Structural requirements for the interaction between peptide antigens and I-Ed molecules
Research output: Contribution to journal › Journal article › Research › peer-review
We have analyzed the structural characteristics of the interaction between I-Ed molecules and their peptide ligands. It was found that unrelated good I-Ed binders share structurally similar "core" regions that were experimentally demonstrated to be crucial for binding to I-Ed molecules. Single amino acid substitution analogues of one good I-Ed binder, hen egg lysozyme 107-116, were analyzed for their capacity to bind to I-Ed molecules and to activate two different I-Ed-restricted T cell hybridomas. The results illustrate the great permissiveness of I-Ed-peptide interaction and the great specificity of T cell recognition. It was concluded from these analyses that basic residues on the peptide molecule play a crucial role in binding to I-Ed. This contrasts with the structural requirements for binding to the other Iad isotype, I-Ad, the crucial hydrophobic residues. Thus, different class II molecules of the same MHC haplotype may have rather distinct peptide binding specificities, thereby expanding the repertoire of possible immunogenic peptides presented for T cell recognition.
Original language | English |
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Journal | Journal of Immunology |
Volume | 143 |
Issue number | 10 |
Pages (from-to) | 3289-94 |
Number of pages | 5 |
ISSN | 0022-1767 |
Publication status | Published - 1989 |
Bibliographical note
Keywords: Amino Acid Sequence; Amino Acids; Animals; Chickens; Egg Proteins; Histocompatibility Antigens Class II; Mice; Molecular Sequence Data; Muramidase; Peptides; Receptors, Antigen; Structure-Activity Relationship; T-Lymphocytes
ID: 9946668