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
SN - 0022-1767
VL - 142
SP - 35
EP - 40
JO - Journal of Immunology
JF - Journal of Immunology
IS - 1
ER -