Structurally diverse forms of HLA-B27 molecules are displayed in vivo in a cell type-dependent manner

Hum Immunol. 2000 Apr;61(4):408-18. doi: 10.1016/s0198-8859(99)00176-7.


The formation of a trimeric complex, composed of heavy chain (HC), beta(2)-microglobulin (beta(2)m) and antigenic peptide, is generally believed to be a prerequisite for the expression of HLA class I molecules at the cell surface in vivo. Therefore, a possible role in immunological processes for HC/beta(2)m complexes devoid of peptide has not been seriously considered. Using a novel HLA-B*2705-transgenic rat model and monoclonal antibodies that distinguish between structurally different forms of HLA-B27 molecules, we demonstrate here that class I molecules which appear to lack antigenic peptides are expressed in abundance on a variety of cell types in lymphoid organs. These results imply a role for structurally diverse, possibly empty, MHC molecules in physiological T cell selection which has so far not been sufficiently appreciated.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified
  • Antibodies, Monoclonal / metabolism
  • B-Lymphocytes / immunology
  • B-Lymphocytes / metabolism
  • Cell Line
  • Cytokines / pharmacology
  • HLA-B27 Antigen / chemistry*
  • HLA-B27 Antigen / genetics
  • HLA-B27 Antigen / immunology*
  • Humans
  • Lymphocyte Activation / immunology
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / genetics
  • Peptides / immunology
  • Rats
  • Rats, Inbred WKY
  • Rats, Sprague-Dawley
  • T-Lymphocytes / immunology
  • T-Lymphocytes / metabolism
  • Tumor Cells, Cultured


  • Antibodies, Monoclonal
  • Cytokines
  • HLA-B27 Antigen
  • Peptides