Sialyl-Lewis X (sLeX), a sialylated fucosylated tetrasaccharide and endogenous antigen, serves as a high-affinity ligand for selectins (E-, P-, and L-selectin)[1]. It interacts with ELAM-1 and CD62, consequently inhibiting CD62-mediated neutrophil recruitment to inflammation sites[2].

Sialyl-Lewis X is a high-affinity ligand of CD62, Antibodies [mAb CSLEX (IgM; anti-sLeX)] to sLeX inhibit CD62-mediated binding of HL-60 cells to activated platelets[1].Liposomes containing glycolipids with the sLeX structure prevents adhesion of HL-60 cells and human neutrophils. HL-60 cell adhesion is partially inhibited (50%) by liposomes containing Lex at 5 μg/ml. However, sLeX liposomes give maximal inhibition at only 1 ug/ml. sLeX liposomes inhibits adhesion with a 10-fold higher affinity than Lex liposomes[1].CD62 binding of neutrophils to activated platelets is inhibited a soluble human milk oligosaccharide that contains the LeX structure. the sLeX sugar is a 30-fold more potent inhibitor than the nonsialylated Lex sugar, which requires 2 μg/ml and 54 μg/ml to achieve 50% inhibition of neutrophil adhesion, respectively[1].