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Anti-idiotypic antibodies as probes of cell surface receptors

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Summary

Anti-idiotypic antibodies have proven to have unique applications as probes in both functional and biochemical studies of cell surface receptors. Anti-idiotypic receptor antibodies have been prepared to antibodies which bind to purified ligand, as in the case of insulin, retinol-binding protein, the mammalian reovirus receptor, and the neutrophil chemotatic receptor, and to natural ligand analogs, such as the beta-adrenergic antagonist alprenolol. These systems have documented the usefulness of anti-idiotypic antibodies in the quantitation and modulation of specific membrane receptors on a variety of cell types. Anti-idotypic antibodies have also been utilized for the isolation of specific membrane receptors, e.g., reovirus and B-1 H globulin receptors. Some anti-idiotypic receptor antibodies, e.g., insulin and reovirus systems, have been shown to mimic the physiological properties of ligand upon binding to cellular receptors. These antibodies enable a new dimension of both receptor based cellular studies and therapeutic regimens. This review focuses on the past use of anti-idiotypic antibodies as probes of cell surface receptors, and on the methodologies required for the successful application of anti-idiotypic antibodies for use in further membrane receptor studies, and of the genes which encode and regulate these receptors. We also discuss the use of anti-idiotypic antibodies in the understanding of and therapeutic approach to receptor related diseases.

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References

  1. Jerne NK: Towards a network theory of the immune system. Ann Immunol 125c: 373–388, 1974.

    Google Scholar 

  2. Sirisinha S, Eisen H H: Autoimmune-like antibodies to the ligand-binding sites of myeloma proteins. Proc Natl Acad Sci USA 68: 3130–3135, 1971.

    Google Scholar 

  3. Cosenza H: Detection of anti-idiotype reactive cells in the response to phosphorylcholine. Eur J Immunol 6: 114–116, 1976.

    Google Scholar 

  4. Geha RS: Presence of auto-anti-idiotypic antibody during the normal human immune response to tetanus toxoid antigen. J Immunol 129: 139–144, 1982.

    Google Scholar 

  5. Hart DA, Wang A-L, Pawlak LL, Nisonoff A: Suppression of idiotypic specificities in adult mice by administration of anti-idiotypic antibody. J Exp Med 135: 1293–1300, 1972.

    Google Scholar 

  6. Owen FL, Ju S-T, Nisonoff A: Presence on idiotype-specific suppressor T cells of receptors that interact with molecules bearing the idiotype. J Exp Med 145: 1559–1566, 1977.

    Google Scholar 

  7. Dietz MH, Sy M-S, Benacerraf B, Nisonoff A, Greene MI, Germain RH: Antigen- and receptor-driven regulatory mechanisms. VII. H-2 restricted anti-idiotypic suppressor factor from efferent suppressor T cells. J Exp Med 153: 450–460, 1981.

    Google Scholar 

  8. Eichman K: Idiotypic suppression. II. Amplification of a suppressor T cell with anti-idiotypic activity. Eur J Immunol 5: 511–517, 1975.

    Google Scholar 

  9. Sege K, Peterson PA: Use of anti-idiotypic antibodies as cell-surface receptor probes. Proc Natl Acad Sci USA 75: 2443–2447, 1978.

    Google Scholar 

  10. Schreiber AB, Couraud PO, Andre C, Vray B, Strosberg DA: Anti-alprenolol anti-idiotypic antibodies bind to Badrenergic receptors and modulate catecholamine-sensitive adenylate cyclase. Proc Natl Acad Sci USA 77: 7385–7389, 1980.

    Google Scholar 

  11. Flier J, Kahn CR, Jarett DB, Roth J: Characterization of antibody to the insulin receptor. A case of insulin-resistant diabetes in man. J Clin Invest 58: 1442–1449, 1976.

    Google Scholar 

  12. Flier J, Kahn CR, Roth J, Bar R: Autoantibodies that impair insulin receptor binding in an unusual diabetic syndrome with severe insulin resistance. Science 190: 63–65, 1975.

    Google Scholar 

  13. Hall R, Smith BR, Mukhtar ED: Thyroid stimulators in health and disease. Clin Endocrinol 4: 213–230, 1975.

    Google Scholar 

  14. Dwyer DS, Bradley RJ, Urquhart CK, Kearney JF: Naturally occurring anti-idiotypic antibodies in myasthenia gravis patients. Nature (London) 301: 611–614, 1983.

    Google Scholar 

  15. Wasserman NH, Penn AS, Freimuth PI, Treptow N, Wentzel S, Cleveland WL, Erlanger BF: Anti-idiotypic route to anti-acetylcholine receptor antibodies and experimental myasthenia gravis. Proc Natl Acad Sci USA 79: 4810–4814, 1982.

    Google Scholar 

  16. Goding JW: Biological effects of antibody to lymphocyte surface receptors. Springer Seminar Immunopathol 5: 463–475, 1982.

    Google Scholar 

  17. Venter JC: Monoclonal antibodies and autoantibodies in the isolation and characterization of neurotransmitter receptors: the future of receptor research. J Mol Cell Cardiol 14:687–693, 1982.

    Google Scholar 

  18. Strauss WL, Ghai G, Fraser CM, Venter JC: Detergent solubilization of mammalian cardiac and hepatic B-adrenergic receptors. Arch Biochem Biophys 196: 566–573, 1979.

    Google Scholar 

  19. Kull FC Jr, Jacobs S, Su Y-F, Cuatrecasas P: A monoclonal antibody to human insulin receptor. Biochem Biophys Res Commun 106: 1019–1026, 1982.

    Google Scholar 

  20. Kasuga M, Van Obberghan E, Yamada KM, Harrison LC: Autoantibodies against the insulin receptor recognize the insulin binding subunits of an oligomeric receptor. Diabetes 30: 354–357, 1981.

    Google Scholar 

  21. Kasuga M, Karlsson FA, Kahn CR: Insulin stimulates the phosphorylation of the 95000 dalton subunit of its own receptor. Science 215: 185–187, 1982.

    Google Scholar 

  22. Kasuga M, Fujito-Yamaguchi Y, Blithe DL, Kahn CR: Tyrosine specific protein kinase activity is associated with the purified insulin receptor. Proc Natl Acad Sci USA 80: 2137–2141, 1983.

    Google Scholar 

  23. Rosen OM, Herrera R, Lowe YO, Petruzzelli LM, Cobb MH: Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc Natl Acad Sci USA 80: 3237–3240, 1983.

    Google Scholar 

  24. Roth RA, Cassell DJ: Insulin receptor: evidence that it is a protein kinase. Science 219: 299–310, 1983.

    Google Scholar 

  25. Taylor RB, Duffus WPH, Raff MC, dePetris S: Redistribution and pinocytosis of lymphocyte surface immunoglobulin molecules induced by anti-immunoglobulin antibody. Nature (New Biol) 233: 225–229, 1971.

    Google Scholar 

  26. Schreiner GF, Unanue ER: Membrane and cytoplasmic changes in B lymphocytes induced by ligand-surface immunoglobulin interaction. Adv Immunol 24:37–165, 1976.

    Google Scholar 

  27. Edelman GM: Surface modulation in cell recognition and cell growth. Science 192: 218–226, 1976.

    Google Scholar 

  28. Bourguignon LYW, Singer SJ: Transmembrane interactions and the capping of surface receptors by their specific ligands. Proc Natl Acad Sci USA 74: 5031–5035 1977.

    Google Scholar 

  29. Sege K, Peterson PA: Anti-idiotypic antibodies against anti-vitamin A transport protein reacts with prealbumin. Nature (London) 271: 167–168, 1978.

    Google Scholar 

  30. Shechter Y, Maron R, Elias D, Cohen IR: Autoantibodies to insulin receptor spontaneously develop as anti-idiotypes in mice immunized with insulin. Science 216: 542–545, 1982.

    Google Scholar 

  31. Couraud PO, Lu BZ, Schmutz A, Durieu-Trautmann O, Klutchko-Delavier C, Hoebeke J, Strosberg DA: Immunological studies of B-adrenergic receptors. J Cell Biochem (in press), 1983.

  32. Homcy CJ, Rockson SG, Haber E: An anti-idiotypic antibody that recognizes the B-adrenergic receptor. J Clin Invest 69: 1147–1154, 1982.

    Google Scholar 

  33. Fraser CM, Venter JC: Monoclonal antibodies to B-adrenergoic receptors: use in purification and molecular characterization of B-receptors. Proc Natl Acad Sci USA 77: 7034–7038, 1980.

    Google Scholar 

  34. Fraser CM, Greguski R, Eddy B, Venter JC: Autoantibodies and monoclonal antibodies in the purification and molecular characterization of neurotransmitter receptors. J Cell Biochem (in press), 1983.

  35. Venter JC, Fraser CM: Beta-adregnergic receptor isolation and characterization with immobilized drugs and monoclonal antibodies. Fed Proc 42: 123–128, 1983.

    Google Scholar 

  36. Marasco WA, Becker EL: Anti-idiotype as antibody against the formyl peptide chemotaxis receptor of the neutrophil. J Immunol 128: 963–968, 1982.

    Google Scholar 

  37. Lambris JD, Ross GD: Characterization of the lymphocyte membrane receptor for factor H (B1 H-globulin) with an antibody to anti-factor H idiotype. J Exp Med 155: 1400–1411, 1982.

    Google Scholar 

  38. Fields BN, Greene MI: Genetic and molecular mechanisms of viral pathogenesis: implications for prevention and treatment. Nature (London) 300: 19–23, 1982.

    Google Scholar 

  39. Burstin SJ, Spriggs DR, Fields BN: Evidence for functional domains on the reovirus type 3 hemagglutinin. Virology 117:146–155, 1982.

    Google Scholar 

  40. Greene MI, Weiner HL: Delayed hypersensitivity in mice infected with reovirus. III. Induction of tolerance and suppressor T cells to viral specific gene products. J Immunol 125:283–287, 1980.

    Google Scholar 

  41. Finberg R, Weiner HL, Fields BN, Benacerraf B, Burakoff SJ: Generation of cytolytic T lymphocytes after reovirus infection: role of S1 gene. Proc Natl Acad Sci USA 76: 442–446, 1979.

    Google Scholar 

  42. Nepom JT, Weiner HL, Dichter MA, Tardieu M, Spriggs DR, Gramm CF, Powers ML, Fields BN, Greene MI: Identification of a hemagglutinin-specific idiotype associated with reovirus recognition shared by lymphoid and neural cells. J Exp Med 155: 155–167, 1982.

    Google Scholar 

  43. Nepom JT, Tardieu M, Epstein RL, Noseworthy JH, Weiner HL, Gentsch J, Fields BN, Greene MI: Virus-binding receptors: similarities to immune receptors as determined by anti-idiotypic antibodies. Surv Immunol Res 1: 255–261, 1982.

    Google Scholar 

  44. Fontana A, Weiner HL: Interacting reovirus with cell surface receptors. II. Generation of suppressor T cells by the hemagglutinin of reovirus type 3. J Immunol 125: 2660–2664, 1980.

    Google Scholar 

  45. Noseworthy JH, Fields BN, Dichter MA, Sobotoka C, Pizer E, Perry LL, Nepom JT, Greene MI: Cell receptors for the mammalian reovirus. I. Syngeneic monoclonal antiidiotypic antibody identifies a cell surface receptor for reovirus. J Immunol 131: 2533–2538, 1983.

    Google Scholar 

  46. Kauffman RS, Noseworthy JH, Nepom JT, Finberg R, Fields BN, Greene MI: Cell receptors for the mammalian reovirus. II. Monoclonal anti-idiotypic antibody blocks viral binding to cells. J Immunol 131: 2539–2541, 1983.

    Google Scholar 

  47. Ertl HC, Greene MI, Noseworthy JH, Fields BN, Nepom JT, Spriggs DR, Finberg RW: Identification of idiotype receptors on reovirus-specific cytolytic T cells. Proc Natl Acad Sci USA 79: 7479–7483, 1983.

    Google Scholar 

  48. Sharpe AH, Ertl HCJ, Finberg RW, Fields BN, Greene, MI: Cell receptors for the mammalian reovirus. IV. Reovirus specific cytolytic T cell lines which have idiotypic receptors recognize anti-idiotypic B cell hybridomas. J Exp Med in press.

  49. Jensenius JC, Williams AF: The T lymphocyte to antigen receptor — paradigm lost. Nature (London) 300: 583–388, 1982.

    Google Scholar 

  50. Kronenberg M, Kraig E. Hood L: Finding the T-cell antigen receptor: past attempts and future promise. Cell 34: 327–319, 1983.

    Google Scholar 

  51. Binz H, Wigzell H: Shared idiotypic determinants on B and T lymphocytes reactive against the same antigenic determinants. I. Demonstration of similar or identical idiotypes on IgG molecules and T cell receptors with specificity for the same alloantigens. J Exp Med 142: 197–211, 197–211, 1975.

    Google Scholar 

  52. Eichmann K, Rajewsky K: Induction of T and B cell immunity by anti-idiotypic antibody. Eur J Immunol 5: 661–666, 1975.

    Google Scholar 

  53. Black SJ, Hammerling GJ, Berek C, Rajewsky K, Eichmann K: Idiotypic analysis of lymphocytes in vitro. I. Specificity and heterogeneity of B and T lymphocytes reactive with anti-idiotypic antibody. J Exp Med 143: 846–860, 1976.

    Google Scholar 

  54. Krawinkel U, Cramer M, Imanishi-Kari T, Jack RS, Rajewsky K, Makela O: Isolated hapten-binding receptors of sensitized lymphocytes. I. Receptors from nylon-wool enriched mouse T lymphocytes lack serological markers of immunoglobulin constant domains but express heavy chain variable portions. Eur J Immunol 8: 566–573, 1977.

    Google Scholar 

  55. Binz H, Wigzell H: Shared idiotypic determinants on B and T lymphocytes reactive against the same antigenic determinants. IV. Isolation of two groups of naturally occurring. idiotypic molecules with specific antigen-binding activity in the serum and urine of normal rats. Scand J Immunol 4: 591–600, 1975.

    Google Scholar 

  56. Binz H, Wigzell H: Shared idiotypic determinants on B and T lymphocytes reactive against the same antigenic determinants. V. Biochemical and serological characteristics of naturally occurring antigen-binding T lymphocyte-derived molecules. Scand J Immunol 5: 559–571, 1976.

    Google Scholar 

  57. Hirai Y, Nisonoff A: Selective suppression of the major idiotypic component of an antihapten response by soluble T cell-derived factors with idiotypic or anti-idiotypic receptors. J Exp Med 151: 1213–1231, 1980.

    Google Scholar 

  58. Taniguchi M, Takei I, Tada T: Functional and molecular organisation of an antigen-specific suppressor factor from a T-cell hybridoma. Nature (London) 283: 227–228, 1981.

    Google Scholar 

  59. Tokuhisa T, Taniguchi M: Constant region determinants in the antigen-binding chain of the suppressor T-cell factor. Nature (London) 298: 174–176, 1982.

    Google Scholar 

  60. Garvey JS, Cremer NE, Sussdorf DH: Methods in Immunology. W.A. Benjamin, Inc, Reading, Massachusetts, 1977, pp 133–188.

    Google Scholar 

  61. Kristiansen T: Matrix-bound antibodies. In: Hoffman-Ostenhof O, (ed). Affinity Chromatography. Pergamon Press, Oxford, 1978, pp 191–206.

    Google Scholar 

  62. Zoller M, Matzku S: Antigen and antibody purification by immunoadsorption: elimination of non-biospecifically bound proteins. J Immunol Methods 11: 287–295, 1976.

    Google Scholar 

  63. Siekevitz M, Gefter ML, Brodeur P, Riblet R, MarshakRothstein A: The genetic basis of antibody production: the dominant anti-arsonate idiotype response of the strain A mouse. Eur J Immunol 12: 1023–1032, 1982.

    Google Scholar 

  64. Kohler G, Milstein C: Continuous cultures of fused cells secreting antibody of predefined specificity. Nature (London) 256: 495–497, 1975.

    Google Scholar 

  65. Hurrell JGR: Monoclonal Hybridoma Antibodies: Techniques and Applications. CRC Press, Inc, Boca Raton, Florida, 1982.

    Google Scholar 

  66. Simmons JG, Hutt-Fletcher M, Fowler E, Feighny RJ: Studies of the Epstein-Barr virus receptor found on Raji cells. I. Extraction of receptor and preparation of anti-receptor antibody. J Immunol 130: 1303–1308, 1983.

    Google Scholar 

  67. Leonard WJ, Depper JM, Robb RJ, Waldmann TA, Greene WC: Characterization of the human receptor for T-cell growth factor. Proc Natl Acad Sci USA 80: 6957–6961, 1983.

    Google Scholar 

  68. Southern EM: Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol 98: 503–517, 1975.

    CAS  PubMed  Google Scholar 

  69. Renant JR, Reiser J, Stark GR: Transfer of proteins from gels to diazobenzyloxymethyl-paper and detection with antisera: a method for studying antibody specificity and antigen structure. Proc Natl Acad Sci USA 76: 3116–3120, 1979.

    Google Scholar 

  70. Young-Kaplan BR, Ashman RF: Order of events leading to surface immunoglobulin capping: analysis of a transmembrane signal. J Immunol 123: 1177–1181, 1981.

    Google Scholar 

  71. Williams JM, Shapiro HM, Milford EL, Strom TB: Multiparameter flow cytometric analysis of lymphocyte subpopulation activation in lectin-stimulated cultures. J Immunol 128: 2676–2681, 1982.

    Google Scholar 

  72. Krishan A: Rapid flow cytofluorometric analysis of mammalian cell cycle by propidium iodide staining. J Cell Biol 66: 188–193, 1974.

    Google Scholar 

  73. Monroe JG, Havran WL, Cambier JC:Blymphocyte activation: entry into cell cycle is accompanied by decreased expression of IgD but not IgM. Eur J Immunol 13: 208–213, 1983.

    Google Scholar 

  74. Monroe JG, Cambier JC: Sorting of B lymphoblasts based upon cell diameter provides cell populations enriched in different stages of cell cycle. J Immunol Methods 63: 45–56, 1983.

    Google Scholar 

  75. Hunter WM: Radioimmunoassay. In: Weir DM (ed). Handbook of Experimental Immunology, third ed, Vol 1. Blackwell Scientific Publications, Oxford, 1978, pp 14.1–14.40.

    Google Scholar 

  76. Carroll AM, Zalutsky M, Schatten S, Perry LL, Bhan A, Sobotka C, Benacerraf B, Greene MI: Monoclonal antibodies to tissue-specific cell surface antigens. I. Characterization of an antibody to a prostate tissue antigen. Cancer Res (submitted).

  77. Marchalonis JJ: An enzymatic method for the trace iodination of immunoglobulin and other proteins. Biochem J 112: 299–305, 1969.

    Google Scholar 

  78. Termer AJ, Lesavre PH, Cooper NR: Purification and radiolabeling of human Clq. J Immunol 127: 648–653, 1981.

    Google Scholar 

  79. Kanellopoulos J, Rossi G, Metzger H: Preparative isolation of the cell receptor for immunoglobulin E. J Biol Chem 254: 7691–7697, 1979.

    Google Scholar 

  80. Mory Y, Chernajovsky Y, Feinstein SI, Chen L, Nir U, Weissenbach J, Malpiece Y, Tiollais P, Marks D, Ladner M, Colby C, Revel M: Synthesis of human interferon Blin Escherichia coli infected by a lambda phage recombinant containing a human genomic fragment. Eur J Biochem 120: 197–202, 1981.

    Google Scholar 

  81. Anderson D, Shapiro L, Shalka AM: In situ immunoassays for translation products. In: Wu R (ed). Methods in Enzymology, Vol 68. Academic Press, New York, 1979, pp 428–436.

    Google Scholar 

  82. Henning U, Royer H-D, Teather RM, Hindennach I, Hollenberg CP: Cloning of the structural gene (omp A) for an integral outer membrane protein of Escherichia coli K-12. Proc Natl Acad Sci USA 76: 4360–4364, 1979.

    Google Scholar 

  83. Young RA, Davis RW: Efficient isolation of genes using antibody probes. Proc Natl Acad Sci USA 80: 1194–1198, 1983.

    Google Scholar 

  84. Kemp DJ, Coppel RL, Cowman AF, Saint RB, Brown GV, Anders RF: Expression of Plasmodium falciparum blood-stage antigens in Escherichia coli: detection with antibodies from immune humans. Proc Natl Acad Sci USA 80: 3787–3791, 1983.

    Google Scholar 

  85. Kaplan DA, Greenfield L, Collier RJ: Chromogenic method to screen very large populations of bacteriophage plaques for the presence of specific antigen. In: Wu, R, Moldave K (eds). Methods in Enzymology, Vol 100. Academic Press, New York, 1983, pp 342–368.

    Google Scholar 

  86. Casadaban MJ, Martinez-Arias A, Shapira SK, Chou J: B-galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast. In: Wu R, Grossman L, Moldave L (eds). Methods in Enzymology, Vol 100. Academic Press, New York, 1983, pp 293–328.

    Google Scholar 

  87. Villa-Kamaroff L, Efstratiadis A, Broome S, Lomedico P, Tizard R, Naber SP, Chick WL, Gilbert W: A bacterial clone synthesizing proinsulin. Proc Natl Acad Sci USA 75: 3727–3731, 1978.

    Google Scholar 

  88. Clarke L, Hitzeman R, Carbon J: Selection of specific, clones from colony banks by screening with radioactive antibody. In: Wu R (ed). Methods in Enzymology, Vol 68. Academic Press, New York, 1979, pp 436–442.

    Google Scholar 

  89. Erlich HA, Cohen SN, McDevitt HO: Immunological detection and characterization of products translated from cloned DNA fragments. In: Wu R (ed). Methods in Enzymology, Vol 68. Academic Press, New York, 1979, pp 443–453.

    Google Scholar 

  90. Kemp DJ, Cowan AF: Direct immunoassay for detecting Escherichia coli colonies that contain polypeptides encoded by cloned DNA segments. Proc Natl Acad Sci USA 78: 4520–4524, 1981.

    Google Scholar 

  91. Melcher U: The purification of B-glactosidase-specific polysomes by affinity chromatography. Anal Biochem 64: 461–465, 1975.

    Google Scholar 

  92. Eschenfeldt WH, Patterson RJ: Do antibody binding techniques identify polysomes synthesizing a specific protein. Biochem Biophys Res Commun 67: 935–945, 1975.

    Google Scholar 

  93. Groner B, Hynes NE, Sippel AE, Jeep S, Hun MCN, Schutz G: Immunoadsorption of specific chicken oviduct polysomes. J Biol Chem 252: 6666–6674, 1977.

    Google Scholar 

  94. Shapiro SZ, Young JR: An immunochemical method for mRNA purification. J Biol Chem 256: 1495–1498, 1981.

    Google Scholar 

  95. Boyer SH, Smith KD, Noyes AN, Young KE: Adjuvants to immunological methods for mRNA purification. J Biol Chem 258: 2068–2071, 1983.

    Google Scholar 

  96. Korman AJ, Knudsen PJ, Kaufman JF, Strominger JL: cDNA clones for the heavy chain of HLA-DR antigens obtained after immunopurification of polysomes by monoclonal antibody. Proc Natl Acad Sci USA 79: 1844–1848, 1982.

    Google Scholar 

  97. Robson KJH, Chandra T, MacGillivray RTA, Woo SLC: Polysomeimmunoprecipitation of henylalaninehydroxy-lase mRNA from rat liver and cloning of its cDNA. Proc Natl Acad Sci USA 79: 4701–4705, 1982.

    Google Scholar 

  98. Gonzales FJ, Kasper CB: Cloning of epoxide hydratase complementary DNA. J Biol Chem 256: 4697–4700, 1981.

    Google Scholar 

  99. Kraus JP, Rosenberg LE: Purification of low-abundance messenger RNAs from rat liver by polysome immunoadsorption. Proc Natl Acad Sci USA 79: 4015–4019, 1982.

    Google Scholar 

  100. Gurdon JB, Wickens MP: The use of Xenopus oocytes for the expression of cloned genes. In: Wu R, Grossman L, Moldave K (eds). Methods in Enzymology, Vol 101. Academic Press, New York, 1983, pp 370–386.

    Google Scholar 

  101. Gaulton GN, Triplett EL: Control of tyrosinase gene expression and its relationship to neural crest induction in Rana pipiens. I. Isolation and characterization of amphi bian tyrosinase mRNA. J Biol Chem 258: 14839–14844, 1983.

    Google Scholar 

  102. Shapiro DJ, Baker HJ: Purification and characterization of Xenopus laevis vitellogenin messenger RNA. J Biol Chem 252: 5244–5250, 1977.

    Google Scholar 

  103. Graham FL, Van der Eb A: A new technique for the assay for infectivity of human adenovirus 5 DNA. J Virol 52: 455–467, 1973.

    Google Scholar 

  104. Shen Y-M, Hirschhorn RR, Mercer WE, Surmacz E, Tsutsui Y, Soprano KJ, Baserga R: Gene transfer: DNA microinjection compared with DNA transfection with a very high efficiency. Mol Cell Biol 2: 1145–1154, 1982.

    Google Scholar 

  105. Szybalski W, Szybalski EH, Ragni G: Genetic studies with human cell lines. In: Syverton Memorial Symposium. Analytic Cell Culture. Natl Cancer Inst Monogr 7: 75–89, 1962.

  106. Perucho M, Hanahan D, Wigler M: Genetic and physical linkage of exogenous sequences in transformed cells. Cell 22: 309–317, 1980.

    Google Scholar 

  107. Kavathas P, Herzenberg L: Stable transformation of mouse L cells for human membrane T-cell differentiation antigens, HLA and B2 microglobulin: selection by fluores cence-activated cell sorting. Proc Natl Acad Sci USA 80: 524–528, 1983.

    Google Scholar 

  108. Barbosa JA, Kamarck ME, Biro PA, Weissman SM, Ruddle FH: Identification of human genomic clones coding the major histocompatibility antigens HLA-A2 and HLA-B7 by DNA-mediated gene transfer. Proc Natl Acad Sci USA 79: 6327–6331, 1982.

    Google Scholar 

  109. Woodward JG, Orn A, Harmon RC, Goodenow RS, Hood L, Frelinger JA: Specific recognition of the product of a transferred major histocompatibility complex gene by cytotoxic T lymphocytes. Proc Natl Acad Sci USA 79: 3613–3617, 1982.

    Google Scholar 

  110. Goldfarb M, Shimizu K, Perucho M, Wigler M: Isolation and preliminary characterization of a human transforming gene from T24 bladder carcinoma cells. Nature (London) 296: 404–409, 1982.

    Google Scholar 

  111. Di Maio D, Treisman R, Maniatis T: Bovine papillomavirus vector that propagates as a plasmid in both mouse and bacterial cells. Proc Natl Acad Sci USA 79: 4030–4034, 1982.

    Google Scholar 

  112. Schaffner W: Direct transfer of cloned genes from bacteria to mammalian cells. Proc Natl Acad Sci USA 77: 2163–2167, 1980.

    Google Scholar 

  113. Mulligan RC, Berg P: Expression of a bacterial gene in mammalian cells. Science 209: 1422–1427, 1980.

    Google Scholar 

  114. Southern PJ, Berg P: Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J Mol Appl Genet 1: 327–341, 1982.

    Google Scholar 

  115. Agarwal KL, Brumstedt J, Noyes BE: A general method for detection and characterization of an mRNA using an oligonucelotide probe. J Biol Chem 156: 1023–1028, 1981.

    Google Scholar 

  116. Suggs SV, Wallaace RB, Hirose T, Kawashima EH, Itakura K: Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human B2-microglobulin. Proc Natl Acad Sci USA 78: 6613–6617, 1981.

    Google Scholar 

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Dr. Gaulton received the NRSA Viral Oncology Training Grant t# CA 09031.

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Gaulton, G.N., Co, M.S., Royer, HD. et al. Anti-idiotypic antibodies as probes of cell surface receptors. Mol Cell Biochem 65, 5–21 (1984). https://doi.org/10.1007/BF00226015

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