruijl, T. D., & van der Vliet, H. J. (2014) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2014.08.003 · Cited by 82 · see citing works
Antibody engineering
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 · see citing works
Generation of Recombinant Antibodies
Kipriyanov, S. M., & Little, M. (1999) · Molecular Biotechnology · doi:10.1385/mb:12:2:173 · Cited by 80 · see citing works
The first constant domain (CH1 and CL) of an antibody used as heterodimerization domain for bispecific miniantibodies
Müller, K. M., Arndt, K. M., Strittmatter, W., & Plückthun, A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00021-0 · Cited by 78 · see citing works
Potent Control of Tumor Growth by CEA/CD3-bispecific Single-chain Antibody Constructs That Are Not Competitively Inhibited by Soluble CEA
Lutterbuese, R., Raum, T., Kischel, R., Lutterbuese, P., Schlereth, B., Schaller, E., Mangold, S., Rau, D., Meier, P., Kiener, P. A., et al. (2009) · Journal of Immunotherapy · doi:10.1097/cji.0b013e31819b7c70 · Cited by 77 · see citing works
Self-citation
Bispecific Antibodies in the Treatment of Hematologic Malignancies
Duell, J., Lammers, P. E., Djuretic, I. M., Chunyk, A. G., Alekar, S., Jacobs, I. A., & Gill, S. I. (2019) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.1396 · Cited by 77 · see citing works
Bispecific monoclonal antibodies for targeted immunotherapy of solid tumors: Recent advances and clinical trials
Hosseini, S. S., Khalili, S., Baradaran, B., Bidar, N., Shahbazi, M., Mosafer, J., Hashemzaei, M., Mokhtarzadeh, A., & Hamblin, M. R. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.058 · Cited by 76 · see citing works
Design and engineering of bispecific antibodies: insights and practical considerations
Madsen, A. V., Pedersen, L. E., Kristensen, P. K., & Goletz, S. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1352014 · Cited by 76 · see citing works
A dimeric bispecific miniantibody combines two specificities with avidity
Müller, K. M., Arndt, K. M., & Plückthun, A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00829-1 · Cited by 76 · see citing works
Bi- and tri-valent T cell engagers deplete tumour-associated macrophages in cancer patient samples
Scott, E. M., Jacobus, E. J., Lyons, B., Frost, S., Freedman, J. D., Dyer, A., Khalique, H., Taverner, W. K., Carr, A., CHAMPION, B. R., et al. (2019) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-019-0807-6 · Cited by 75 · see citing works
A Novel Antibody Engineering Strategy for Making Monovalent Bispecific Heterodimeric IgG Antibodies by Electrostatic Steering Mechanism
Liu, Z., Leng, E. C., Gunasekaran, K., Pentony, M., Shen, M., Howard, M., Stoops, J. D., Manchulenko, K., Razinkov, V. I., Liu, H., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620260 · Cited by 75 · see citing works
Phage diabody repertoires for selection of large numbers of bispecific antibody fragments
McGuinness, B., Walter, G., FitzGerald, K., Schuler, P., Mahoney, W. C., Duncan, A., & Hoogenboom, H. R. (1996) · Nature Biotechnology · doi:10.1038/nbt0996-1149 · Cited by 75 · see citing works
Are BiTEs the “missing link” in cancer therapy?
Suryadevara, C. M., Gedeon, P. C., Sanchez-Perez, L. A., Verla, T. G., Alvarez-Breckenridge, C. A., Choi, B. D., Fecci, P. E., & Sampson, J. H. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1008339 · Cited by 72 · see citing works
Bispecific antibodies for targeted delivery of anti-cancer therapeutic agents: A review
Beishenaliev, A., Loke, Y. L., Goh, S. J., Geo, H. N., Mugila, M., Misran, M., Chung, L. Y., Kiew, L. V., Roffler, S. R., & Teo, Y. Y. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.05.032 · Cited by 71 · see citing works
T Cell–Activating Bispecific Antibodies in Cancer Therapy
Trabolsi, A., Arumov, A., & Schatz, J. H. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900496 · Cited by 70 · see citing works
Improved anti-leukemia activities of adoptively transferred T cells expressing bispecific T-cell engager in mice
Liu, X., Barrett, D. M., Jiang, S., Fang, C., Kalos, M. D., Grupp, S. A., June, C. H., & Zhao, Y. (2016) · Blood Cancer Journal · doi:10.1038/bcj.2016.38 · Cited by 68 · see citing works
Bispecific antibodies in haematological malignancies
Viardot, A., & Bargou, R. C. (2018) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2018.04.002 · Cited by 67 · see citing works
Fab Chains As an Efficient Heterodimerization Scaffold for the Production of Recombinant Bispecific and Trispecific Antibody Derivatives
Schoonjans, R., Willems, A. V., Schoonooghe, S., Fiers, W. C., Grooten, J., & Mertens, N. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.12.7050 · Cited by 67 · see citing works
The role of CD8+ T cells in immune responses to colorectal cancer
Titu, L. V., Monson, J. R. T., & Greenman, J. (2002) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-002-0276-4 · Cited by 66 · see citing works

Construction and biological activity of a recombinant bispecific single-chain antibody designed for therapy of minimal residual colorectal cancer
Kufer, P., Mack, M., Gruber, R., Lutterbüse, R., Zettl, F., & Riethmüller, G. (1997) · Cancer Immunology Immunotherapy · doi:10.1007/s002620050431 · Cited by 51 · see citing works
Self-citation
Biologic properties of a bispecific single-chain antibody directed against 17-1A (EpCAM) and CD3: tumor cell-dependent T cell stimulation and cytotoxic activity
Mack, M., Gruber, R., Schmidt, S., Riethmüller, G., & Kufer, P. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.8.3965 · Cited by 86 · see citing works
Self-citation
Production and characterization of bispecific single-chain antibody fragments
Jonge, J. D., Brissinck, J., Heirman, C., Demanet, C. J., Léo, O., Moser, M., & Thielemans, K. (1995) · Molecular Immunology · doi:10.1016/0161-5890(95)00089-5 · Cited by 34 · see citing works
Single-chain mono- and bispecific antibody derivatives with novel biological properties and antitumour activity from a COS cell transient expression system.
Hayden, M. S., Linsley, P. S., Gayle, M. A., Bajorath, J., Brady, W., Norris, N. A., Fell, H. P., Ledbetter, J. A., & Gilliland, L. K. (1994) · PubMed · Cited by 53 · see citing works
Development and Characterization of a Bispecific Single-Chain Antibody Directed Against T Cells and Ovarian Carcinoma
Kriangkum, J., Xu, B., Gervais, C., Paquette, D., Jacobs, F. A., Martin, L., & Suresh, M. R. (2000) · Hybridoma · doi:10.1089/027245700315770 · Cited by 24 · see citing works

Authors: Mack, M., Riethmüller, G., & Kufer, P.
Affiliations: Institut für Immunologie (DE)
ORCID: Mack, M
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1995-07-18
Volume: 92
Issue: 15
Pages: 7021-7025
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.92.15.7021
PMC: PMC41463
OpenAlex: W2086146164
Cited by: 351
References: 39
Citations by year: 2026: 8 · 2025: 11 · 2024: 15 · 2023: 7 · 2022: 10 · 2021: 20 · 2020: 12 · 2019: 22 · 2018: 19 · 2017: 20 · 2016: 12 · 2015: 22 · 2014: 16 · 2013: 13 · 2012: 14
FWCI: 12.32
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords: bispecific antibodies, single-chain antibody, single-chain Fv fragments, CD3 antigen, colorectal cancer, minimal residual disease, tumor cell killing, CHO cell expression, Ni-NTA affinity purification, antibody therapy
MeSH terms: Amino Acid Sequence, Antibody Specificity, Antineoplastic Agents, Base Sequence, Cloning, Molecular, Escherichia coli, Immunoglobulin Fragments, Immunoglobulin Variable Region, Molecular Sequence Data, Recombinant Proteins, Tumor Cells, Cultured, Blotting, Western

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A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity.

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