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
. 1978 Jul;75(7):3390–3394. doi: 10.1073/pnas.75.7.3390

Primary structure of murine major histocompatibility complex alloantigens: Amino acid sequence studies of the cyanogen bromide fragments of the H-2Kb glycoprotein*

J E Coligan †, T J Kindt †, B M Ewenstein ‡, H Uehara ‡, T Nisizawa ‡,§, S G Nathenson ‡
PMCID: PMC392782  PMID: 277939

Abstract

Radiochemical microtechniques have been used in the amino acid sequence analysis of five major CNBr fragments of the glycoprotein specified by the murine major histocompatibility complex gene H-2kb. These fragments have been tentatively aligned and represent the NH2-terminal 80% of the intact molecule. All amino acids except Asp, Asn, and Gln have been assigned in 128 out of 149 possible positions in the NH2-terminal portions of each of these fragments. These assignments, which represent approximately 50% of the total sequence from these fragments, are listed below in the order of their alignment in the intact H-2Kb molecule: IIIn, -PHSLRYFVTAVSRP(G)L(G)(E)PRYM; IIIa, EVGYV--TEFVRF-S-AE(A)PRYEPR(A)--M; Ib, E-EGPEYWERET-KAK(G)-E-SFR--LRTLL(G)YY--TK; Ia, AALITK-KWE-AGEAERLRAYLEGTC-E-L; Ic, ELVETRPAG-GTF-KWAS-VVPLGKE-YY(T). The unassigned positions represented by dashes in the above sequences may be tentatively assigned as Asp, Asn, or Gln.

The NH2-terminal sequence obtained for the H-2Kb molecule was compared to the limited sequence information available for other major histocompatibility complex gene products. An 84% homology (16 of 19 residues) to the H-2Kq and H-2Kk molecules, which are identical to one another in the positions compared, was observed. A similar comparison with 28 of the 31 NH2-terminal residues of HLA-B7 indicated 68% homology. Furthermore, significant homology was observed between H-Kb and HLA-B7 in a region of glycosylation, which occurs between positions 85 and 100 in the two molecules.

Keywords: histocompatibility antigens, radiolabeling, immunoprecipitation

Full text

PDF
3392

Selected References

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

  1. Brown J. L., Kato K., Silver J., Nathenson S. G. Notable diversity in peptide composition of murine H-2K and H-2D alloantigens. Biochemistry. 1974 Jul 16;13(15):3174–3178. doi: 10.1021/bi00712a027. [DOI] [PubMed] [Google Scholar]
  2. Cullen S. E., Freed J. H., Nathenson S. G. Structural and serological properties of murine Ia alloantigens. Transplant Rev. 1976;30:236–270. doi: 10.1111/j.1600-065x.1976.tb00222.x. [DOI] [PubMed] [Google Scholar]
  3. Ewenstein B. M., Nisizawa T., Uehara H., Nathenson S. G., Coligan J. E., Kindt T. J. Primary structure of murine major histocompatibility complex alloantigens: isolation, biochemical characterization, and preliminary alignment of CNBr fragments from the H-2Ib glycoprotein. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2909–2913. doi: 10.1073/pnas.75.6.2909. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Klapper D. G., Wilde C. E., 3rd, Capra J. D. Automated amino acid sequence of small peptides utilizing Polybrene. Anal Biochem. 1978 Mar;85(1):126–131. doi: 10.1016/0003-2697(78)90282-8. [DOI] [PubMed] [Google Scholar]
  5. McMillan M., Cecka J. M., Murphy D. B., McDevitt H. O., Hood L. Structure of murine Ia antigens: partial NH2-terminal amino acid sequences of products of the I-E or I-C subregion. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5135–5139. doi: 10.1073/pnas.74.11.5135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Nathenson S. G., Brown J. L., Ewenstein B. M., Nisizawa T., Sears D. W., Freed J. H. Structural differences between parent and variant H-2K glycoproteins from mouse strains carrying H-2 gene mutations. Cold Spring Harb Symp Quant Biol. 1977;41(Pt 1):343–349. doi: 10.1101/sqb.1977.041.01.041. [DOI] [PubMed] [Google Scholar]
  7. Ostberg L., Rask L., Wigzell H., Peterson P. A. Thymus leukaemia antigen contains beta2-microglobulin. Nature. 1975 Feb 27;253(5494):735–737. doi: 10.1038/253735a0. [DOI] [PubMed] [Google Scholar]
  8. Parham P., Alpert B. N., Orr H. T., Strominger J. L. Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation. J Biol Chem. 1977 Nov 10;252(21):7555–7567. [PubMed] [Google Scholar]
  9. Paul W. E., Benacerraf B. Functional specificity of thymus- dependent lymphocytes. Science. 1977 Mar 25;195(4284):1293–1300. doi: 10.1126/science.320663. [DOI] [PubMed] [Google Scholar]
  10. Schwartz B. D., Kato K., Cullen S. E., Nathenson S. G. H-2 histocompatibility alloantigens. Some biochemical properties of the molecules solubilized by NP-40 detergent. Biochemistry. 1973 May 22;12(11):2157–2164. doi: 10.1021/bi00735a023. [DOI] [PubMed] [Google Scholar]
  11. Schwartz B. D., Nathenson S. G. Isolation of H-2 alloantigens solubilized by the detergent NP-40. J Immunol. 1971 Nov;107(5):1363–1367. [PubMed] [Google Scholar]
  12. 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. Biochemistry. 1969 Oct;8(10):4048–4062. doi: 10.1021/bi00838a023. [DOI] [PubMed] [Google Scholar]
  13. Shreffler D. C., David C. S. The H-2 major histocompatibility complex and the I immune response region: genetic variation, function, and organization. Adv Immunol. 1975;20:125–195. doi: 10.1016/s0065-2776(08)60208-4. [DOI] [PubMed] [Google Scholar]
  14. Silver J., Russell W. A., Reis B. L., Frelinger J. A. Chemical characterization of murine Ia alloantigens determined by the i-E/i-C subregions of the H-2 complex. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5131–5134. doi: 10.1073/pnas.74.11.5131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Terhorst C., Robb R., Jones C., Strominger J. L. Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins. Proc Natl Acad Sci U S A. 1977 Sep;74(9):4002–4006. doi: 10.1073/pnas.74.9.4002. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Vitetta E. S., Capra J. D. The protein products of the murine 17th chromosome: genetics and structure. Adv Immunol. 1978;26:147–193. doi: 10.1016/s0065-2776(08)60230-8. [DOI] [PubMed] [Google Scholar]
  18. Vitetta E., Uhr J. W., Boyse E. A. Isolation and characterization of H-2 and TL alloantigens from the surface of mouse lymphocytes. Cell Immunol. 1972 Jun;4(2):187–191. doi: 10.1016/0008-8749(72)90019-6. [DOI] [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