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.
Chen
B P
BP
Department of Cell Biology, Stanford University, California 94305.
Rothbard
J
J
Parham
P
P
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