Journal of Experimental Medicine, Vol 172, 931-936, Copyright © 1990 by Rockefeller University Press
Apparent lack of MHC restriction in binding of class I HLA molecules to solid-phase peptides
BP Chen, J Rothbard and P Parham
Department of Cell Biology, Stanford University, California 94305.
The specificity of binding of solubilized, purified HLA-A,B molecules to
solid-phase peptides has been examined using the assay described by
Bouillet et al. [1989. Nature (Lond.). 339:473.] 64 peptides derived from
the sequences of viral antigens, HLA-A,B,C heavy chains, and clathrin light
chains were tested for binding to HLA-A2.1, Aw68.1, Aw69, B44, and B5,
molecules that differ by 5-17 residues of the peptide binding groove. 15 of
the peptides, including those known to be T cell epitopes, gave significant
binding. The pattern of peptide binding for each of the five HLA-A,B
molecules was not significantly different. Binding was demonstrated to be a
property of native beta 2m- associated HLA-A,B molecules that preserved
conformational antigenic determinants after binding to peptide. In
comparison to our previous results from solution-based assays the
proportion of HLA-A,B molecules that can bind solid-phase peptides is very
high. This accessibility of solid-phase peptides to the binding site of MHC
molecules may be directly related to the observed absence of MHC
specificity in the binding.
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