Immunogenetics

, Volume 51, Issue 10, pp 765–770

What to do with HLA-DO?

  • Marieke van Ham
  • Marcel van Lith
  • Alexander Griekspoor
  • Jacques Neefjes
Review

DOI: 10.1007/s002510000208

Cite this article as:
van Ham, M., van Lith, M., Griekspoor, A. et al. Immunogenetics (2000) 51: 765. doi:10.1007/s002510000208

Abstract.

Antigenic peptide binding to MHC class II molecules in the endocytic pathway occurs via a multifactorial process that requires the support of a specialized lysosomal chaperone called HLA-DM. DM shows both in primary amino acid sequence and quaternary structure a high homology to both MHC class I and class II molecules. Like the peptide presenting class II molecules, DM is expressed in all professional antigen presenting cells. DM catalyzes the dissociation of peptides that do not bind stably to the class II peptide-binding groove, thereby leading to the preferential presentation of stably binding antigenic peptides. The recently discovered HLA-DO molecule is mainly expressed in B cells and associates with DM, thereby markedly affecting DM function. Like DM, the genes encoding the HLA-DO heterodimer lie within the MHC class II region and exhibit strong homology to classical class II molecules. This review evaluates the unique effects of DO on DM-mediated antigen presentation by MHC class II molecules and discusses the possible physiological relevance for the B cell-specific expression of DO and its function.

HLA-DM HLA-DO MHC class II antigen presentation B lymphocytes Autoimmunity 

Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Marieke van Ham
    • 1
  • Marcel van Lith
    • 1
  • Alexander Griekspoor
    • 1
  • Jacques Neefjes
    • 1
  1. 1.Division of Tumor Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands

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