Heparan sulfate-glucosamine 3-O-sulfotransferase 3B1 (HS3ST3B1)

Heparan sulfate-glucosamine 3-O-sulfotransferase 3B1 (HS3ST3B1) is a type II integral membrane enzyme of the sulfotransferase family, responsible for the specific 3-O-sulfation of glucosamine residues in heparan sulfate during its biosynthesis[1][2][5]. This rare terminal sulfation modification controls the formation of unique heparan sulfate motifs that mediate a range of biological activities—including modulation of protein–ligand interactions, growth factor signaling (such as FGF, VEGF, and TGF-β), and immune cell trafficking[2][3][4]. HS3ST3B1’s enzymatic action creates specialized binding sites required for the entry of pathogens like Herpes simplex virus-1[5], but it also serves roles in normal development (notably in epithelial and glandular morphogenesis[3]), immune regulation, and potentially tissue regeneration. The gene is differentially expressed in immune cells and tissues such as liver and placenta, as well as in various cancers, where altered expression is linked to changes in invasiveness, angiogenesis, or EMT[4][5]. Mouse knockout studies indicate its involvement in organ development and function, particularly in secretory glands[3]. No approved drugs directly target HS3ST3B1, but its role as an entry factor for viruses and as a modifier of cancer cell behavior highlights its potential as a therapeutic target or biomarker in specific contexts.

Other names

Heparan sulfate glucosamine 3-O-sulfotransferase 3B1HS3ST3B13OST3B1HS3ST3B3-OST-3Bh3-OST-3B30ST3B1Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1heparan sulfate (glucosamine) 3-O-sulfotransferase 3B1

Not applicable for classic drugs; enzyme’s activity generates 3-O-sulfated heparan sulfate motifs, acting as binding or entry receptors (e.g., for Herpes simplex virus-1)[5]. Modulation of extracellular protein binding (e.g., VEGF, TGF-β) via heparan sulfate structure alteration[4]. Regulation of epithelial–mesenchymal transition through changes in glycosaminoglycan fine structure[4][5].