Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Mar;73(3):910–914. doi: 10.1073/pnas.73.3.910

Structure of HLA antigens: amino-acid and carbohydrate compositions and NH2-terminal sequences of four antigen preparations.

C Terhorst, P Parham, D L Mann, J L Strominger
PMCID: PMC336029  PMID: 1062804

Abstract

Amino-acid and carbohydrate compositions in addition to limited NH2-terminal sequence data of four preparations of HLA antigens, including products of both of the major histocompatibility loci (HLA-A and HLA-B), show that the antigens have great homology in the primary structure. A striking observation is that HLA antigens also have a considerable structure homology with mouse H-2 antigens. HLA antigens appear to have one carbohydrate side chain which has the same composition in all four cases. The possible relation of the structure of the heavy chain of HLA antigens to immunoglobulins is discussed, based on the limited data which are available so far.

Full text

PDF
912

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anundi H., Rask L., Ostberg L., Peterson P. A. The subunit structure of thymus leukemia antigens. Biochemistry. 1975 Nov 18;14(23):5046–5054. doi: 10.1021/bi00694a003. [DOI] [PubMed] [Google Scholar]
  2. Armerding D., Kubo R. T., Grey H. M., Katz D. H. Activation of T and B lymphocytes in vitro: presence of beta2-microblobulin determinants on allogeneic effect factor. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4577–4581. doi: 10.1073/pnas.72.11.4577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berggård I., Bearn A. G. Isolation and properties of a low molecular weight beta-2-globulin occurring in human biological fluids. J Biol Chem. 1968 Aug 10;243(15):4095–4103. [PubMed] [Google Scholar]
  4. Brauer A. W., Margolies M. N., Haber E. The application of 0.1 M quadrol to the microsequence of proteins and the sequence of tryptic peptides. Biochemistry. 1975 Jul;14(13):3029–3035. doi: 10.1021/bi00684a036. [DOI] [PubMed] [Google Scholar]
  5. Capaldi R. A., Vanderkooi G. The low polarity of many membrane proteins. Proc Natl Acad Sci U S A. 1972 Apr;69(4):930–932. doi: 10.1073/pnas.69.4.930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cresswell P., Dawson J. R. Dimeric and monomeric forms of HL-A antigens solubilized by detergent. J Immunol. 1975 Jan;114(1 Pt 2):523–525. [PubMed] [Google Scholar]
  7. Cresswell P., Springer T., Strominger J. L., Turner M. J., Grey H. M., Kubo R. T. Immunological identity of the small subunit of HL-A antigens and beta2-microglobulin and its turnover on the cell membrane. Proc Natl Acad Sci U S A. 1974 May;71(5):2123–2127. doi: 10.1073/pnas.71.5.2123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cresswell P., Turner M. J., Strominger J. L. Papain-solubilized HL-A antigens from cultured human lymphocytes contain two peptide fragments. Proc Natl Acad Sci U S A. 1973 May;70(5):1603–1607. doi: 10.1073/pnas.70.5.1603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 1967 Jul;6(7):1948–1954. doi: 10.1021/bi00859a010. [DOI] [PubMed] [Google Scholar]
  10. Fish W. W., Mann K. G., Tanford C. The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride. J Biol Chem. 1969 Sep 25;244(18):4989–4994. [PubMed] [Google Scholar]
  11. Fitch W. M., Margoliash E. Construction of phylogenetic trees. Science. 1967 Jan 20;155(3760):279–284. doi: 10.1126/science.155.3760.279. [DOI] [PubMed] [Google Scholar]
  12. Goodfellow P. N., Jones E. A., Van Heyningen V., Solomon E., Bobrow M., Miggiano V., Bodmer W. F. The beta2-microglobulin gene is on chromosome 15 and not in the HL-A region. Nature. 1975 Mar 20;254(5497):267–269. doi: 10.1038/254267a0. [DOI] [PubMed] [Google Scholar]
  13. Grey H. M., Kubo R. T., Colon S. M., Poulik M. D., Cresswell P., Springer T., Turner M., Strominger J. L. The small subunit of HL-A antigens is beta 2-microglobulin. J Exp Med. 1973 Dec 1;138(6):1608–1612. doi: 10.1084/jem.138.6.1608. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Mendez E., Lai C. Y. Regeneration of amino acids from thiazolinones formed in the Edman degradation. Anal Biochem. 1975 Sep;68(1):47–53. doi: 10.1016/0003-2697(75)90677-6. [DOI] [PubMed] [Google Scholar]
  16. Natori T., Tanigaki N., Appella E., Pressman D. Amino acid composition and physicochemical properties of mouse beta2-microglobulin. Biochem Biophys Res Commun. 1975 Jul 22;65(2):611–617. doi: 10.1016/s0006-291x(75)80190-2. [DOI] [PubMed] [Google Scholar]
  17. Parham P., Humphreys R. E., Turner M. J., Strominger J. L. Heterogeneity of HL-A antigen preparations is due to variable sialic acid content. Proc Natl Acad Sci U S A. 1974 Oct;71(10):3998–4001. doi: 10.1073/pnas.71.10.3998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Parham P., Terhorst C., Herrmann H., Humphreys R. E., Waterfield M. D., Strominger J. L. Immunological and chemical purity of papain-solubilized HL-A antigens. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1594–1598. doi: 10.1073/pnas.72.4.1594. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Peterson P. A., Cunningham B. A., Berggård I., Edelman G. M. 2 -Microglobulin--a free immunoglobulin domain. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1697–1701. doi: 10.1073/pnas.69.7.1697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Peterson P. A., Rask L., Sege K., Klareskog L., Anundi H., Ostberg L. Evolutionary relationship between immunoglobulins and transplantation antigens. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1612–1616. doi: 10.1073/pnas.72.4.1612. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sanderson A. R., Cresswell P., Welsh K. I. Involvement of carbohydrate in the immunochemical determinant area of HL-A substances. Nat New Biol. 1971 Mar 3;230(1):8–12. doi: 10.1038/newbio230008a0. [DOI] [PubMed] [Google Scholar]
  22. Silver J., Hood L. Structure and evolution of transplantation antigens: partial amino-acid sequences of H-2K and H-2D alloantigens. Proc Natl Acad Sci U S A. 1976 Feb;73(2):599–603. doi: 10.1073/pnas.73.2.599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Smithies O., Poulik M. D. Initiation of protein synthesis at an unusual position in an immunoglobulin gene? Science. 1972 Jan 14;175(4018):187–189. doi: 10.1126/science.175.4018.187. [DOI] [PubMed] [Google Scholar]
  24. Springer T. A., Strominger J. L., Mann D. Partial purification of detergent-soluble HL-A antigen and its cleavage by papain. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1539–1543. doi: 10.1073/pnas.71.4.1539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Strominger J. L., Cresswell P., Grey H., Humphreys R. E., Mann D., McCuneJ, Parham P., Robb R., Sanderson A. R., Springer T. A. The immunoglobulin-like structure of human histocompatibility antigens. Transplant Rev. 1974;21(0):126–143. doi: 10.1111/j.1600-065x.1974.tb01549.x. [DOI] [PubMed] [Google Scholar]
  26. Summers M. R., Smythers G. W., Oroszlan S. Thin-layer chromatography of sub-nanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets. Anal Biochem. 1973 Jun;53(2):624–628. doi: 10.1016/0003-2697(73)90114-0. [DOI] [PubMed] [Google Scholar]
  27. Turner M. J., Cresswell P., Parham P., Strominger J. L., Mann D. L., Sanderson A. R. Purification of papain-solubilized histocompatibility antigens from a cultured human lymphoblastoid line, RPMI 4265. J Biol Chem. 1975 Jun 25;250(12):4512–4519. [PubMed] [Google Scholar]
  28. Vitetta E. S., Artzt K., Bennett D., Boyse E. A., Jacob F. Structural similarities between a product of the T/t-locus isolated from sperm and teratoma cells, and H-2 antigens isolated from splenocytes. Proc Natl Acad Sci U S A. 1975 Aug;72(8):3215–3219. doi: 10.1073/pnas.72.8.3215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  30. Weiner A. M., Platt T., Weber K. Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis. J Biol Chem. 1972 May 25;247(10):3242–3251. [PubMed] [Google Scholar]
  31. van Someren H., Westerveld A., Hagemeijer A., Mees J. R., Meera Khan P., Zaalberg O. B. Human antigen and enzyme markers in man-Chinese hamster somatic cell hybrids: evidence for synteny between the HL-A, PGM3, ME1, and IPO-B loci. Proc Natl Acad Sci U S A. 1974 Mar;71(3):962–965. doi: 10.1073/pnas.71.3.962. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES