Identification of the naturally processed form of hen egg white lysozyme bound to the murine major histocompatibility complex class II molecule I-Ak.
A murine B-cell lymphoma bearing the class II major histocompatibility complex molecule I-Ak was cultured with the protein antigen hen egg white lysozyme (HEL). The I-Ak molecules were purified, and their associated peptides were extracted for characterization. Five HEL peptides were identified. Four contained the 10 amino acid residues HEL 52-61 (DYGILQINSR) but were heterogeneous in length and flanking residues. This core sequence is known to confer a high binding affinity for I-Ak. One additional peptide contained the amino acid residues HEL 48-60. These data demonstrate that the HEL epitope containing residues 52-61 is the most abundant HEL epitope presented on the major histocompatibility complex of the antigen-presenting cells and consequently explains its immunodominance.
Nelson
C A
CA
Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.
Roof
R W
RW
McCourt
D W
DW
Unanue
E R
ER
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D005260:Female; D000949:Histocompatibility Antigens Class II / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification; D011485:Protein Binding
D000949:Histocompatibility Antigens Class II; D010446:Peptide Fragments; D009113:Muramidase