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


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, Mr) 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.

Access options

Rent or Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.


  1. 1

    Zinkernagel, R. M. & Doherty, P. C. Adv. Immun. 27, 51–177 (1980).

  2. 2

    Rosenthal, A. S. Immun. Rev. 40, 136–152 (1978).

  3. 3

    Klein, J., Juretic, A., Baxevanis, C. N. & Nagy, Z. A. Nature 291, 455–460 (1981).

  4. 4

    Shreffler, D. C. Transplantn Rev. 32, 140–167 (1976).

  5. 5

    Goetze, D. (ed.) The Major Histocompatibility System in Man and Animals (Springer, Berlin, 1977).

  6. 6

    Monaco, J. J. & McDevitt, H. O. Proc. natn. Acad. Sci. U.S.A. 79, 3001–3005 (1982).

  7. 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).

  8. 8

    Monaco, J. J. & McDevitt, H. O. J. Immun. (submitted).

  9. 9

    Mauel, J. & Defendi, V. J. exp. Med. 134, 335–350 (1971).

  10. 10

    Lanier, L. L. et al. Immunogenetics 16, 367–371 (1982).

  11. 11

    Ralph, P., Moore, M. A. S. & Nilsson, K. J. exp. Med. 143, 1528–1533 (1976).

  12. 12

    Wool, I. G. A. Rev. Biochem. 48, 719–754 (1979).

Download references

Author information



Rights and permissions

Reprints 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

Further reading


By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.