Abstract
ST6Gal1 is a critical sialyltransferase enzyme that controls the addition of α2,6-linked sialic acids to the termini of glycans. Attachment of sialic acids to glycoproteins as a posttranslational modification influences cellular responses, and is a well-known modifier of immune cell behavior. ST6Gal1 activity impacts processes such as: effector functions of immunoglobulin G via Fc sialylation, hematopoietic capacity by hematopoietic stem and progenitor cell surface sialylation, and lymphocyte activation thresholds though CD22 engagement and inhibition of galectins. This review summarizes recent studies that suggest α2,6 sialylation by ST6Gal1 has an immunoregulatory effect on immune reactions.