Definition of peptide binding motifs amongst the HLA-A*30 allelic group

HLA class I molecules present endogenously processed peptide ligands for su rveillance by the T-cell, receptor. This potentially immunogenic surface of HLA and peptide is a consequence of the polymorphism found within the HLA molecule and its preference for ligand binding together with peptide confor mation within the binding groove. To investigate the relation between the p olymorphic differences between some closely related HLA alleles and their e ffect on peptide preference, transfectants were established, each containin g one of four allelic variants of HLA-A*30. Peptides from all four transfec tants were eluted, and both individual ligands and peptide pools were seque nced. The data shows two distinct peptide motifs which distinguish A*3001 f rom the other three known A*30 variants. Differences in preferences at mino r positions within the peptide sequence were noted between A*3002, A*3003 a nd A*3003, providing additional evidence of the implications of sequence po lymorphism to HLA function.