The epitope recognized by pan-HLA class I-reactive monoclonal antibody W6/32 and its relationship to unusual stability of the HLA-B27/beta2-microglobulin complex

Immunogenetics. 2001 Aug;53(6):440-6. doi: 10.1007/s002510100353.

Abstract

A broadly used pan-HLA class I-reactive monoclonal antibody W6/32 is believed to recognize a conformational epitope dependent on association between heavy chains and beta2-microglobulin (beta2m). However, in the present study we report that W6/32 does recognize at least some free HLA class I heavy chains under the partially denaturating conditions of nonreducing Western blotting, namely nearly all HLA-B allelic products. Furthermore, we confirm and largely extend our previous observation that complexes of beta2m with heavy chains of a few HLA class I allelic forms (most notably HLA-B27) exhibit unusual resistance to dissociation by SDS, which is reminiscent of MHC class II molecules. In addition, our data indicate the existence of covalent (disulfide-linked) heterodimers of certain HLA class I heavy chains (namely Cw1 and Cw4) and beta2m.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology*
  • Cell Line
  • Cells, Cultured
  • Epitopes / immunology*
  • HLA-B Antigens / immunology
  • HLA-B27 Antigen / immunology
  • HLA-B27 Antigen / metabolism*
  • Histocompatibility Antigens Class I / immunology*
  • Humans
  • Macromolecular Substances
  • Mice
  • Protein Denaturation
  • Sodium Dodecyl Sulfate / chemistry
  • beta 2-Microglobulin / metabolism*

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • HLA-B Antigens
  • HLA-B27 Antigen
  • Histocompatibility Antigens Class I
  • Macromolecular Substances
  • beta 2-Microglobulin
  • Sodium Dodecyl Sulfate