Identification of the naturally processed form of hen egg white lysozyme bound to the murine major histocompatibility complex class II molecule I-Ak.
CA Nelson, RW Roof, DW McCourt… - Proceedings of the …, 1992 - National Acad Sciences
CA Nelson, RW Roof, DW McCourt, ER Unanue
Proceedings of the National Academy of Sciences, 1992•National Acad SciencesA 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 …
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 …
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.
National Acad Sciences