I-Ad-binding peptides derived from unrelated protein antigens share a common structural motif
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I-Ad-binding peptides derived from unrelated protein antigens share a common structural motif. / Sette, A; Buus, S; Colon, S; Miles, C; Grey, H M.
In: Journal of Immunology, Vol. 141, No. 1, 1988, p. 45-8.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - I-Ad-binding peptides derived from unrelated protein antigens share a common structural motif
AU - Sette, A
AU - Buus, S
AU - Colon, S
AU - Miles, C
AU - Grey, H M
N1 - Keywords: Amino Acid Sequence; Amino Acids; Animals; Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinins, Viral; Histocompatibility Antigens Class II; Mice; Molecular Sequence Data; Myoglobin; Ovalbumin; Peptides; Protein Binding; Receptors, Amino Acid; Receptors, Cell Surface; Structure-Activity Relationship
PY - 1988
Y1 - 1988
N2 - Purified Ia molecules can specifically bind many unrelated peptide Ag, and such binding appears to be a necessary, albeit not sufficient, prerequisite for the immunogenicity of the proteins from which such peptides are derived. We have recently analyzed the affect of single amino acid substitutions on the I-Ad binding of the immunogenic peptide OVA 323-339. The results obtained demonstrated the very permissive nature of Ag-Ia interaction. We also showed that unrelated peptides that are good I-Ad binders share a common structural motif and speculated that recognition of such motifs could represent a mechanism to achieve a very permissive type of interaction that yet retained some degree of specificity. In the present set of experiments we analyzed the I-Ad binding pattern of a series of overlapping peptides derived from sperm whale myoglobin (residues 102-125) and influenza hemagglutinin (residues 121-146) to determine whether the peptide regions predicted on the basis of structural similarity to be involved in I-Ad binding were in fact involved. In both cases, the I-Ad-interacting determinants were found to contain the sequence motif postulated to be important for I-Ad binding. These data support the hypothesis that I-Ad molecules recognize a large library of Ag by virtue of common structural motifs present in peptides derived from phylogenetically unrelated proteins.
AB - Purified Ia molecules can specifically bind many unrelated peptide Ag, and such binding appears to be a necessary, albeit not sufficient, prerequisite for the immunogenicity of the proteins from which such peptides are derived. We have recently analyzed the affect of single amino acid substitutions on the I-Ad binding of the immunogenic peptide OVA 323-339. The results obtained demonstrated the very permissive nature of Ag-Ia interaction. We also showed that unrelated peptides that are good I-Ad binders share a common structural motif and speculated that recognition of such motifs could represent a mechanism to achieve a very permissive type of interaction that yet retained some degree of specificity. In the present set of experiments we analyzed the I-Ad binding pattern of a series of overlapping peptides derived from sperm whale myoglobin (residues 102-125) and influenza hemagglutinin (residues 121-146) to determine whether the peptide regions predicted on the basis of structural similarity to be involved in I-Ad binding were in fact involved. In both cases, the I-Ad-interacting determinants were found to contain the sequence motif postulated to be important for I-Ad binding. These data support the hypothesis that I-Ad molecules recognize a large library of Ag by virtue of common structural motifs present in peptides derived from phylogenetically unrelated proteins.
M3 - Journal article
C2 - 2837512
VL - 141
SP - 45
EP - 48
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 1
ER -
ID: 9947503