Diabetes Research and Clinical Practice
Volume 74, Issue 2, Supplement , Pages S51-S62 , 30 November 2006

Engineered antibodies: A new tool for use in diabetes research

References 

  1. von Behring E, Kitasato S. The mechanism of diphtheria immunity and tetanus immunity in animals. Mol. Immunol. 1890;28(12):1319–13201317
  2. Edelman GM, Benacerraf B. On structural and functional relations between antibodies and proteins of the gamma-system. Proc. Natl. Acad. Sci. U.S.A. 1962;48:1035–1042
  3. Kehry M, Sibley C, Fuhrman J, et al. Amino acid sequence of a mouse immunoglobulin μ chain. Proc. Natl. Acad. Sci. U.S.A. 1979;76(6):2932–2936
  4. Wu TT, Kabat EA. An analysis of the sequences of the variable regions of Bence-Jones proteins and myeloma light chains and their implication for antibody complementarity. J. Exp. Med. 1970;132:211–249
  5. Kabat EA, Wu TT. Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains. Ann. NY Acad. Sci. 1971;190:382–393
  6. Milstein C. General motors cancer research foundation awards: monoclonal antibodies. Cancer. 1982;49(10):1953–1957
  7. Azzazy HME, Highsmith WE. Phage display technology: clinical applications and recent innovations. Clin. Biochem. 2002;35:425–445
  8. Weigert M, Gatmaitan L, Loh E, et al. Rearrangement of genetic information may produce immunoglobulin diversity. Nature. 1978;276(5690):785–790
  9. Cory S, Tyler BM, Adams JM. Sets of immunoglobulin V kappa genes homologous to ten cloned V kappa sequences: implications for the number of germline V kappa genes. J. Mol. Appl. Genet. 1981;1(2):103–116
  10. Fitzsimmons SP, Rotz BT, Shapiro MA. Asymmetric contribution to Ig repertoire diversity by V kappa exons: differences in the utilization of V kappa 10 exons. J. Immunol. 1998;161(5):2290–2300
  11. Brack C, Hirama M, Lenhard-Schuller R, Tonegawa S. Complete immunoglobulin gene is created by somatic recombination. Cell. 1978;15:1–14
  12. Davis MM, Calame K, Early PW, et al. An immunoglobulin heavy-chain gene is formed by at least two recombinational events. Nature. 1980;283(5749):733–739
  13. Köhler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975;256(5517):495–497
  14. Vaughan TJ, Williams AJ, Pritchard K, et al. Human antibodies with sub-nanomolar affinities isolated from a large non-immunised phage display library. Nat. Biotechnol. 1996;14(3):309–314
  15. Winter G, Milstein C. Man-made antibodies. Nature. 1991;349(6307):293–299
  16. Morrison SL, Johnson MJ, Herzenberg LA, Oi VT. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc. Natl. Acad. Sci. U.S.A. 1984;81(21):6851–6855
  17. Adair JR. Engineering antibodies for therapy. Immunol. Rev. 1992;130:5–40
  18. Jones PT, Dear PH, Foote J, et al. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature. 1986;321(6069):522–525
  19. Verhoeyen M, Milstein C, Winter G. Reshaping human antibodies: grafting an antilysozyme activity. Science. 1988;239(4847):1534–1536
  20. Kashmiri SV, de Pascalis R, Gonzales NR, Schlom J. SDR grafting—a new approach to antibody humanization. Methods. 2005;36(1):25–34
  21. Huston JS, Levinson D, Mudgett-Hunter M, et al. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1988;85:5879–5883
  22. Riechmann L, Muyldermans S. Single domain antibodies: comparison of camel VH and camelised human VH domains. J. Immunol. Meth. 1999;231:25–38
  23. Padoa CJ, Banga JP, Madec AM, et al. Recombinant Fabs of human monoclonal antibodies specific to the middle epitope of GAD65 inhibit type 1 diabetes-specific GAD65Abs. Diabetes. 2003;52(11):2689–2695
  24. Padoa CJ, Crowther NJ, Thomas JW, et al. Epitope analysis of insulin autoantibodies using recombinant Fab. Clin. Exp. Immunol. 2005;140(3):564–571
  25. Schlosser M, Banga JP, Madec AM, et al. Dynamic changes of GAD65 autoantibody epitope specificities in individuals at risk of developing type 1 diabetes. Diabetologia. 2005;48(5):922–930
  26. Glockshuber R, Malia M, Pfitzinger I, Plückthun A. A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry. 1990;29(6):1362–1367
  27. Bird RE, Hardman KD, Jacobson JW, et al. Single-chain antigen-binding proteins. Science. 1988;243:423–426
  28. Anand NN, Dubuc G, Phipps J, et al. Synthesis and expression in Escherichia coli of cistronic DNA encoding an antibody fragment specific for a Salmonella serotype B O-antigen. Gene. 1991;100:39–44
  29. Takkinen K, Laukkanen ML, Sizmann D, et al. An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli. Protein Eng. 1991;4(7):837–841
  30. Denzin LK, Voss EW. Construction, characterization, and mutagenesis of an anti-fluorescein single chain antibody idiotype family. J. Biol. Chem. 1992;267(13):8925–8931
  31. Malby RL, Caldwell JB, Gruen LC, et al. Recombinant antineuraminidase single chain antibody: expression, characterization, and crystallization in complex with antigen. Proteins. 1993;16(1):57–63
  32. Lilley GG, Dolezal O, Hillyard CJ, Bernard C, Hudson PJ. Recombinant single-chain antibody peptide conjugates expressed in Escherichia coli for the rapid diagnosis of HIV. J. Immunol. Meth. 1994;171(2):211–226
  33. Smith GP. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 1985;228(4705):1315–1317
  34. Pack P, Plückthun A. Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli. Biochemistry. 1992;31(6):1579–1584
  35. Müller KM, Arndt KM, Strittmatter W, Plückthun A. The first constant domain (C(H)1 and C(L)) of an antibody used as heterodimerization domain for bispecific miniantibodies. FEBS Lett. 1998;422(2):259–264
  36. Hu S, Shively L, Raubitschek A, et al. Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts. Cancer Res. 1996;56(13):3055–3061
  37. Adams GP, McCartney JE, Tai MS, et al. Highly specific in vivo tumor targeting by monovalent and divalent forms of 741F8 anti-c-erbB-2 single-chain Fv. Cancer Res. 1993;53(17):4026–4034
  38. Holliger P, Prospero T, Winter G. Diabodies: small bivalent and bispecific antibody fragments. Proc. Natl. Acad. Sci. U.S.A. 1993;90(14):6444–6448
  39. Iliades P, Kortt AA, Hudson PJ. Triabodies: single chain Fv fragments without a linker form trivalent trimers. FEBS Lett. 1997;409(3):437–441
  40. McCafferty J, Griffiths AD, Winter G, Chiswell DJ. Phage antibodies: filamentous phage displaying antibody variable domains. Nature. 1990;348(6301):552–554
  41. Parmley SF, Smith GP. Antibody-selectable filamentous fd phage vectors: affinity purification of target genes. Gene. 1988;73(2):305–318
  42. Hawkins RE, Winter G. Cell selection strategies for making antibodies from variable gene libraries: trapping the memory pool. Eur. J. Immunol. 1992;22:867–870
  43. Persson MA, Caothien RH, Burton DR. Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning. Proc. Natl. Acad. Sci. U.S.A. 1991;88:2432–2436
  44. Hayashi N, Welschof M, Zewe M, et al. Simultaneous mutagenesis of antibody CDR regions by overlap extension and PCR. Biotechniques. 1994;17(2):314–315310, 312
  45. Pini A, Viti F, Santucci A, et al. Design and use of a phage display library. Human antibodies with subnanomolar affinity against a marker of angiogenesis eluted from a two-dimensional gel. J. Biol. Chem. 1998;273(34):21769–21776
  46. de Carvalho Nicacio C, Williamson RA, Parren PW, et al. Neutralizing human Fab fragments against measles virus recovered by phage display. J. Virol. 2002;76(1):251–258
  47. Larrick JW, Danielsson L, Brenner CA, et al. Rapid cloning of rearranged immunoglobulin genes from human hybridoma cells using mixed primers and the polymerase chain reaction. Biochem. Biophys. Res. Commun. 1989;160(3):1250–1256
  48. Zebedee SL, Barbas CF, Hom YL, et al. Human combinatorial antibody libraries to hepatitis B surface antigen. Proc. Natl. Acad. Sci. U.S.A. 1992;89(8):3175–3179
  49. Sheets MD, Amersdorfer P, Finnern R, et al. Efficient construction of a large nonimmune phage antibody library: the production of high affinity human single-chain antibodies to protein antigens. Proc. Natl. Acad. Sci. U.S.A. 1998;95:6157–6162
  50. Kang AS, Barbas CF, Janda KD, et al. Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces. Proc. Natl. Acad. Sci. U.S.A. 1991;88(10):4363–4366
  51. Barbas CF, Kang AS, Lerner RA, Benkovic SJ. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. U.S.A. 1991;88(18):7978–7982
  52. Skerra A, Dreher ML, Winter G. Filter screening of antibody Fab fragments secreted from individual bacterial colonies: specific detection of antigen binding with a two-membrane system. Anal. Biochem. 1991;196(1):151–155
  53. Griffiths AD, Williams SC, Hartley O, et al. Isolation of high affinity human antibodies directly from large synthetic repertoires. EMBO J. 1994;13(14):3245–3260
  54. Watkins JD, Beuerlein G, Wu H, et al. Discovery of human antibodies to cell surface antigens by capture lift screening of phage-expressed antibody libraries. Anal. Biochem. 1998;256(2):169–177
  55. Schier R, Marks JD. Efficient in vitro affinity maturation of phage antibodies using BIAcore guided selections. Hum Antibodies Hybridomas. 1996;7(3):97–105
  56. Hanes J, Plückthun A. In vitro selection, and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. U.S.A. 1997;94:4937–4942
  57. Schaffitzel C, Hanes J, Jermutus L, Plückthun A. Ribosome display: an in vitro method for selection and evolution of antibodies from libraries. J. Immunol. Meth. 1999;231:119–135
  58. Bruggemann M, Spicer C, Buluwela L, et al. Human antibody production in transgenic mice: expression from 100kb of the human IgH locus. Eur. J. Immunol. 1991;21(5):1323–1326
  59. Bruggemann M, Taussig MJ. Production of human antibody repertoires in transgenic mice. Curr. Opin. Biotechnol. 1997;8(4):455–458
  60. Duchosal MA, Eming SA, Mcconahey PJ, Dixon FJ. The hu-PBL-SCID mouse model. Long-term human serologic evolution associated with the xenogeneic transfer of human peripheral blood leukocytes into SCID mice. Cell. Immunol. 1992;139(2):468–477
  61. Yokota T, Milenic DE, Whitlow M, Schlom J. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res. 1992;52(12):3402–3408
  62. Yamaguchi A, Ding K, Maehara M, et al. Expression of nm23-H1 Gene and Sialyl Lewis X antigen in breast cancer. Oncology. 1998;55:357–362
  63. Raju R, Foote J, Banga JP, et al. Analysis of GAD65 autoantibodies in Stiff-Person syndrome patients. J. Immunol. 2005;175(11):7755–7762
  64. Vandewalle CL, Falorni A, Svanholm S, et al. High diagnostic sensitivity of glutamate decarboxylase autoantibodies in insulin-dependent diabetes mellitus with clinical onset between age 20 and 40 years. The Belgian Diabetes Registry. J. Clin. Endocrinol. Metab. 1995;80(3):846–851
  65. Jaume JC, Parry SL, Madec AM, et al. Suppressive effect of glutamic acid decarboxylase 65-specific autoimmune B lymphocytes on processing of T cell determinants located within the antibody epitope. J. Immunol. 2002;169(2):665–672
  66. Reijonen H, Daniels TL, Lernmark A, Nepom GT. GAD65-specific autoantibodies enhance the presentation of an immunodominant T-cell epitope from GAD65. Diabetes. 2000;49(10):1621–1626
  67. Tuomi T, Rowley MJ, Knowles WJ, et al. Autoantigenic properties of native and denatured glutamic acid decarboxylase: evidence for a conformational epitope. Clin. Immunol. Immunopathol. 1994;71(1):53–59
  68. Schwartz HL, Chandonia JM, Kash SF, et al. High-resolution autoreactive epitope mapping and structural modeling of the 65kDa form of human glutamic acid decarboxylase. J. Mol. Biol. 1999;287(5):983–999
  69. Daw K, Powers AC. Two distinct glutamic acid decarboxylase auto-antibody specificities in IDDM target difference epitopes. Diabetes. 1995;44(2):216–220
  70. Hampe CS, Hammerle LP, Bekris L, et al. Recognition of glutamic acid decarboxylase (GAD) by autoantibodies from different GAD antibody-positive phenotypes. J. Clin. Endocrinol. Metab. 2000;85(12):4671–4679
  71. Björk E, Velloso LA, Kämpe O, Karlsson FA. GAD autoantibodies in IDDM, Stiff-Man Syndrome, and autoimmune polyendocrine syndrome type I recognize different epitopes. Diabetes. 1994;43:161–165
  72. Daw K, Ujihara N, Atkinson M, Powers AC. Glutamic acid decarboxylase autoantibodies in Stiff-Man syndrome and insulin-dependent diabetes mellitus exhibit similarities and differences in epitope recognition. J. Immunol. 1996;156(2):818–825
  73. Ziegler B, Schlosser M, Luhder F, et al. Murine monoclonal glutamic acid decarboxylase (GAD)65 antibodies recognize autoimmune-associated GAD epitope regions targeted in patients with type 1 diabetes mellitus and Stiff-Man syndrome. Acta Diabetol. 1996;33(3):225–231
  74. Falorni A, Gambelunghe G, Forini F, et al. Autoantibody recognition of COOH-terminal epitopes of GAD65 marks the risk for insulin requirement in adult-onset diabetes mellitus. J. Clin. Endocrinol. Metab. 2000;85(1):309–316
  75. Bonifacio E, Lampasona V, Bernasoni L, Ziegler AG. Maturation of the humoral autoimmune response to epitopes of GAD in preclinical childhood type 1 diabetes. Diabetes. 2000;49(2):202–208
  76. Simitsek PD, Campbell DG, Lanzavecchia A, et al. Modulation of antigen processing by bound antibodies can boost or suppress class II major histocompatibility complex presentation of different T cell determinants. J. Exp. Med. 1995;181(6):1957–1963
  77. Watts C. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 1997;15:821–850
  78. Ziegler AG, Hummel M, Schenker M, Bonifacio E. Autoantibody appearance and risk for development of childhood diabetes in offspring of parents with type 1 diabetes: the 2-year analysis of the German BABYDIAB Study. Diabetes. 1999;48:460–468
  79. Graham J, Hagopian WA, Kockum I, et al. Genetic effects on age-dependent onset and islet cell autoantibody markers in type 1 diabetes. Diabetes. 2002;51(5):1346–1355
  80. Karjalainen J, Salmela P, Ilonen J, et al. A comparison of childhood and adult type I diabetes mellitus. N. Engl. J. Med. 1989;320(14):881–886
  81. Diaz JL, Wilkin T. Differences in epitope restriction of autoantibodies to native human insulin (IAA) and antibodies to heterologous insulin (IA). Diabetes. 1987;36(1):66–72
  82. Wilkin T, Mirza I, Armitage M, et al. Insulin autoantibody polymorphisms with greater discrimination for diabetes in humans. Diabetologia. 1988;31:670–674
  83. Devendra D, Galloway TS, Horton SJ, et al. The use of phage display to distinguish insulin autoantibody (IAA) from insulin antibody (IA) idiotypes. Diabetologia. 2003;46:802–809
  84. Schlosser M, Hahmann J, Ziegler B, et al. Sensitive monoclonal antibody-based sandwich ELISA for determination of the diabetes-associated autoantigen glutamic acid decarboxylase GAD65. J. Immunoassay. 1997;18:289–307
  85. Kolm-Litty V, Berlo S, Bonifacio E, et al. Human monoclonal antibodies isolated from type I diabetes patients define multiple epitopes in the protein tyrosine phosphatase-like IA-2 antigen. J. Immunol. 2000;165:4676–4684
  86. Daniel D, Wegmann DR. Protection of nonobese diabetic mice from diabetes by intranasal or subcutaneous administration of insulin peptide B-(9-23). Proc. Natl. Acad. Sci. U.S.A. 1996;93:956–960
  87. King H, Aubert RE, Herman WH. Global burden of diabetes, 1995–2025: prevalence, numerical estimates, and projections. Diab. Care. 1998;21(9):1414–1431
  88. Wareham NJ, Byrne CD, Williams R, et al. Fasting proinsulin concentrations predict the development of type 2 diabetes. Diab. Care. 1999;22(2):262–270
  89. Sobey WJ, Beer SF, Carrington CA, et al. Sensitive and specific two-site immunoradiometric assays for human insulin, proinsulin, 65–66 split proinsulin and 32–33 split proinsulins. Biochem. J. 1989;260:535–541
  90. Warren DJ, Bjerner J, Paus E, et al. Use of an in vivo biotinylated single-chain antibody as capture reagent in an immunometric assay to decrease the incidence of interference from heterophilic antibodies. Clin. Chem. 2005;51(5):830–838
  91. Yalow RS, Berson SA. Plasma insulin concentrations in nondiabetic and early diabetic subjects. Determinations by a new sensitive immuno-assay technic. Diabetes. 1959;9(4):254–260
  92. Kim SJ, Park Y, Hong HJ. Antibody engineering for the development of therapeutic antibodies. Mol. Cells. 2005;20(1):17–29
  93. Marks JD, Hoogenboom HR, Griffiths AD, Winter G. Molecular evolution of proteins on filamentous phage. J. Biol. Chem. 1992;267(23):16007–16010
  94. Hudson PJ, Souriau C. Engineered antibodies. Nature Med. 2003;9(1):129–134
  95. Binder KA, Banga JP, Madec AM, et al. Epitope analysis of GAD65Ab using fusion proteins and rFab. J. Immunol. Meth. 2004;295:101–109
  96. Nijpels G, Popp-Snijders C, Kostense PJ, et al. Fasting proinsulin and 2-h post-load glucose levels predict the conversion to NIDDM in subjects with impaired glucose tolerance: the Hoorn Study. Diabetologia. 1996;39(1):113–118

PII: S0168-8227(06)00282-8

doi: 10.1016/j.diabres.2006.06.033

Diabetes Research and Clinical Practice
Volume 74, Issue 2, Supplement , Pages S51-S62 , 30 November 2006