Functional mapping of the anti-idiotypic antibody anti-TS1 scFv using site-directed mutagenesis and kinetic analysis

References

• Milenic DE, Brady ED, Brechbiel MW. Antibody-targeted radiation cancer therapy. Nat Rev Drug Discov 2004; 3:488 - 499
   PubMed Web of Science ®Google Scholar
• Sandstrom P, Johansson A, Ullen A, Rathsman S, Riklund-Ahlstrom K, Stigbrand T. Idiotypic-anti-idiotypic antibody interactions in experimental radioimmunotargeting. Clin Cancer Res 1999; 5:3073 - 3078
   Google Scholar
• Sharkey RM, Boerman OC, Natale A, Pawlyk D, Monestier M, Losman MJ, et al. Enhanced clearance of radiolabeled murine monoclonal antibody by a syngeneic anti-idiotype antibody in tumor-bearing nude mice. Int J Cancer 1992; 51:266 - 273
   PubMed Web of Science ®Google Scholar
• Ullen A, Ahlstrom KR, Heitala S, Nilsson B, Arlestig L, Stigbrand T. Secondary antibodies as tools to improve tumor to non tumor ratio at radioimmunolocalisation and radioimmunotherapy. Acta Oncol 1996; 35:281 - 285
   PubMed Web of Science ®Google Scholar
• Johansson A, Erlandsson A, Eriksson D, Ullen A, Holm P, Sundstrom BE, et al. Idiotypic-anti-idiotypic complexes and their in vivo metabolism. Cancer 2002; 94:1306 - 1313
   PubMed Web of Science ®Google Scholar
• Ullen A, Sandstrom P, Ahlstrom KR, Sundstrom B, Nilsson B, Arlestig L, et al. Use of anticytokeratin monoclonal anti-idiotypic antibodies to improve tumor:nontumor ratio in experimental radioimmunolocalization. Cancer Res 1995; 55:5868 - 5873
   Web of Science ®Google Scholar
• Eriksson D, Joniani HM, Sheikholvaezin A, Lofroth PO, Johansson L, Riklund Ahlstrom K, et al. Combined low dose radio- and radioimmunotherapy of experimental HeLa Hep 2 tumours. Eur J Nucl Med Mol Imaging 2003; 30:895 - 906
   PubMed Web of Science ®Google Scholar
• Riklund KE, Makiya R, Sundstrom B, Back O, Henriksson R, Hietala SO, et al. Inhibition of growth of HeLa cell tumours in nude mice by 125I-labeled anticytokeratin and antiPLAP monoclonal antibodies. Anticancer Res 1991; 11:555 - 560
   PubMed Web of Science ®Google Scholar
• Jafari R, Holm P, Sandegren J, Stigbrand T, Sundstrom BE. Localization of complexed anti-cytokeratin 8 scFv TS1-218 to HeLa HEp-2 multicellular tumor spheroids and experimental tumors. Cancer Biotherapy and Radiopharmaceuticals 2010; 25:455 - 463
   PubMed Web of Science ®Google Scholar
• Holm P, Jafari R, Sundstrom BE. Functional mapping and single chain construction of the anti-cytokeratin 8 monoclonal antibody TS1. Mol Immunol 2007; 44:1075 - 1084
   PubMed Web of Science ®Google Scholar
• Iacob RE, Keck Z, Olson O, Foung SK, Tomer KB. Structural elucidation of critical residues involved in binding of human monoclonal antibodies to hepatitis C virus E2 envelope glycoprotein. Biochim Biophys Acta 2008; 1784:530 - 542
   PubMed Web of Science ®Google Scholar
• Jermutus L, Honegger A, Schwesinger F, Hanes J, Pluckthun A. Tailoring in vitro evolution for protein affinity or stability. Proc Natl Acad Sci USA 2001; 98:75 - 80
   PubMed Web of Science ®Google Scholar
• Reichmann D, Rahat O, Albeck S, Meged R, Dym O, Schreiber G. The modular architecture of protein-protein binding interfaces. Proc Natl Acad Sci USA 2005; 102:57 - 62
   PubMed Web of Science ®Google Scholar
• Worn A, Pluckthun A. Stability engineering of antibody single-chain Fv fragments. J Mol Biol 2001; 305:989 - 1010
   PubMed Web of Science ®Google Scholar
• Braden BC, Poljak RJ. Structural features of the reactions between antibodies and protein antigens. FASEB J 1995; 9:9 - 16
   PubMed Web of Science ®Google Scholar
• Davies DR, Cohen GH. Interactions of protein antigens with antibodies. Proc Natl Acad Sci USA 1996; 93:7 - 12
   PubMed Web of Science ®Google Scholar
• Shiroishi M, Tsumoto K, Tanaka Y, Yokota A, Nakanishi T, Kondo H, et al. Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL. J Biol Chem 2007; 282:6783 - 6791
   PubMed Web of Science ®Google Scholar
• Collis AV, Brouwer AP, Martin AC. Analysis of the antigen combining site: correlations between length and sequence composition of the hypervariable loops and the nature of the antigen. J Mol Biol 2003; 325:337 - 354
   PubMed Web of Science ®Google Scholar
• Dougan DA, Malby RL, Gruen LC, Kortt AA, Hudson PJ. Effects of substitutions in the binding surface of an antibody on antigen affinity. Protein Eng 1998; 11:65 - 74
   PubMedGoogle Scholar
• Janin J, Chothia C. The structure of protein-protein recognition sites. J Biol Chem 1990; 265:16027 - 16030
   PubMed Web of Science ®Google Scholar
• MacCallum RM, Martin AC, Thornton JM. Antibody-antigen interactions: contact analysis and binding site topography. J Mol Biol 1996; 262:732 - 745
   PubMed Web of Science ®Google Scholar
• Almagro JC. Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires. J Mol Recognit 2004; 17:132 - 143
   PubMed Web of Science ®Google Scholar
• Gabdoulline RR, Wade RC. On the protein-protein diffusional encounter complex. J Mol Recognit 1999; 12:226 - 234
   PubMed Web of Science ®Google Scholar
• Sheinerman FB, Honig B. On the role of electrostatic interactions in the design of protein-protein interfaces. J Mol Biol 2002; 318:161 - 177
   PubMed Web of Science ®Google Scholar
• Albeck S, Unger R, Schreiber G. Evaluation of direct and cooperative contributions towards the strength of buried hydrogen bonds and salt bridges. J Mol Biol 2000; 298:503 - 520
   PubMed Web of Science ®Google Scholar
• Ramirez-Benitez MC, Almagro JC. Analysis of antibodies of known structure suggests a lack of correspondence between the residues in contact with the antigen and those modified by somatic hypermutation. Proteins 2001; 45:199 - 206
   PubMed Web of Science ®Google Scholar
• Ohlin M, Borrebaeck CA. Insertions and deletions in hypervariable loops of antibody heavy chains contribute to molecular diversity. Mol Immunol 1998; 35:233 - 238
   PubMed Web of Science ®Google Scholar
• Khalifa MB, Weidenhaupt M, Choulier L, Chatellier J, Rauffer-Bruyere N, Altschuh D, et al. Effects on interaction kinetics of mutations at the VH-VL interface of Fabs depend on the structural context. J Mol Recognit 2000; 13:127 - 139
   PubMed Web of Science ®Google Scholar
• Vargas-Madrazo E, Paz-Garcia E. An improved model of association for VH-VL immunoglobulin domains: asymmetries between VH and VL in the packing of some interface residues. J Mol Recognit 2003; 16:113 - 120
   PubMed Web of Science ®Google Scholar
• Weidenhaupt M, Khalifa MB, Hugo N, Choulier L, Altschuh D, Vernet T. Functional mapping of conserved, surface-exposed charges of antibody variable domains. J Mol Recognit 2002; 15:94 - 103
   PubMed Web of Science ®Google Scholar
• Friguet B, Chaffotte AF, Djavadi-Ohaniance L, Goldberg ME. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J Immunol Methods 1985; 77:305 - 319
   PubMed Web of Science ®Google Scholar
• Malmborg AC, Borrebaeck CA. BIAcore as a tool in antibody engineering. J Immunol Methods 1995; 183:7 - 13
   PubMed Web of Science ®Google Scholar
• Erlandsson A, Holm P, Ullen A, Stigbrand T, Sundstrom BE. Studies of the interactions between the anticytokeratin 8 monoclonal antibody TS1, its antigen and its anti-idiotypic antibody alphaTS1. J Mol Recognit 2003; 16:157 - 163
   PubMed Web of Science ®Google Scholar
• Johansson A, Sandstrom P, Ullen A, Behravan G, Erlandsson A, Levi M, et al. Epitope specificity of the monoclonal anticytokeratin antibody TS1. Cancer Res 1999; 59:48 - 51
   PubMed Web of Science ®Google Scholar
• Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998; 280:1 - 9
   PubMed Web of Science ®Google Scholar
• Fields BA, Goldbaum FA, Ysern X, Poljak RJ, Mariuzza RA. Molecular basis of antigen mimicry by an anti-idiotope. Nature 1995; 374:739 - 742
   PubMed Web of Science ®Google Scholar
• Gaida FJ, Pieper D, Roder UW, Shively JE, Wagener C, Neumaier M. Molecular characterization of a cloned idiotypic cascade containing a network antigenic determinant specific for the human carcinoembryonic antigen. J Biol Chem 1993; 268:14138 - 14145
   PubMed Web of Science ®Google Scholar
• Johnson G, Moore SW. Functional idiotypic mimicry of an adhesion- and differentiation-promoting site on acetylcholinesterase. J Cell Biochem 2004; 91:999 - 1009
   PubMed Web of Science ®Google Scholar
• Kolesnikov AV, Kozyr AV, Alexandrova ES, Koralewski F, Demin AV, Titov MI, et al. Enzyme mimicry by the antiidiotypic antibody approach. Proc Natl Acad Sci USA 2000; 97:13526 - 13531
   PubMed Web of Science ®Google Scholar
• Weissenhorn W, Chen YH, Riethmuller G, Rieber EP, Weiss EH. VH-related idiotopes detected by site-directed mutagenesis. A study induced by the failure to find CD4 anti-idiotypic antibodies mimicking the cellular receptor of HIV. J Immunol 1992; 149:1237 - 1241
   PubMed Web of Science ®Google Scholar
• Kipriyanov SM, Moldenhauer G, Martin AC, Kupriyanova OA, Little M. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity. Protein Eng 1997; 10:445 - 453
   PubMedGoogle Scholar
• Morea V, Lesk AM, Tramontano A. Antibody modeling: implications for engineering and design. Methods 2000; 20:267 - 279
   PubMed Web of Science ®Google Scholar
• Liang S, Liu Z, Li W, Ni L, Lai L. Construction of protein binding sites in scaffold structures. Biopolymers 2000; 54:515 - 523
   PubMed Web of Science ®Google Scholar
• Jackson RM. Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: implications for the protein docking problem. Protein Sci 1999; 8:603 - 613
   PubMed Web of Science ®Google Scholar
• Kaplan H, Long BG, Young NM. Chemical properties of functional groups of mouse immunoglobulins of the IgA, IgG2a and IgM classes. Biochemistry 1980; 19:2821 - 2827
   PubMed Web of Science ®Google Scholar
• Schreiber G, Fersht AR. Rapid, electrostatically assisted association of proteins. Nat Struct Biol 1996; 3:427 - 431
   PubMedGoogle Scholar
• Selzer T, Albeck S, Schreiber G. Rational design of faster associating and tighter binding protein complexes. Nat Struct Biol 2000; 7:537 - 541
   PubMedGoogle Scholar
• Sundstrom BE, Nathrath WB, Stigbrand TI. Diversity in immunoreactivity of tumor-derived cytokeratin monoclonal antibodies. J Histochem Cytochem 1989; 37:1845 - 1854
   PubMed Web of Science ®Google Scholar
• Erlandsson A, Eriksson D, Johansson L, Riklund K, Stigbrand T, Sundstrom BE. In vivo clearing of idiotypic antibodies with antiidiotypic antibodies and their derivatives. Mol Immunol 2006; 43:599 - 606
   PubMed Web of Science ®Google Scholar
• Yang J, Moyana T, MacKenzie S, Xia Q, Xiang J. One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-alpha) from Escherichia coli caused by the synergistic effects of glycine and triton X-100. Appl Environ Microbiol 1998; 64:2869 - 2874
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680 - 685
   PubMed Web of Science ®Google Scholar
• Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997; 18:2714 - 2723
   PubMed Web of Science ®Google Scholar