Abstract
INTERACTIONS between major histocompatibility complex (MHC) molecules and the CD4 or CDS coreceptors have a major role in intrathymic T-cell selection1. On mature T cells, each of these two glycoproteins is associated with a class-specific bias in MHC molecule recognition by the T-cell receptor. CD4+ T cells respond to antigen in association with MHC class II molecules and CD8+ T cells respond to antigen in association with MHC class I molecules. Physical interaction between the CD4/MHC class II molecules and CD8/MHC class I molecules has been demonstrated by cell adhesion assay2–5, and a binding site for CDS on class I has been identified6,7. Here we demonstrate that a region of the MHC class IIβ-chain β2 domain, structurally analogous to the CDS-binding loop in the MHC class I α3 domain, is critical for function with both mouse and human CD4.
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
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
von Boehmer, H. A. Rev. Immun. 6, 309–326 (1988).
Doyle, C. & Strominger, J. L. Nature 330, 256–259 (1987).
Norment, A. M., Salter, R. D., Parham, P., Engelhard, V. H. & Littman, D. R. Nature 336, 79–81 (1988).
Rosenstein, Y. Ratnofsky, S., Burakoff, S. J. & Herrmann, S. H. J. exp. Med. 169, 149–160 (1989).
Clayton, L. K., Sieh, M., Pious, D. A. & Reinherz, E. L. Nature 339, 548–551 (1989).
Potter, T. A., Rajan, T. V., Dick, R. F. II & Bluestone, J. A. Nature 337, 73–75 (1989).
Salter, R. D. et al. Nature 345, 41–46 (1990).
Lamarre, D. et al. Science 245, 743–746 (1989).
von Hoegen, P., Miceli, M. C., Tourvieille, B., Schilham, M. & Parnes, J. E. J. exp. Med. 170, 1879–1886 (1989).
Kaufman, J. F., Auffray, C., Korman, A. J., Shackelford, D. A. & Strominger, J. Cell 36, 1–13 (1984).
Travers, P., Blundell, T. L., Sternberg, M. J. E. & Bodmer, W. F. Nature 310, 235–238 (1984).
Braunstein, N. S. & Germain, R. N. Proc. natn. Acad. Sci. U.S.A. 84, 2921–2925 (1987).
Brown, J. H. et al. Nature 332, 845–850 (1988).
Gorga, J. C., et al. Proc. natn. Acad. Sci. U.S.A. 86, 2321–2325 (1989).
Lemke, H., Hämmerling, G. J. & Hämmerling, U. Immunol. Rev. 47, 175–206 (1979).
Kappler, J., Skidmore, B., White, J. & Marrack, P. J. exp. Med. 153, 1198–1214 (1981).
Bhattacharya, A., Dorf, M. E. & Springer, T. A. J. Immun. 127, 2488–2495 (1981).
Saper, M. A., Bjorkman, P. J. & Wiley, D. C. J. molec. Biol. 219, 277–319 (1991).
Wang, J. et al. Nature 348, 411–418 (1990).
Fleury, S. et al. Cell 66, 1037–1049 (1991).
Golding, H. et al. Nature 317, 425–427 (1985).
Kabat, E. A., Wu, T. T., Reid-Miller, M., Perry, H. M. & Gottesman, K. S. in Sequences of Proteins of Immunological Interest (US Department of Health and Human Services, PHS, NIH 1987).
Miller, J. & Germain, R. N. J. exp. Med. 164, 1478–1489 (1986).
Dalbadie-McFarland, G. et al. Proc. natn. Acad. Sci. U.S.A. 79, 6409–6413 (1982).
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. & Pease, L. R. Gene 77, 51–59 (1989).
Crowe, J. S. et al. Nucleic Acids Res. 19, 184 (1991).
Layet, C. & Germain, R. N. Proc. natn. Acad. Sci. U.S.A. 88, 2346–2350 (1991).
Margulies, D. H. et al. J. Immun. 130, 463–470 (1981).
Ronchese, F., Brown, M. A. & Germain, R. N. J. Immun. 139, 629–638 (1987).
Marrack, P., et al. J. exp. Med. 158, 1077–1091 (1983).
Littman, D. R. & Gettner, S. N. Nature 325, 453–455 (1987).
Zamoyska, R., Vollmer, A. C., Sizer, K. C., Liaw, C. W. & Parnes, J. R. Cell 43, 153–163 (1985).
Sleckman, B. P. et al. Nature 328, 351–353 (1987).
Ronchese, F., Schwartz, R. H. & Germain, R. N. Nature 329, 254–256 (1987).
Glaichenhaus, N., Shastri, N., Littman, D. R. & Turner, J. M. Cell 64, 511–520 (1991).
Cammarota, G. et al. Nature 356, 799–801 (1992).
Lombardi, G. et al. J. Immun. 147, 2034–2040 (1991).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
König, R., Huang, LY. & Germain, R. MHC class II interaction with CD4 mediated by a region analogous to the MHC class I binding site for CD8. Nature 356, 796–798 (1992). https://doi.org/10.1038/356796a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/356796a0
This article is cited by
-
Genome-wide pharmacogenetics of anti-drug antibody response to bococizumab highlights key residues in HLA DRB1 and DQB1
Scientific Reports (2022)
-
Protective association of HLA-DPB1*04:01:01 with acute encephalopathy with biphasic seizures and late reduced diffusion identified by HLA imputation
Genes & Immunity (2022)
-
Haplotype structures and polymorphisms of dog leukocyte antigen (DLA) class I loci shaped by intralocus and interlocus recombination events
Immunogenetics (2022)
-
Revisiting the role of CD4+ T cells in cancer immunotherapy—new insights into old paradigms
Cancer Gene Therapy (2021)
-
Affinity-matured HLA class II dimers for robust staining of antigen-specific CD4+ T cells
Nature Biotechnology (2021)