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Engineering soluble major histocompatibility molecules: Why and how

  • Structure and Function of Major Histocompatibility Complex Class I Genes and Proteins (Part I), Symposium
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References

  1. Shimada, A.; Nathenson, S.G.: Murine histocompatibility-2 (H-2) alloantigens. Purification and some chemical properties of soluble products from H-2b and H-2d genotypes released by papain digestion of membrane fractions. Biochemistry8: 4048–4062 (1969).

    Article  PubMed  CAS  Google Scholar 

  2. Tarner, M.J.; Cresswell, P.; Parham, P.; Mann, D.L.; Sanderson, A.R.; Strominger, J.L.: Purification and some properties of papain solubilized histocompatibility antigens from a cultured human lymphoblastoid line RPMI 4265. J. biol. Chem.250: 4512–4519 (1975).

    Google Scholar 

  3. Springer, T.A.; Mann, D.L.; DeFranco, A.L.; Strominger, J.L.: Detergent solubilization, purification, and separation of specificities of HLA antigens from a cultured human lymphoblastoid line, RPMI 4265. J. biol. Chem.252: 4682–4693 (1977).

    PubMed  CAS  Google Scholar 

  4. Zuniga, M.; Hood, L.: Clonal variation in cell surface display of an H-2 protein lacking a cytoplasmic tail. J. Cell Biol.102: 1–10 (1986).

    Article  PubMed  CAS  Google Scholar 

  5. Arnold, B.; Tucker, M.J.; Hämmerling, G.J.: Secretion of H-2K antigens by B cell myeloma after transfection with modified genes (Abstract No. 2.31.17). 6th Int. Congr. Immunology, Toronto, 1986.

  6. Margulies, D.H.; Ramsey, A.L.; Boyd, L.F.; McCluskey, J.: Genetic engineering of an H-2Dd/Q10b chimeric histocompatibility antigen: purification of soluble protein from transformant cell supernatants. Proc. natn. Acad. Sci. USA83: 5252–5256 (1986).

    Article  CAS  Google Scholar 

  7. Snell, G.D.; Dausset, J.; Nathenson, S.G.: Histocompatibility (Academic Press, New York 1976).

    Google Scholar 

  8. Lew, A.M.; Lillehoj, E.P.; Cowan, E.P.; Maloy, W.L.; vanSchraendijk, M.R.; Coligan, J.E.: Class I genes and molecules: an update. Immunology57: 3–18 (1986).

    PubMed  CAS  Google Scholar 

  9. Hood, L.; Steinmetz, M.; Malissen, B.: Genes of the major histocompatibility complex of the mouse. Annu. Rev. Immunol.1: 529–568 (1983).

    Article  PubMed  CAS  Google Scholar 

  10. Klein, J.; Figueroa, F.: The evolution of MHC class I genes. Immunol. today7: 41–44 (1986).

    CAS  Google Scholar 

  11. Flaherty, L.: Tla-region antigens; in Dorf The role of the major histocompatibility complex in immunology, pp. 33–57 (Garland STPM. New York 1981).

    Google Scholar 

  12. Nathenson, S.G.; Geliebter, J.; Pfaffenbach, G.M.; Zeff, R.A.: Murine major histocompatibility complex class-I mutants: molecular analysis and structure-functions implications. Annu. Rev. Immunol.4: 471–502 (1986).

    Article  PubMed  CAS  Google Scholar 

  13. Malissen, B.: Transfer and expression of MHC genes. Immunol. today7: 106–112 (1986).

    CAS  Google Scholar 

  14. Margulies, D.H.; McCluskey, J.: Exon, shuffling: new genes from old. Surv. immunol. Res.4: 146–159 (1985).

    PubMed  CAS  Google Scholar 

  15. McCluskey, J.; Boyd, L.; Foo, M.; Forman, J.; Margulies, D.H.; Bluestone, J.A.: Analysis of hybrid H-2D and L antigens with reciprocally mismatched aminoterminal domains: functional T cell recognition requires preservation of fine structural determinants. J. Immun.137: 3881–3890 (1986).

    PubMed  CAS  Google Scholar 

  16. Steinmetz, M.; Hood, L.: Genes of the major histocompatibility complex in mouse and man. Science222: 727–733 (1983).

    Article  PubMed  CAS  Google Scholar 

  17. Schwartz, R.H.: Immune response (Ir) genes of the murine major histocompatibility complex. Adv. Immunol.38: 31–201 (1986).

    Article  PubMed  CAS  Google Scholar 

  18. Babbitt, B.P.; Matsueda, G.; Haber, E.; Unanue, E.; Allen, P.M.: Antigenic competition at the level of peptide-Ia binding. Proc. natn. Acad. Sci. USA83: 4509–4513 (1986).

    Article  CAS  Google Scholar 

  19. Babbitt, B.P.; Allen, P.M.; Matsueda, G.; Haber, E.; Unanue, E.: Binding of immunogenic peptides to Ia histocompatibility molecules. Nature317: 359–361 (1985).

    Article  PubMed  CAS  Google Scholar 

  20. Buus, S.; Colon, S.; Smith, C.; Freed, J.H.; Miles, C.; Grey, H.M.: Interaction between a ‘processed’ ovalbumin peptide and Ia molecules. Proc. natn. Acad. Sci. USA83: 3968–3971 (1986).

    Article  CAS  Google Scholar 

  21. Watts, T.H.; Brian, A.A.; Kappler, J.W.; Marrack, P.; McConnell, H.M.: Antigen presentation by supported planar membranes containing affinity purified I-Ad. Proc. natn. Acad. Sci. USA81: 7564–7568 (1984).

    Article  CAS  Google Scholar 

  22. Watts, T.H.; Gaub, H.E.; McConnell, H.M.: T-cell-mediated association of peptide antigen and major histocompatibility complex protein by energy transfer in an evanescent wave-field. Nature320: 179–181 (1986).

    Article  PubMed  CAS  Google Scholar 

  23. Bjorkman, P.J.; Strominger, J.L.; Wiley, D.: Crystallization and X-ray diffraction studies on the histocompatibility antigens HLA-A2 and HLA-A28 from human cell membranes. J. molec. Biol.186: 205–210 (1986).

    Article  Google Scholar 

  24. Segal, D.M.; Padlan, E.A.; Cohen, G.H.; Rudikoff, S.; Potter, M.; Davies, D.R.: The three-dimensional structure of a phosphocholine-binding mouse immunoglobulin Fab and the nature of the antigen binding site. Proc. natn. Acad. Sci. USA71: 4298–4302 (1974).

    Article  CAS  Google Scholar 

  25. Saul, F.A.; Amzel, L.M.; Poljak, R.J.: Preliminary refinement and structural analysis of the fab fragment from human immunoglobulin New at 2.0 Å. J. biol. Chem.253: 585–597 (1978).

    PubMed  CAS  Google Scholar 

  26. Amit, A.G.; Mariuzza, R.A.; Phillips, S.E.V.; Poljak, R.J.: Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science233: 747–753 (1986).

    Article  PubMed  CAS  Google Scholar 

  27. Suh, S.W.; Bhat, T.N.; Navis, M.A.; Cohen, G.H.; Rao, D.N.; Rudikoff, S.; Davies, D.R.: The galactin-binding immunoglobulin Fab J539: an X-ray diffraction study at 2.6−Å resolution. Proteins Struct. Funct. Genet.1: 74–80 (1986).

    Article  PubMed  CAS  Google Scholar 

  28. Sabatini, D.D.; Kreibich, G.; Morimoto, T.; Adesnik, M.: Mechanisms for the incorporation of proteins in membranes and organelles. J. Cell Biol.92: 1–22 (1982).

    Article  PubMed  CAS  Google Scholar 

  29. Wickner, W.T.; Lodish, H.F.: Multiple mechanisms of protein insertion into and across membranes. Science230: 400–407 (1985).

    Article  PubMed  CAS  Google Scholar 

  30. Garoff, H.: Using recombinant DNA techniques to study protein targetting in the eucaryotic cell. Annu. Rev. Cell. Biol.1: 403–445 (1985).

    Article  PubMed  CAS  Google Scholar 

  31. Farquhar, M.G.: Progress in unravelling pathways of Golgi traffic. Annu. Rev. Cell. Biol.1: 447–488 (1985).

    Article  PubMed  CAS  Google Scholar 

  32. Palade, G.: Intracellular aspects of the process of protein secretion. Science189: 347–358 (1975).

    Article  PubMed  CAS  Google Scholar 

  33. Milstein, C.; Brownlee, G.G.; Harrison, T.M.; Mathews, M.B.: A possible precursor of immunoglobulin light chains. Nature new Biol.239: 117–120 (1972).

    Article  PubMed  CAS  Google Scholar 

  34. Watson, M.E.E.: Compilation of published signal sequences. Nucl. Acids Res.12: 5145–5149 (1984).

    Article  PubMed  CAS  Google Scholar 

  35. Waller, P.; Blobel, G.: Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J. Cell Biol.91: 557–561 (1981).

    Article  Google Scholar 

  36. Walter, P.; Blobel, G.: Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature299: 691–698 (1982).

    Article  PubMed  CAS  Google Scholar 

  37. Meyer, D.I.; Krause, E.; Dobberstein, B.: Secretory protein translocation across membranes—the role of the ‘docking protein’. Nature297: 647–650 (1982).

    Article  PubMed  CAS  Google Scholar 

  38. Eilers, M.; Schatz, G.: Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature322: 228–232 (1986).

    Article  PubMed  CAS  Google Scholar 

  39. Fields, S.; Winter, G.; Brownlee, G.C.: Structure of the neuraminidase gene in human influenza virus A/PR/8/34. Nature290: 213–217 (1981).

    Article  PubMed  CAS  Google Scholar 

  40. Schneider, C.; Owen, M.J.; Banville, D.; Williams, J.G.: Primary structure of the human transferrin receptor deduced from the mRNA sequence. Nature311: 675–678 (1984).

    Article  PubMed  CAS  Google Scholar 

  41. Strubin, M.; Mach, B.; Long, E.O.: The complete sequence of the mRNA for the HLA-DR-associated invariant chain reveals a polypeptide with an unusual transmembrane polarity. Eur. molec. Biol. org. J.3: 869–872 (1984).

    CAS  Google Scholar 

  42. Holland, E.C.; Leung, J.; Drickamer, K.: Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence. Proc. natn. Acad. Sci. USA81: 7338–7342 (1984).

    Article  CAS  Google Scholar 

  43. Nathans, J.; Hogness, D.S.: Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin. Cell34: 807–814 (1983).

    Article  PubMed  CAS  Google Scholar 

  44. Young, E.F.; Ralston, E.; Blake, J.; Raniachandran, J.; Hall, Z.W.; Stroud, R.M.: Topological mapping of acetylcholine receptor: evidence for a model with five transmembrane segments and a cytoplasmic COOH-terminal peptide. Proc. natn. Acad. Sci. USA82: 626–630 (1985).

    Article  CAS  Google Scholar 

  45. Kopito, R.; Lodish, H.: Primary structure and transmembrane orientation of the murine anion exchange protein. Nature316: 234–238 (1985).

    Article  PubMed  CAS  Google Scholar 

  46. Jamieson, J.D.; Palade, G.E.: Intracellular transport of secretory proteins in the pancreatic exocrine cell. IV. Metabolic requirements. J. Cell Biol.39: 589–603 (1968).

    Article  PubMed  CAS  Google Scholar 

  47. Allen, H.; Fraser, J.; Flyer, D.; Calvin, S.; Flavell, R.A.: β2-Microglobulin is not required for cell surface expression of the murine class I histocompatibility antigen H-2Db or of a truncated H-2Db. Proc. natn. Acad. Sci. USA83: 7447–7451 (1986).

    Article  CAS  Google Scholar 

  48. Kreis, T.E.; Lodish, H.F.: Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell46: 929–937 (1986).

    Article  PubMed  CAS  Google Scholar 

  49. Gething, M.J.; McCammon, K.; Sambrook, J.: Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell46: 939–950 (1986).

    Article  PubMed  CAS  Google Scholar 

  50. Morrison, S.L.; Scharff, M.D.: Mutational events in mouse myeloma cells. CRC crit. Rev. Immunol.3: 1–22 (1981).

    CAS  Google Scholar 

  51. Pepe, V.H.; Sonenshein, G.E.; Yoshimura, M.I.; Shulman, M.J.: Gene transfer of immunoglobulin light chain restores heavy chain secretion. J. Immun.137: 2367–2372 (1986).

    PubMed  CAS  Google Scholar 

  52. Haas, I.G.; Wabl, M.: Immunoglobulin heavy chain binding protein. Nature306: 387–389 (1983).

    Article  PubMed  CAS  Google Scholar 

  53. Munro, S.; Pelham, H.R.B.: An Hsp-70-like protein in the ER: identity with the 78 kD glucoseregulated protein and immunoglobulin heavy chain binding protein. Cell46: 291–300 (1986).

    Article  PubMed  CAS  Google Scholar 

  54. Sly, W.S.; Fischer, H.D.: The phosphomannosyl recognition system for intracellular and intercellular transport of lysosomal enzymes. J. Cell Biochem.18: 67–85 (1982).

    Article  PubMed  CAS  Google Scholar 

  55. Gething, M.J.; Sambrook, J.: Construction of influenza hemagglutinin genes that code for intracellular and secreted forms of the protein. Nature300: 598–603 (1982).

    Article  PubMed  CAS  Google Scholar 

  56. Sveda, M.M.; Markoff, L.J.; Lai, C.J.: Cell surface expression of the influenza virus haemagglutinin requires the hydrophobic carboxy-terminal sequences. Cell30: 649–656 (1982).

    Article  PubMed  CAS  Google Scholar 

  57. Rose, J.K.; Bergmann, J.E.: Expression from cloned cDNA of cell-surface and secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells. Cell30: 753–762 (1982).

    Article  PubMed  CAS  Google Scholar 

  58. Bocke, J.D.; Model, P.: A prokaryotic membrane anchor sequence: carboxyl terminus of bacteriophage F1 gene III protein retains it in the membrane. Proc. natn. Acad. Sci. USA79: 5200–5204 (1982).

    Article  Google Scholar 

  59. Gottlieb, T.A.; Beaudry, G.; Rizzolo, L.; Colman, A.; Rindler, M.; Adesnik, M.; Sabatini, D.D.: Secretion of endogenous and exogenous proteins from polarized MDCK cell monolayers. Proc. natn. Acad. Sci. USA83: 2100–2104 (1986).

    Article  CAS  Google Scholar 

  60. Cosman, D.; Khoury, G.; Jay, G.: Tissue-specific expression of an unusual H-2 (class I)-related gene. Proc. natn. Acad. Sci. USA79: 4947–4951 (1982).

    Article  CAS  Google Scholar 

  61. Kress, M.; Cosman, D.; Khoury, G.; Jay, G.: Secretion of a transplantation-related antigen. Cell34: 189–196 (1983).

    Article  PubMed  CAS  Google Scholar 

  62. Mellor, A.L.; Weiss, E.H.; Kress, M.; Jay, G.; Flavell, R.A.: A non-polymorphic class I gene in the murine major histocompatibility complex. Cell36: 139–144 (1984).

    Article  PubMed  CAS  Google Scholar 

  63. Maloy, W.L.; Coligan, J.E.; Barra, Y.; Jay, G.: Detection of a secreted form of the murine H-2 class I antigen with an antibody against its predicted carboxyl terminus. Proc. natn. Acad. Sci. USA81: 1216–1220 (1984).

    Article  CAS  Google Scholar 

  64. Devlin, J.J.; Lew, A.M.; Flavell, R.A.; Coligan, J.E.: Secretion of a soluble class I molecule encoded by the Q10 gene of the C57BL/10 mouse. Eur. molec. Biol. org. J.4: 369–374 (1985).

    CAS  Google Scholar 

  65. Barra, Y.; Tanaka, K.; Isselbacher, K.; Khoury, G.; Jay, G.: Stable transfer and restricted expression of a cloned class I gene encoding a secreted transplantation-like antigen. Mol. cell. Biol.5: 1295–1300 (1985).

    PubMed  CAS  Google Scholar 

  66. Lew, A.M.; Maloy, W.L.; Coligan, J.E.: Characteristics of the expression of the murine soluble class I molecule (Q10). J. Immun.136: 254–258 (1986).

    PubMed  CAS  Google Scholar 

  67. Lew, A.M.; Valas, R.B.; Maloy, W.L.; Coligan, J.E.: A soluble class I molecule analagous to mouse Q10 in the horse and related species. Immunogenetics23: 277–283 (1986).

    Article  PubMed  CAS  Google Scholar 

  68. Krangel, M.S.; Pious, D.; Strominger, J.L.: Characterization of a B lymphoblastoid line that secretes HLA-A2. J. Immun.132: 2984–2991 (1984).

    PubMed  CAS  Google Scholar 

  69. Krangel, M.S.: Secretion of HLA-A and-B antigens via an alternative RNA splicing pathway. J. exp. Med.163: 1173–1190 (1986).

    Article  PubMed  CAS  Google Scholar 

  70. Kyte, J.; Doolittle, R.F.: A simple method for displaying the hydropathic character of a protein. J. molec. Biol.157: 105–132 (1982).

    Article  PubMed  CAS  Google Scholar 

  71. Schimke, R.T.: Gene amplication in cultured animal cells. Cell37: 705–713 (1984).

    Article  PubMed  CAS  Google Scholar 

  72. Montoya-Zavala, M.; Hamlin, J.L.: Similar 150-kilobase DNA sequences are amplified in independently derived methotrexate-resistant Chinese hamster cells. Mol. cell. Biol.5: 619–627 (1985).

    PubMed  CAS  Google Scholar 

  73. Ringold, G.M.; Yamamoto, K.R.; Bishop, J.M.; Varmus, H.E.: Glucocorticoid-stimulated accumulation of mouse mammary tumor virus RNA: increased rate of synthesis of viral RNA. Proc. natn. Acad. Sci. USA74: 2879–2883 (1977).

    Article  CAS  Google Scholar 

  74. Pavlakis, G.N.; Dean, H.; Hamer, D.H.: Regulation of a metallothionein-growth hormone hybrid gene in bovine papilloma virus. Proc. natn. Acad. Sci. USA80: 397–401 (1983).

    Article  CAS  Google Scholar 

  75. Calame, K.L.: Mechanisms that regulate immunoglobulin gene expression. Annu. Rev. Immunol.3: 159–195 (1985).

    Article  PubMed  CAS  Google Scholar 

  76. Garcia, J.V.; Bich-Thuy, L.T.; Stafford, J.; Queen, C.: Synergism between immunoglobulin enhancers and promoters. Nature322: 383–385 (1986).

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 20892, Bethesda, MD, (USA)

    David H. Margulies, Richard Lopez, Lisa F. Boyd & James McCluskey

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  1. David H. Margulies
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  2. Richard Lopez
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  4. James McCluskey
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Margulies, D.H., Lopez, R., Boyd, L.F. et al. Engineering soluble major histocompatibility molecules: Why and how. Immunol Res 6, 101–116 (1987). https://doi.org/10.1007/BF02918107

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