Apparent lack of MHC restriction in binding of class I HLA molecules to solid-phase peptides.
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.
Department of Cell Biology, Stanford University, California 94305.
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Chen
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Rothbard
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Parham
D000595:Amino Acid Sequence; D002460:Cell Line; D000939:Epitopes / Q000032:analysis; D015234:HLA-A Antigens / Q000302:isolation & purification; D015235:HLA-B Antigens / Q000302:isolation & purification; D015236:HLA-C Antigens / Q000302:isolation & purification; D006801:Humans; D008285:Major Histocompatibility Complex; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000939:Epitopes; D015234:HLA-A Antigens; D015235:HLA-B Antigens; D015236:HLA-C Antigens; D010455:Peptides