H–2-linked low-molecular weight polypeptide antigens assemble into an unusual macromolecular complex (original) (raw)

Nature volume 309, pages 797–799 (1984)Cite this article

Abstract

The major histocompatibility complex (MHC) is a cluster of tightly linked genes whose products are of central importance in the functioning of the immune system. Class I and II MHC antigens are integral membrane proteins which regulate cell-surface interactions between T cells and their targets1–3, while class III antigens are components of the complement system of serum proteins4. All available evidence indicates that the structure and function of the MHC and its gene products are highly conserved among species (for review, see ref. 5). We recently reported6 the existence in murine cells of a fourth class of MHC-linked polypeptides which are biochemically and genetically distinct from previously identified MHC gene products: BALB.B anti-BALB/c (anti-H–2d) antiserum immunoprecipitates a set of 16 cytoplasmic low-molecular weight polypeptides (LMP) from BALB/c spleen cells and from the WEHI-3 cell line. The production of these peptides is coordinately regulated (by immune interferon) with the production of the class I and II MHC antigens7,8, suggesting that they too are functionally relevant to the immune system. We demonstrate here that these 16 polypeptides are associated with one another in vivo as a very large (580,000-molecular weight, _M_r) noncovalent complex. The unusual nature of this complex has allowed the non-immunochemical identification of similar complexes from (serologically negative) H–2b murine cells and from a human cell line. Thus, LMP antigens display two properties in common with other MHC antigens: they are both polymorphic and genetically conserved across species.

This is a preview of subscription content, access via your institution

Access options

Subscribe to this journal

Receive 51 print issues and online access

$199.00 per year

only $3.90 per issue

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Additional access options:

Similar content being viewed by others

References

  1. Zinkernagel, R. M. & Doherty, P. C. Adv. Immun. 27, 51–177 (1980).
    Article Google Scholar
  2. Rosenthal, A. S. Immun. Rev. 40, 136–152 (1978).
    Article CAS Google Scholar
  3. Klein, J., Juretic, A., Baxevanis, C. N. & Nagy, Z. A. Nature 291, 455–460 (1981).
    Article ADS CAS Google Scholar
  4. Shreffler, D. C. Transplantn Rev. 32, 140–167 (1976).
    CAS Google Scholar
  5. Goetze, D. (ed.) The Major Histocompatibility System in Man and Animals (Springer, Berlin, 1977).
  6. Monaco, J. J. & McDevitt, H. O. Proc. natn. Acad. Sci. U.S.A. 79, 3001–3005 (1982).
    Article ADS CAS Google Scholar
  7. Monaco, J. J., Ku, G. & McDevitt, H. O. in Ir Genes: Past, Present and Future (eds Pierce, C. W., Cullen, S. E., Kapp, J. A., Schwarte, B. D. & Shreffler, D. C.) 69–73 (Humana, Clifton, New Jersey, 1983).
    Book Google Scholar
  8. Monaco, J. J. & McDevitt, H. O. J. Immun. (submitted).
  9. Mauel, J. & Defendi, V. J. exp. Med. 134, 335–350 (1971).
    Article CAS Google Scholar
  10. Lanier, L. L. et al. Immunogenetics 16, 367–371 (1982).
    Article CAS Google Scholar
  11. Ralph, P., Moore, M. A. S. & Nilsson, K. J. exp. Med. 143, 1528–1533 (1976).
    Article CAS Google Scholar
  12. Wool, I. G. A. Rev. Biochem. 48, 719–754 (1979).
    Article CAS Google Scholar

Download references

Author information

Authors and Affiliations

  1. Department of Medical Microbiology, Stanford University School of Medicine, Stanford, California, 94305, USA
    John J. Monaco & Hugh O. McDevitt

Authors

  1. John J. Monaco
    You can also search for this author inPubMed Google Scholar
  2. Hugh O. McDevitt
    You can also search for this author inPubMed Google Scholar

Rights and permissions

About this article

Cite this article

Monaco, J., McDevitt, H. H–2-linked low-molecular weight polypeptide antigens assemble into an unusual macromolecular complex.Nature 309, 797–799 (1984). https://doi.org/10.1038/309797a0

Download citation