Table 1.
Comparison of the peptide sequence around the O-glycosylated Thr+1 of PILRα ligands
Amino acid position |
||||||||||
Ligand | −3 | −2 | −1 | +1 | +2 | +3 | +4 | +5 | +6 | Kd, μM |
HSV-1 gB (53-61) | G | P | A | T | P | A | P | P | A | 2.3* |
mCD99 Thr45 (42-50) | M | K | P | T | P | K | A | P | T | 2.8† |
mCD99 Thr50 (47-55) | K | A | P | T | P | K | K | P | S | 3.3† |
PAMP§ | G | L | A | T | P | H | P | N | S | Not measured |
NPDC1§ | L | P | S | T | P | G | T | P | T | 0.049‡ |
COLEC12§ | N | E | P | T | P | A | P | E | D | 1.1‡ |
The N-terminal region (30–108) of gB was used for the binding study.
The single Ala mutation (T45 or T50) did not cause any reduction of PILRα binding compared with mCD99 wild type (Kd = 2.2 μM) (11).
These affinity contained the avidity effect of Fc-fused dimerization (8).
These are the predicted O-glycosylation sites of each PILRα ligand.