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 (sLeX) serves as a high-affinity ligand for CD62. The use of antibodies, specifically mAb CSLEX (IgM; anti-sLeX), obstructs the CD62-mediated attachment of HL-60 cells to activated platelets. Moreover, liposomes integrated with glycolipids mimicking the sLeX configuration are effective in preventing the adhesion of HL-60 cells and human neutrophils. Notably, sLeX liposomes demonstrate a superior inhibitory capability on cell adhesion, exhibiting a tenfold greater affinity compared to Lex liposomes, achieving maximum inhibition at a lower concentration (1 µg/ml) compared to a partial (50%) inhibition achieved by Lex liposomes at a higher concentration (5 µg/ml). Additionally, a soluble human milk oligosaccharide containing the LeX structure also impedes the binding of neutrophils to activated platelets, wherein sLeX is identified as a substantially more effective inhibitor (30-fold) than its nonsialylated counterpart, Lex. Specifically, to attain a 50% reduction in neutrophil adhesion, sLeX requires only 2 µg/ml, in contrast to Lex, which necessitates 54 µg/ml.