TY - JOUR

T1 - Structural analysis of peptides capable of binding to more than one Ia antigen

AU - Sette, A

AU - Buus, S

AU - Colon, S

AU - Miles, C

AU - Grey, H M

N1 - Keywords: Amino Acid Sequence; Animals; Antigen-Antibody Reactions; Binding Sites, Antibody; DNA Restriction Enzymes; Hemagglutinins, Viral; Histocompatibility Antigens Class II; Mice; Mice, Inbred AKR; Molecular Sequence Data; Myoglobin; Ovalbumin; Peptides; Repressor Proteins; Structure-Activity Relationship

PY - 1989

Y1 - 1989

N2 - The Ia binding regions were analyzed for three unrelated peptide Ag (sperm whale myoglobin 106-118, influenza hemagglutinin 130-142, and lambda repressor protein 12-26) for which binding to more than one Ia molecule has previously been demonstrated. By determining the binding profile of three separate series of truncated synthetic peptides, it was found that in all three cases the different Ia reactivities mapped to largely overlapping regions of the peptides; although, for two of the peptides, the regions involved in binding the different Ia specificities were distinct. Moreover, subtle differences were found to dramatically influence some, but not other, Ia reactivities. Using a large panel of synthetic peptides it was found that a significant correlation exists between the capacity of peptides to interact with different alleles of the same molecule (i.e., IAd and IAk), but no correlation was found with the capacity of peptides to interact with different isotypes within the same haplotype (i.e., IAd and IEd). These data suggest that different alleles of the same MHC molecule may actually recognize closely related structures, whereas different isotypes may recognize unrelated, albeit non-mutually exclusive, structures on an Ag molecule.

AB - The Ia binding regions were analyzed for three unrelated peptide Ag (sperm whale myoglobin 106-118, influenza hemagglutinin 130-142, and lambda repressor protein 12-26) for which binding to more than one Ia molecule has previously been demonstrated. By determining the binding profile of three separate series of truncated synthetic peptides, it was found that in all three cases the different Ia reactivities mapped to largely overlapping regions of the peptides; although, for two of the peptides, the regions involved in binding the different Ia specificities were distinct. Moreover, subtle differences were found to dramatically influence some, but not other, Ia reactivities. Using a large panel of synthetic peptides it was found that a significant correlation exists between the capacity of peptides to interact with different alleles of the same molecule (i.e., IAd and IAk), but no correlation was found with the capacity of peptides to interact with different isotypes within the same haplotype (i.e., IAd and IEd). These data suggest that different alleles of the same MHC molecule may actually recognize closely related structures, whereas different isotypes may recognize unrelated, albeit non-mutually exclusive, structures on an Ag molecule.

M3 - Journal article

C2 - 2535860

VL - 142

SP - 35

EP - 40

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 1

ER -