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2-Microglobulin- Free Heavy Chains of HLA-B2705 on the Cell Surface1
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138
The human class I MHC molecules are known to generally exist on the
cell surface either as peptide-containing complexes of H chain
(
-chain) and 
2-microglobulin (2m) or
as 2m-free H chains incapable of binding peptides. In
this study, a uniquely conformed peptide-containing
2m-free HLA-B2705 H chain has been isolated using the
recently described highly efficient perfusion-affinity chromatography
system for purification of class I MHC protein molecules. This form
recognized by the mAb MARB4 is very closely associated with the
remainder of the peptide containing HLA-B2705/2m complex
reactive with mAb ME1 and is present to 
1–10% of mAb ME1 reactive
forms on the cell surface. Also, HLA-B2705 purified using the mAb ME1
affinity column includes this unique mAb MARB4-reactive, unusually
stable peptide-containing 2m-free form. A peptide
nonamer GRWRGWYTY was isolated and identified from this
2m-free HLA-B2705 H chain and was used to assemble the
mAb MARB4 reactive form efficiently on the surface of cells expressing
HLA-B2705. The discovery of this form opens new avenues for further
investigation of the role of HLA-B27 in
spondyloarthropathies.
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