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Sodium Dodecyl Sulfate-Resistant HLA-DR "Superdimer" Bands Are in Some Cases Class II Heterodimers Bound to Antibody¹

Christoph Hitzel^*, Ulrike Grüneberg^2,, Marieke van Ham^,, John Trowsdale^2, and Norbert Koch^3,*,

^* Division of Immunobiology, University of Bonn, Bonn, Germany; Human Immunogenetics Laboratory, Imperial Cancer Research Fund, London, United Kingdom; and Department of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam, The Netherlands

The detection of dimers of dimers in MHC class II crystals has excited speculation about their possible functions in T cell Ag recognition. Biochemical evidence for the existence of DR superdimers falls short of proof and is controversial. To monitor B lymphoma cells for high m.w. complexes of HLA-DR molecules, membrane preparations and cell lysates were screened by one- and two-dimensional Western blotting. Under these conditions, in which DRß heterodimers were readily detected, no DR complexes with an (ß)₂-chain composition could be identified. Two mAbs (L243 and D1-12) immunoprecipitated high m.w. DR complexes suspected to be superdimers. However, biochemical analysis revealed that, rather than superdimers, these were SDS-stable complexes of DR in combination with the Abs. Thus, previous observations of HLA-DR superdimer bands may also reflect complexes of DR molecules with bound Ab.

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