Identification of the Naturally Processed Form of Hen Egg White Lysozyme Bound to the Murine Major Histocompatibility Complex Class II Molecule I-A^k
Abstract
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.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- August 1992
- DOI:
- 10.1073/pnas.89.16.7380
- Bibcode:
- 1992PNAS...89.7380N