TY - JOUR

T1 - Structural requirements for the interaction between peptide antigens and I-Ed molecules

AU - Sette, A

AU - Adorini, L

AU - Appella, E

AU - Colón, S M

AU - Miles, C

AU - Tanaka, S

AU - Ehrhardt, C

AU - Doria, G

AU - Nagy, Z A

AU - Buus, S

N1 - 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

PY - 1989

Y1 - 1989

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 2809202

VL - 143

SP - 3289

EP - 3294

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 10

ER -