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. Author manuscript; available in PMC: 2022 Apr 21.
Published in final edited form as: J Immunol. 2020 Mar 30;204(9):2349–2359. doi: 10.4049/jimmunol.1901079

Table II.

Relative binding affinity of the proinsulin peptides to HLA-DR and DQ molecules.

Peptide DR3 DR4 DRB4 DQ2 DQ8
B8-22 >1 250 >3 333 >1 000 >50 1
B11-25 1 250 333 >1 000 15 1
B14-28 1 000 2 667 >1 000 >50 61
B17-C1 >1 250 >3 333 >1 000 >50 >143
B20-C4 6 >3 333 >1 000 >50 >143
C10-24 >1 250 >3 333 >1 000 >50 >143
C13-27 >1 250 >3 333 >1 000 >50 >143
C16-30 >1 250 >3 333 >1 000 >50 >143
C19-33 >1 250 1 764 141 15 49
C22-A1 48 3 >1 000 >50 >143
C25-A4 >1 250 153 >1 000 >50 >143
A1-15 106 >3 333 >1 000 5 9

Results are expressed as a relative binding ratio obtained by dividing the IC50 of the peptides by that of a reference peptide that binds strongly to the HLA molecule. Lower numbers correspond to a higher binding affinity. Bold: binding ratio below 100 (moderate binding) or below 10 (high binding). Each peptide-HLA combination was evaluated in two independent experiments. Peptides were tested at 10 different concentrations up to a maximal concentration of 100 000 nM. This maximal concentration was used to define the maximal relative binding ratio for each HLA molecule tested. The sequences and mean IC50 values of the reference peptides used were: MT2-16 (AKTIAYDEEARRGLE) for DRB1*03:01 (75 nM), HA306-318 (PKYVKQNTLKLAT) for DRB1*04:01 (30 nM), E2/E7 (AGDLLAIETDKATI) for DRB4*01:01 (63 nM), HCI46-63 (EPRAPWIEQEQGPEYWDQE) for DQ2 (DQA1*05:01/DQB1*02:01; 1400 nM) and DQB45-57 (ADVEVYRAVTPLGPPD) for DQ8 (DQA1*03:01/DQB1*03:02; 730 nM). DR3=DRB1*03:01, DR4=DRB1*04:01, DRB4=DRB4*01:01.