Structure of H-2 Major Histocompatibility Complex Products

Recent Studies on the H-2Kb Glycoprotein and on the H-2Kb MHC Mutants
  • Stanley G. Nathenson
  • Bruce M. Ewenstein
  • Hiroshi Uehara
  • John M. Martinko
  • John E. Coligan
  • Thomas J. Kindt


The immune response is a reaction to a foreign or nonself substance. Intricately involved in this highly specific and tightly regulated protective-reaction mechanism are the gene products of the major histocompatibility complex (MHC) (Klein, 1975; Snell et al., 1976; Paul and Benacerraf, 1977; Götze, 1977; Snell, 1978). This genetic system was referred to as the H-2 locus when it was initially recognized as a determinant of transplantation acceptance or rejection nearly 45 years ago by P.A. Gorer (1936). The serological and genetic features were gradually unraveled over the ensuing years. The complexity, both in terms of number of genes and in terms of polymorphism, led to the use of the term H-2 major histocompatibility complex to refer to this chromosomal region in the mouse. Similar MHC complexes have been found in other species (Götze, 1977).


Major Histocompatibility Complex Tryptic Peptide Carbohydrate Moiety Cyanogen Bromide Partial Amino Acid Sequence 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Acton, R.T., and Lynn, J.D. (eds.), 1977, Cell Culture and Its Application, Academic Press, New York.Google Scholar
  2. Bailey, D.W., and Kohn, H.I., 1965, Inherited histocompatibility changes in progeny of irradiated and unirradiated inbred mice, Genet. Res. 6:330.PubMedCrossRefGoogle Scholar
  3. Brown, J.L., and Nathenson, S.G., 1977, Structural differences between parent and mutant H-2K glycoproteins from two H-2K gene mutants: B6.C-H-2ba (Hzl) and B6-H-2ba (M505), J. Immunol. 118:98.PubMedGoogle Scholar
  4. Brown, J.L., Kato, K., Silver, J., and Nathenson, S.G., 1974, Notable diversity in peptide composition of murine H-2K and H-2D alloantigens, Biochemistry 13:3174.PubMedCrossRefGoogle Scholar
  5. Coligan, J.E., Kindt, T.J., Ewenstein, B.M., Uehara, H., Nisizawa, T., and Nathenson, S.G., 1978, Primary structure of murine major histocompatibility complex alloantigen: Amino acid sequence studies of the cyanogen bromide fragments of the H-2Kb glycoprotein, Proc. Natl. Acad. Sci. U.S.A. 75:3390.PubMedCrossRefGoogle Scholar
  6. Coligan, J.E., Kindt, T.J., Ewenstein, B.M., Uehara, H., Martinko, J.M., and Nathenson, S.G., 1979, Further structural analysis of the murine H-2Kb glycoprotein using radiochemical methodology, Mol. Immunol. 16:3.PubMedCrossRefGoogle Scholar
  7. Cook, R.G., Vitetta, E.S., Uhr, J.W., Klein, J., Wilde, C.E., III, and Capra, J.D., 1978, Structural studies on protein products of murine chromosome 17. III. Partial amino sequence of an H-2Kq molecule, J. Immunol. 121:1015.PubMedGoogle Scholar
  8. Egorov, I.K., 1967, A mutation of the histocompatibility-2 locus in the mouse, Genetika 9:136.Google Scholar
  9. Ewenstein, B.M., Nisizawa, T., Uehara, H., Nathenson, S.G., Coligan, J.E., and Kindt, T.J., 1978, Primary structure of murine major histocompatibility complex alloantigens: Isolation, biochemical characterization and preliminary alignment of CNBr fragments from the H-2Kb glycoprotein, Proc. Natl. Acad. Sci. U.S.A. 75:2909.PubMedCrossRefGoogle Scholar
  10. Ewenstein, B.M., Uehara, H., Nisizawa, T., Nathenson, S.G., Melvold, R.W., and Kohn, H.I., 1980, Biochemical studies on the H-2K antigens of the MHC mutants bm 3 and bm 11, Immunogenetics 11:383.PubMedCrossRefGoogle Scholar
  11. Ferguson, W.S., Terhorst, C.T., Robb, R.J., and Strominger, J.L., 1979, Localization of the disulfide bridges of human histocompatibility antigens, Mol. Immunol. 16:23.PubMedCrossRefGoogle Scholar
  12. Gaily, J.A., 1973, Structure of immunoglobulins, in: The Antigens, Vol. I (M. Sela, ed.), pp. 161–298, Academic Press, New York.Google Scholar
  13. Gorer, P.A., 1936, The detection of antigenic differences in mouse erythrocytes by the employment of immune sera, Brt. J. Exp. Pathol. 17:42.Google Scholar
  14. Götze, D. (ed.), 1977, The Major Histocompatibility System in Man and Animals, Springer-Verlag, Berlin and New York.Google Scholar
  15. Gross, E., 1967, The cyanogen bromide reaction, in: Methods in Enzymology (C.H.W. Hirs, ed.), pp. 238–255, Academic Press, New York.Google Scholar
  16. Henning, R., Milner, R.J., Reske, K., Cunningham, B.A., and Edelman, G.M., 1976, Subunit structure, cell surface orientation and partial amino acid sequences of murine histocompatibility antigens, Proc. Natl. Acad. Sci. U.S.A. 73:118.PubMedCrossRefGoogle Scholar
  17. Hunkapiller, M.W., and Hood, L.E., 1978, Direct micro sequence analysis of polypeptides using an improved sequenator, a nonprotein carrier (Polybrene) and high pressure liquid chromatography, Biochemistry 17:2122.CrossRefGoogle Scholar
  18. Jacobs, J.W., Kemper, B., Niall, H.D., Habener, J.F., and Potts, J.J., Jr., 1974, Structural analysis of human proparathyroid hormone by a new micro sequencing approach, Nature (London) 249:155.CrossRefGoogle Scholar
  19. Kimball, E.S., Coligan, J.E., and Kindt, T.J., 1979, Structural characterization of antigens encoded by rabbit RLA-11 histocompatibility genes, Immunogenetics 8:201.CrossRefGoogle Scholar
  20. Klein, J., 1975, Biology of the Mouse H-2 Complex, Springer-Verlag, New York.Google Scholar
  21. Klein, J., 1978, H-2 mutations: Their genetics and effect on immune functions, Adv. Immunol. 26:55.PubMedCrossRefGoogle Scholar
  22. Kohn, H.I., Klein, J., Melvold, R.W., Nathenson, S.G., Pious, D., and Shreffler, D.C., 1978, The First H-2 Mutant Workshop, Immunogenetics 7:279.PubMedCrossRefGoogle Scholar
  23. McKean, D.J., Peters, E.H., Waldby, J.I., and Smithies, O., 1974, Amino acid sequence determination with radioactive proteins, Biochemistry 13:3048.PubMedCrossRefGoogle Scholar
  24. McKenzie, I.F.C., Pang, T., and Blanden, R.V., 1977, The use of H-2 mutants as models for the study of T cell activation, Immunol. Rev. 35:181.CrossRefGoogle Scholar
  25. Melvold, R.W., and Kohn, H.I., 1976, Eight new mutations associated with the H-2 complex, Immunogenetics 3:185.CrossRefGoogle Scholar
  26. Nathenson, S.G., and Cullen, S.E., 1974, Biochemical properties and immunochemicalgenetic relationships of mouse H-2 alloantigens, Biochim. Biophys. Acta 344:1.PubMedCrossRefGoogle Scholar
  27. Nathenson, S.G., and Muramatsu, T., 1971, Properties of the carbohydrate portion of mouse H-2 alloantigen glycoproteins, in: Glycoproteins of Blood Cells and Plasma (G.A. Jamieson and T.J. Greenwalt, eds.), pp. 245–262, J.B. Lippincott, Philadelphia.Google Scholar
  28. Natori, T., Tanagaki, N., Appella, E., and Pressman, D., 1975, Amino acid composition and physicochemical properties of mouse β2-microglobulin, Biochem. Biophys. Res. Commun. 65:611.PubMedCrossRefGoogle Scholar
  29. Nisizawa, T., Ewenstein, B.M., Uehara, H., and Nathenson, S.G., 1981, Biochemical studies on the H-2K antigen of the MHC bm 1, Immunogenetics 12:33.PubMedCrossRefGoogle Scholar
  30. Parham, P., Alpert, B.N., Orr, H.T., and Strominger, J.L., 1977, Carbohydrate moiety of HLA antigens: Antigenic properties and amino acid sequences around the site of glycoprotein, J. Biol. Chem. 252:7555.PubMedGoogle Scholar
  31. Paul, W.E., and Benacerraf, B., 1977, Functional specificity of thymus-dependent lymphocytes, Science 195:1293.PubMedCrossRefGoogle Scholar
  32. Peterson, P.A., Rask, L., Sege, K., Klareskog, L., Anundi, H., and Ostberg, L., 1975, Evolutionary relationship between immunoglobulins and transplantation antigens, Proc. Natl. Acad. Sci. U.S.A. 72:1612.PubMedCrossRefGoogle Scholar
  33. Pleogh, H.L., Orr, H.R., Robb, R., and Strominger, J.L., 1978, Structure of HLA antigens, in: Biological Markers of Neoplasia (H. Ruddon, ed.), pp. 201–211, North Holland, New York.Google Scholar
  34. Rask, L., Lindstrom, J.B., and Peterson, P.A., 1974, Subunit structure of H-2 alloantigens, Nature (London) 249:833.CrossRefGoogle Scholar
  35. Schwartz, B.D., Kato, K., Cullen, S.E., and Nathenson, S.G., 1973, H-2 histocompatibility alloantigens: Some biochemical properties of the molecules solubilized by NP-40 detergent, Biochemistry 12:2157.PubMedCrossRefGoogle Scholar
  36. Shimada, A., and Nathenson, S.G., 1969, 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, Biochemistry 8:4048.PubMedCrossRefGoogle Scholar
  37. Silver, J., and Hood, L., 1974, Detergent-solubilized H-2 alloantigen is associated with a small molecular weight polypeptide, Nature (London) 249:764.CrossRefGoogle Scholar
  38. Silver, J., and Hood, L.E., 1976, Structure and evolution of transplantation antigens: Partial amino acid sequences of H-2K and H-2D alloantigens, Proc. Natl. Acad. Sci. U.S.A. 73:599.PubMedCrossRefGoogle Scholar
  39. Snell, G.D., 1978, T-cells, T-cell recognition structures and the major histocompatibility complex, Immunol. Rev. 38:3.PubMedCrossRefGoogle Scholar
  40. Snell, G.D., Dausset, J., and Nathenson, S.G., 1976, Histocompatibility, Academic Press, New York.Google Scholar
  41. Wittman-Liebold, B., 1973, Amino acid sequence studies on 10 ribosomal proteins of E. coli with an improved sequenator equipped with an automatic conversion device, Hoppe-Seyler’s Z. Physiol. Chem. 354:1415.CrossRefGoogle Scholar
  42. Vitetta, E., and Capra, J.D., 1978, The protein products of the murine 17th chromosome: Genetics and structure, Adv. Immunol. 26:147.PubMedCrossRefGoogle Scholar
  43. Vitetta, E.S., Capra, J.D., Klapper, D.G., Klein, J., and Uhr, J.W., 1976, The partial amino acid sequence of an H-2K molecule, Proc. Natl. Acad. Sci. U.S.A. 73:905.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1981

Authors and Affiliations

  • Stanley G. Nathenson
    • 1
  • Bruce M. Ewenstein
    • 1
  • Hiroshi Uehara
    • 1
  • John M. Martinko
    • 1
  • John E. Coligan
    • 2
  • Thomas J. Kindt
    • 2
  1. 1.Department of Microbiology and Immunology and Department of Cell BiologyAlbert Einstein College of MedicineBronxUSA
  2. 2.Laboratory of ImmunogeneticsNational Institutes of HealthBethesdaUSA

Personalised recommendations