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. 2016 Jan 5;6:1506. doi: 10.3389/fmicb.2015.01506

Table 2.

HLA-DR4 restricted cryptic epitopes identified within domain I with relative binding affinity.

LF peptide sequence Relative binding affinity of peptide to HLA-DR molecules
DR1 DR3 DR4 DR7 DR11 DR13 DR15
111 GGKIYIVDGDITKHISLEAL 130 122 >1000 61 15 75 21 6
161 VLVIQSSEDYVENTEKALNV 180 1702 82 29 66 168 >172 958
181 YYEIGKILSRDILSKINQPY 200 69 3 19 4 0.4 5 43
221 LLFTNQLKEHPTDFSVEFLE 240 909 >76 6 51 148 >172 193

The relative binding affinity of peptides to HLA-DR molecules were expressed as a relative activity (ratio of the IC50 of the peptide to the IC50 of a reference peptide which binds strongly to the individual HLA II molecule). Peptides with a high relative binding affinity of <10 are indicated in bold, while moderate binding is characterized by a range of relative affinity varying from 10 to 100. Means were calculated from at least three independent measurements.