Naturally processed HLA class I bound peptides from c-myc-transfected cells reveal allele-specific motifs.
Naturally processed peptides, bound to HLA-A2, A68, B40 molecules, were isolated from a c-myc transfected lymphoblastoid B cell lines for sequence analysis. Forty-three sequences of bound peptides could be grouped into three structural motifs. One of the peptide sequences obtained, SLLPAIVEL, was identical to a previously reported peptide bound to HLA-A2.1 and was used for grouping HLA-A2-bound peptides. A second motif, identical to that previously reported for HLA-A68-bound peptides, was also observed. A distinct third motif, consistent with the structure of the HLA-B40 "45 pocket," was observed. The peptides within this group contained glutamate in position 2, usually followed by a hydrophobic residue in positions 3 and 9. Within this motif group of peptides bound to MHC class I molecules, one peptide, HEETPPTTS, was 100% homologous to residues 243-251 of the c-myc protein.
Harris
P E
PE
Division of Immunogenetics, College of Physicians and Surgeons of Columbia University, New York, NY 10032.
Colovai
A
A
Liu
Z
Z
Dalla Favera
R
R
Suciu-Foca
N
N
D000199:Actins / Q000235:genetics; D000483:Alleles; D000595:Amino Acid Sequence; D017951:Antigen Presentation; D001483:Base Sequence; D002461:Cell Line, Transformed; D016213:Cyclins / Q000235:genetics; D016259:Genes, myc; D015395:Histocompatibility Antigens Class I / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D011498:Protein Precursors / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014162:Transfection
D000199:Actins; D016213:Cyclins; D015395:Histocompatibility Antigens Class I; D010455:Peptides; D011498:Protein Precursors