Prediction of major histocompatibility complex binding regions of protein antigens by sequence pattern analysis
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Prediction of major histocompatibility complex binding regions of protein antigens by sequence pattern analysis. / Sette, A; Buus, S; Appella, E; Smith, J A; Chesnut, R; Miles, C; Colon, S M; Grey, H M.
I: Proceedings of the National Academy of Science of the United States of America, Bind 86, Nr. 9, 1989, s. 3296-300.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Prediction of major histocompatibility complex binding regions of protein antigens by sequence pattern analysis
AU - Sette, A
AU - Buus, S
AU - Appella, E
AU - Smith, J A
AU - Chesnut, R
AU - Miles, C
AU - Colon, S M
AU - Grey, H M
N1 - Keywords: Amino Acid Sequence; Animals; Antigens; Binding Sites; Eukaryotic Cells; Haplotypes; Histocompatibility Antigens Class II; Mice; Molecular Sequence Data; Ovalbumin; Prokaryotic Cells; Proteins; Viral Proteins
PY - 1989
Y1 - 1989
N2 - We have previously experimentally analyzed the structural requirements for interaction between peptide antigens and mouse major histocompatibility complex (MHC) molecules of the d haplotype. We describe here two procedures devised to predict specifically the capacity of peptide molecules to interact with these MHC class II molecules (IAd and IEd). The accuracy of these procedures has been tested on a large panel of synthetic peptides of eukaryotic, prokaryotic, and viral origin, and also on a set of overlapping peptides encompassing the entire staphylococcal nuclease molecule. For both sets of peptides, IAd and IEd binding was successfully predicted in approximately 75% of the cases. This suggests that definition of such sequence "motifs" could be of general use in predicting potentially immunogenic peptide regions within proteins.
AB - We have previously experimentally analyzed the structural requirements for interaction between peptide antigens and mouse major histocompatibility complex (MHC) molecules of the d haplotype. We describe here two procedures devised to predict specifically the capacity of peptide molecules to interact with these MHC class II molecules (IAd and IEd). The accuracy of these procedures has been tested on a large panel of synthetic peptides of eukaryotic, prokaryotic, and viral origin, and also on a set of overlapping peptides encompassing the entire staphylococcal nuclease molecule. For both sets of peptides, IAd and IEd binding was successfully predicted in approximately 75% of the cases. This suggests that definition of such sequence "motifs" could be of general use in predicting potentially immunogenic peptide regions within proteins.
M3 - Journal article
C2 - 2717617
VL - 86
SP - 3296
EP - 3300
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 9
ER -
ID: 9947088