This enzyme sulfates the residues marked with an asterisk in sequences containing at least IdoA2S-GlcN*- or ?GlcA2S.GlcN*-. Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other, [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamines residues preceded by GlcA2S. EC 2.8.2.23, [heparan sulfate]-glucosamine 3-sulfotransferase 1, prefers GlcA or IdoA, whereas EC 2.8.2.30, [heparan sulfate]-glucosamine 3-sulfotransferase 3, prefers IdoAS
This enzyme sulfates the residues marked with an asterisk in sequences containing at least -> IdoA2S-> GlcN*-> or -> GlcA2S-> GlcN*-> (symbols as in {iupac/2carb/38::2-Carb-38}). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
3-O-sulfotransferase-2-generated heparan sulfate serves as a receptor during herpes simplex virus type-1 entry and spread. The enzyme plays a role in HSV-1 pathogenesis
i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1 mediating the viral cellular entry, overview, i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1
heparan sulfate chains contain sulfated domains termed the HS fine structure, which gives HS specific binding affinities for extracellular ligands, heparan sulfate 3-O-sulfotransferases catalyze the transfer of sulfate groups to the 3-O position of glucosamine residues of heparan sulfate, a rare, but essential heparan sulfate chain modification required for HS fine structure
modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
HSV-1 glycoprotein gD, both the wild-type and the mutant Rid1 form, can interact with [heparan sulfate]-glucosamine 3-sulfate generated by HS 3-OST-2, overview
heparan sulfate chains contain sulfated domains termed the HS fine structure, which gives HS specific binding affinities for extracellular ligands, heparan sulfate 3-O-sulfotransferases catalyze the transfer of sulfate groups to the 3-O position of glucosamine residues of heparan sulfate, a rare, but essential heparan sulfate chain modification required for HS fine structure
modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
developmental expression analysis of the 3-OST gene family, mRNA expression patterns in several tissues/organs throughout early zebrafish development, including early cleavage stages, somites, brain, internal body organ primordial, and pectoral fin development, overview
DNA and amino acid sequence determination and analysis and developmental expression analysis of the 3-OST gene family, sequence comparisons, phylogentic analysis, overview
expression of 3-OST-2 renders CHO-K1 cell, which are normally resistant, susceptible to viral entry of wild-type and a Q27P mutant, Rid1, forms of HSV-1, requiring the gD receptors, Rid1 mutation at gD prevents its entry via some receptors including HVEM and 3-OS HS generated by 3-OST-3, overview
the results provide evidence for specific epigenetic regulation of 3-OST genes resulting in altered heparan sulfate proteoglycans and point to a defect of heparan sulfate-3-O-sulfation as a factor in cancer progression
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells.
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Promoter hypermethylation of HS3ST2, SEPTIN9 and SLIT2 combined with FGFR3 mutations as a sensitive/specific urinary assay for diagnosis and surveillance in patients with low or high-risk non-muscle-invasive bladder cancer.
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers
Bui, C.; Ouzzine, M.; Talhaoui, I.; Sharp, S.; Prydz, K.; Coughtrie, M.W.; Fournel-Gigleux, S.
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells
Comprehensive analysis of herpes simplex virus 1 (HSV-1) entry mediated by zebrafish 3-O-sulfotransferase isoforms: implications for the development of a zebrafish model of HSV-1 infection