The epitope recognized by pan-HLA class I-reactive monoclonal antibody W6/32 and its relationship to unusual stability of the HLA-B27/β2-microglobulin complex

Denise G. Wiesch, Deborah A. Meyers

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

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 β2-microglobulin (β2m). 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 β2m 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 β2m.

Original languageEnglish (US)
Pages (from-to)440-446
Number of pages7
JournalImmunogenetics
Volume53
Issue number6
DOIs
StatePublished - 2001
Externally publishedYes

Keywords

  • Epitope
  • HLA class I
  • HLA-B27
  • W6/32
  • β-microglobulin

ASJC Scopus subject areas

  • Immunology
  • Genetics

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