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Artykuły w czasopismach na temat „Sialyltransferases”

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Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 20 lutego 2023

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1

Rosenstock, Philip, Kaya Bork, Chiara Massa, Philipp Selke, Barbara Seliger i Rüdiger Horstkorte. "Sialylation of Human Natural Killer (NK) Cells Is Regulated by IL-2". Journal of Clinical Medicine 9, nr 6 (11.06.2020): 1816. http://dx.doi.org/10.3390/jcm9061816.

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Sialic acids are terminal sugars on the cell surface that are found on all cell types including immune cells like natural killer (NK) cells. The attachment of sialic acids to different glycan structures is catalyzed by sialyltransferases in the Golgi. However, the expression pattern of sialyltransferases in NK cells and their expression after activation has not yet been analyzed. Therefore, the present study determines which sialyltransferases are expressed in human NK cells and if activation with IL-2 changes the sialylation of NK cells. The expression of sialyltransferases was analyzed in the three human NK cell lines NK-92, NKL, KHYG-1 and primary NK cells. NK-92 cells were cultured in the absence or presence of IL-2, and changes in the sialyltransferase expression were measured by qPCR. Furthermore, specific sialylation was investigated by flow cytometry. In addition, polySia and NCAM were measured by Western blot analyses. IL-2 leads to a reduced expression of ST8SIA1, ST6GAL1 and ST3GAL1. α-2,3-Sialylation remained unchanged, while α-2,6-sialylation was increased after IL-2 stimulation. Moreover, an increase in the amount of NCAM and polySia was observed in IL-2-activated NK cells, whereas GD3 ganglioside was decreased. In this study, all sialyltransferases that were expressed in NK cells could be identified. IL-2 regulates the expression of some sialyltransferases and leads to changes in the sialylation of NK cells.

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2

Janesch, Bettina, Hirak Saxena, Lyann Sim i Warren W. Wakarchuk. "Comparison of α2,6-sialyltransferases for sialylation of therapeutic proteins". Glycobiology 29, nr 10 (8.07.2019): 735–47. http://dx.doi.org/10.1093/glycob/cwz050.

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AbstractThe development of therapeutic proteins for the treatment of numerous diseases is one of the fastest growing areas of biotechnology. Therapeutic efficacy and serum half-life are particularly important, and these properties rely heavily on the glycosylation state of the protein. Expression systems to produce authentically fully glycosylated therapeutic proteins with appropriate terminal sialic acids are not yet perfected. The in vitro modification of therapeutic proteins by recombinant sialyltransferases offers a promising and elegant strategy to overcome this problem. Thus, the detailed expression and characterization of sialyltransferases for completion of the glycan chains is of great interest to the community. We identified a novel α2,6-sialyltransferase from Helicobacter cetorum and compared it to the human ST6Gal1 and a Photobacterium sp. sialyltransferase using glycoprotein substrates in a 96-well microtiter-plate-based assay. We demonstrated that the recombinant α2,6-sialyltransferase from H. cetorum is an excellent catalyst for modification of N-linked glycans of different therapeutic proteins.

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3

Czuchry, Diana, Paul Desormeaux, Melissa Stuart, Donald L. Jarvis, Khushi L. Matta, Walter A. Szarek i Inka Brockhausen. "Identification and Biochemical Characterization of the Novel α2,3-Sialyltransferase WbwA from Pathogenic Escherichia coli Serotype O104". Journal of Bacteriology 197, nr 24 (21.09.2015): 3760–68. http://dx.doi.org/10.1128/jb.00521-15.

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ABSTRACTThe sialyl-T antigen sialylα2-3Galβ1-3GalNAc is a common O-glycan structure in human glycoproteins and is synthesized by sialyltransferase ST3Gal1. The enterohemorrhagicEscherichia coliserotype O104 has the rare ability to synthesize a sialyl-T antigen mimic. We showed here that thewbwAgene of theE. coliO104 antigen synthesis gene cluster encodes an α2,3-sialyltransferase WbwA that transfers sialic acid from CMP-sialic acid to Galβ1-3GalNAcα-diphosphate-lipid acceptor. Nuclear magnetic resonance (NMR) analysis of purified WbwA enzyme reaction product indicated that the sialyl-T antigen sialylα2-3Galβ1-3GalNAcα-diphosphate-lipid was synthesized. We showed that the conserved His-Pro (HP) motif and Glu/Asp residues of two EDG motifs in WbwA are important for the activity. The characterization studies showed that WbwA fromE. coliO104 is a monofunctional α2,3-sialyltransferase and is distinct from human ST3Gal1 as well as all other known sialyltransferases due to its unique acceptor specificity. This work contributes to knowledge of the biosynthesis of bacterial virulence factors.IMPORTANCEThis is the first characterization of a sialyltransferase involved in the synthesis of an O antigen inE. coli. The enzyme contributes to the mimicry of human sialyl-T antigen and has unique substrate specificity but very little sequence identity to other sialyltransferases. Thus, the bacterial sialyltransferase is related to the human counterpart only by the similarity of biochemical activity.

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4

Yang, Rui, Mengge Gong, Siming Jiao, Juntian Han, Cui Feng, Meishan Pei, Zhongkai Zhou, Yuguang Du i Jianjun Li. "Protein Engineering of Pasteurella multocida α2,3-Sialyltransferase with Reduced α2,3-Sialidase Activity and Application in Synthesis of 3′-Sialyllactose". Catalysts 12, nr 6 (25.05.2022): 579. http://dx.doi.org/10.3390/catal12060579.

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Sialyltransferases are key enzymes for the production of sialosides. The versatility of Pasteurella multocida α2,3-sialyltransferase 1 (PmST1) causes difficulties in the efficient synthesis of α2,3-linked sialylatetd compounds, especial its α2,3-sialidase activity. In the current study, the α2,3-sialidase activity of PmST1 was further reduced by rational design-based protein engineering. Three double mutants PMG1 (M144D/R313Y), PMG2 (M144D/R313H) and PMG3 (M144D/R313N) were designed and constructed using M144D as the template and kinetically investigated. In comparison with M144D, the α2,3-sialyltransferase activity of PMG2 was enhanced by 1.4-fold, while its α2,3-sialidase activity was reduced by 4-fold. Two PMG2-based triple mutants PMG2-1 (M144D/R313H/T265S) and PMG2-2 (M144D/R313H/E271F) were then designed, generated and characterized. Compared with PMG2, triple mutants showed slightly improved α2,3-sialyltransferase activity, but their α2,3-sialidase activities were increased by 2.1–2.9 fold. In summary, PMG2 was used for preparative-scale production of 3′-SL (3′-sialyllactose) with a yield of >95%. These new PmST1 mutants could be potentially utilized for efficient synthesis of α2,3-linked sialosides. This work provides a guide to designing and constructing efficient sialyltransferases.

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5

Sticher, U., H. J. Gross i R. Brossmer. "Purification of α 2,6-sialyltransferase from rat liver by dye chromatography". Biochemical Journal 253, nr 2 (15.07.1988): 577–80. http://dx.doi.org/10.1042/bj2530577.

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We describe a simple three-step purification for Gal-beta 1,4-GlcNAc-alpha 2,6-sialyltransferase (EC 2.4.99.1) from rat liver which uses chromatography on Cibacron Blue F3GA and f.p.l.c. It gives a highly purified (11,000-fold) enzyme in 19% yield, which is free of other sialyltransferases, CMP-NeuAc hydrolase, sialidases and proteinases.

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6

Lee, Ki-Young, Hyung Gu Kim, Mi Ran Hwang, Jung Il Chae, Jai Myung Yang, Young Choon Lee, Young Kug Choo, Young Ik Lee, Sang-Soo Lee i Su-Il Do. "The Hexapeptide Inhibitor of Galβ1,3GalNAc-specific α2,3-Sialyltransferase as a Generic Inhibitor of Sialyltransferases". Journal of Biological Chemistry 277, nr 51 (11.10.2002): 49341–51. http://dx.doi.org/10.1074/jbc.m209618200.

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The mammalian Galβ1,3GalNAc-specific α2,3-sialyltransferase (ST3Gal I) was expressed as a secreted glycoprotein in High FiveTM(Trichoplusia ni) cells. Using this recombinant ST3Gal I, we screened the synthetic hexapeptide combinatorial library to explore a sialyltransferase inhibitor. We found that the hexapeptide, NH2-GNWWWW, exhibited the most strong inhibition of ST3Gal I among five different hexapeptides that were finally selected. The kinetic analysis of ST3Gal I inhibition demonstrated that this hexapeptide could act as a competitive inhibitor (Ki= 1.1 μm) on CMP-NeuAc binding to the enzyme. Moreover, the hexapeptide was shown to strongly inhibit bothN-glycan-specific α2,3- and α2,6-sialyltranferasein vitro, suggesting that this peptide may inhibit the broad range of sialyltransferases regardless of their linkage specificity. The inhibitory activityin vivowas investigated by RCA-I lectin blot analyses and by metabolicd-[6-3H]GlcNH2radiolabeling analyses ofN- andO-linked oligosaccharides in Chines hamster ovary cells. Our results demonstrate that the hexapeptide can act as a generic inhibitor of theN- andO-glycan-specific sialyltransferases in mammalian cells, which results in the significantly reduced NeuAc expression on cellular glycoproteinsin vivo.

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7

Pietrobono, Silvia, i Barbara Stecca. "Aberrant Sialylation in Cancer: Biomarker and Potential Target for Therapeutic Intervention?" Cancers 13, nr 9 (22.04.2021): 2014. http://dx.doi.org/10.3390/cancers13092014.

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Sialylation is an integral part of cellular function, governing many biological processes including cellular recognition, adhesion, molecular trafficking, signal transduction and endocytosis. Sialylation is controlled by the levels and the activities of sialyltransferases on glycoproteins and lipids. Altered gene expression of these enzymes in cancer yields to cancer-specific alterations of glycoprotein sialylation. Mounting evidence indicate that hypersialylation is closely associated with cancer progression and metastatic spread, and can be of prognostic significance in human cancer. Aberrant sialylation is not only a result of cancer, but also a driver of malignant phenotype, directly impacting key processes such as tumor cell dissociation and invasion, cell-cell and cell-matrix interactions, angiogenesis, resistance to apoptosis, and evasion of immune destruction. In this review we provide insights on the impact of sialylation in tumor progression, and outline the possible application of sialyltransferases as cancer biomarkers. We also summarize the most promising findings on the development of sialyltransferase inhibitors as potential anti-cancer treatments.

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8

Harduin-Lepers, Anne, Rosella Mollicone, Philippe Delannoy i Rafael Oriol. "The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach". Glycobiology 15, nr 8 (20.04.2005): 805–17. http://dx.doi.org/10.1093/glycob/cwi063.

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9

Yamamoto, Takeshi, Yoshimitsu Takakura i Hiroshi Tsukamoto. "Bacterial Sialyltransferases". Trends in Glycoscience and Glycotechnology 18, nr 102 (2006): 253–65. http://dx.doi.org/10.4052/tigg.18.253.

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10

Ratnam, Shobhitha, Arun Nagpurkar i Sailen Mookerjea. "Characterization of serum, liver, and intestinal sialyltransferases from rats treated with colchicine". Biochemistry and Cell Biology 65, nr 3 (1.03.1987): 183–87. http://dx.doi.org/10.1139/o87-023.

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A modified high pressure liquid chromatographic method using lactose (Galβ1 → 4G1c) as an exogenous acceptor has been used to characterize the sialyltransferases known to increase in the serum of colchicine-treated rats. The results show a 10-fold increase of Galβ1 → 4GlcNAc α2 → 6sialytransferase (α2 → 6 ST), whereas the Galβ1 → 3GlcNAc α2 → 3sialyltransferase showed only 1.6-fold increase in the serum after 17 h of colchicine treatment. The sialyltransferase activity in serum using exogenous desialylated, α1-acid glycoprotein as acceptor also showed an eightfold increase. In liver homogenate and Golgi membrane, the sialyltransferase activity when assayed with desialylated α1-acid glycoprotein as acceptor showed a slight decrease after 4 h, but returned to normal level after 17 h. A similar trend was seen when the two transferases were assayed with lactose as acceptor. The antiserum to rat α2 → 6 ST inhibited the sialyltransferase activity in serum, liver, and jejunal incubation medium. Jejunal sections from rats treated with colchicine for 4 h in presence of heated serum showed a decrease of sialyltransferase, with consequent increase of the α2 → 6 ST enzyme activity in the medium. This result suggests that intestinal tissue could be a source of increased serum enzyme activity in colchicine treatment.

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11

Tsukamoto, H., Y. Takakura, T. Mine i T. Yamamoto. "Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, -/ -Galactoside 2,3-Sialyltransferase and -Galactoside 2,6-Sialyltransferase". Journal of Biochemistry 143, nr 2 (4.11.2007): 187–97. http://dx.doi.org/10.1093/jb/mvm208.

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12

Yamamoto, Takeshi. "Marine Bacterial Sialyltransferases". Marine Drugs 8, nr 11 (5.11.2010): 2781–94. http://dx.doi.org/10.3390/md8112781.

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13

Snider, M. D., i O. C. Rogers. "Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells." Journal of Cell Biology 100, nr 3 (1.03.1985): 826–34. http://dx.doi.org/10.1083/jcb.100.3.826.

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The intracellular movement of cell surface transferrin receptor (TfR) after internalization was studied in K562 cultured human erythroleukemia cells. The sialic acid residues of the TfR glycoprotein were used to monitor transport to the Golgi complex, the site of sialyltransferases. Surface-labeled cells were treated with neuraminidase, and readdition of sialic acid residues, monitored by isoelectric focusing of immunoprecipitated TfR, was used to assess the movement of receptor to sialyltransferase-containing compartments. Asialo-TfR was resialylated by the cells with a half-time of 2-3 h. Resialylation occurred in an intracellular organelle, since it was inhibited by treatments that allow internalization of surface components but block transfer out of the endosomal compartment. Moreover, roughly half of the resialylated molecules were cleaved when cells were retreated with neuraminidase after culturing, indicating that this fraction of the molecules had returned to the cell surface. These results suggest that TfR is transported from the cell surface to the Golgi complex, the intracellular site of sialyltransferases, and then returns to the cell surface. This pathway, which has not been previously described for a cell surface receptor, may be different from the route followed by TfR in iron uptake, since reported rates of transferrin uptake and release are significantly more rapid than the resialylation of asialo-TfR.

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14

Senda, Motohiro, Akihiro Ito, Akiko Tsuchida, Tomoko Hagiwara, Tsuguhiro Kaneda, Yoko Nakamura, Kenji Kasama i in. "Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: downregulation of ST6GalNAc VI in renal cancers". Biochemical Journal 402, nr 3 (26.02.2007): 459–70. http://dx.doi.org/10.1042/bj20061118.

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Although disialyl glycosphingolipids such as GD3 and GD2 have been considered to be associated with malignant tumours, whether branched-type disialyl glycosphingolipids show such an association is not well understood. We investigated the sialyltransferases responsible for the biosynthesis of DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside). Among six GalNAc:α2,6-sialyltransferases cloned to date, we focused on ST6GalNAc III, V and VI, which utilize sialylglycolipids as substrates. In vitro enzyme analyses revealed that ST6GalNAc III and VI generated DSGG from MSGG with Vmax/Km values of 1.91 and 4.16 respectively. Transfection of the cDNA expression vectors for these enzymes resulted in DSGG expression in a renal cancer cell line. Although both ST6GalNAc III and VI genes were expressed in normal kidney cells, the expression profiles of ST6GalNAc VI among 20 renal cancer cell lines correlated clearly with those of DSGG, suggesting that the sialyltransferase involved in the synthesis of DSGG in the kidney is ST6GalNAc-VI. ST6GalNAc-VI and DSGG were found in proximal tubule epithelial cells in normal kidney tissues, while they were downregulated in renal cancer cell lines and cancer tissues. All these findings indicated that DSGG was suppressed during the malignant transformation of the proximal tubules as a maturation arrest of glycosylation.

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15

Park, Jong-Yi, Mi-Ryung Park, Deug-Nam Kwon, Min-Hui Kang, Mihye Oh, Jae-Woong Han, Ssang-Goo Cho i in. "Alpha 1,3-Galactosyltransferase Deficiency in Pigs Increases Sialyltransferase Activities That Potentially Raise Non-Gal Xenoantigenicity". Journal of Biomedicine and Biotechnology 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/560850.

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We examined whether deficiency of the GGTA1 gene in pigs altered the expression of several glycosyltransferase genes. Real-time RT-PCR and glycosyltransferase activity showed that 2 sialyltransferases [α2,3-sialyltransferase (α2,3ST) andα2,6-sialyltransferase (α2,6ST)] in the heterozygote GalT KO liver have higher expression levels and activities compared to controls. Enzyme-linked lectin assays indicated that there were also more sialic acid-containing glycoconjugate epitopes in GalT KO livers than in controls. The elevated level of sialic-acid-containing glycoconjugate epitopes was due to the low level ofα-Gal in heterozygote GalT KO livers. Furthermore, proteomics analysis showed that heterozygote GalT KO pigs had a higher expression of NAD+-isocitrate dehydrogenase (IDH), which is related to the CMP-N-acetylneuraminic acid hydroxylase (CMAH) enzyme reaction. These findings suggest the deficiency of GGTA1 gene in pigs results in increased production ofN-glycolylneuraminic acid (Neu5Gc) due to an increase ofα2,6-sialyltransferase and a CMAH cofactor, NAD+-IDH. This indicates that Neu5Gc may be a critical xenoantigen. The deletion of the CMAH gene in the GalT KO background is expected to further prolong xenograft survival.

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16

Li, M., V. Andersen i P. Lance. "Expression and Regulation of Glycosyltransferases for N-Glycosyl Oligosaccharides in Fresh Human Surgical and Murine Tissues and Cultured Cell Lines". Clinical Science 89, nr 4 (1.10.1995): 397–404. http://dx.doi.org/10.1042/cs0890397.

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1. Mammalian membrane and serum proteins are glycosylated by the addition of heterogeneous N-linked oligosaccharides. It has been widely speculated that oligosaccharide diversity is achieved by corresponding heterogeneity of expression of the glycosyltransferases that are responsible for oligosaccharide synthesis. 2. We surveyed mRNA levels of three sequentially acting glycosyltransferases, N-acetylglucosaminyltransferase I, β1,4-galactosyltransferase and α2,6-sialyltransferase, in 11 human tissues and confirmed the expected variations. 3. The size heterogeneity of α2,6-sialyltransferase transcripts reported in rat tissues was evident neither in the human tissue survey nor in a panel of murine RNAs. Tissue distributions of alternative terminal sialyltransferases, α2,6-sialyltransferase and α2,3-sialyltransferase, were distinct. 4. Relative glycosyltransferase mRNA levels in four transformed human cell lines cultured in vitro did not fully reflect levels in the corresponding human tissues. 5. Expression of α2,6-sialyltransferase mRNA was approximately 2.6-fold greater in adenocarcinomatous than in normal human colon, and β1,4-galactosyltransferase expression was approximately 1.8-fold greater in normal than in adenocarcinomatous colon. 6. n-Butyrate (0.003–0.005 mol/l), a short-chain fatty acid that is produced by colonic bacterial fermentation, caused approximately 80% inhibition of α2,6-sialyltransferase, approximately 2.5-fold induction of β1,4-galactosyltransferase and approximately 6-fold induction of N-acetylglucosaminyltransferase mRNAs in T84 (colonic) cells. The effects on α2,6-sialyltransferase and β1,4-galactosyltransferase were near maximal by 6 h, but induction of N-acetylglucosaminyltransferase was fully apparent only after exposure for 24 h.

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17

Mandrell, R. E., A. J. Lesse, J. V. Sugai, M. Shero, J. M. Griffiss, J. A. Cole, N. J. Parsons, H. Smith, S. A. Morse i M. A. Apicella. "In vitro and in vivo modification of Neisseria gonorrhoeae lipooligosaccharide epitope structure by sialylation." Journal of Experimental Medicine 171, nr 5 (1.05.1990): 1649–64. http://dx.doi.org/10.1084/jem.171.5.1649.

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After growth of gonococci in the presence of cytidine monophospho-N-acetyl-neuraminic acid (CMP-NANA), their 4.5-kD lipooligosaccharide (LOS) component was increased by approximately 400 daltons, whereas the LOS of strains lacking the 4.5-kD component were unaffected. Expression of mAb-defined epitopes on the 4.5-kD component was decreased on LOS of strains grown in CMP-NANA, and treatment of the LOS with neuraminidase reversed this affect. Gonococci incubated with human PMNs also had decreased expression of the 4.5-kD+ epitopes. A detergent extract of gonococci incorporated radiolabeled NANA in the LOS, suggesting the presence of a sialyltransferase in gonococci. Exogenous sialyltransferases also could use LOS as an acceptor.

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18

Harduin-Lepers, Anne. "Sialyltransferases functions in cancers". Frontiers in Bioscience E4, nr 1 (2012): 499–515. http://dx.doi.org/10.2741/e396.

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19

Izumi, Masayuki, i Chi-Huey Wong. "Microbial Sialyltransferases for Carbohydrate Synthesis." Trends in Glycoscience and Glycotechnology 13, nr 72 (2001): 345–60. http://dx.doi.org/10.4052/tigg.13.345.

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20

Takashima, Shou, i Shuichi Tsuji. "Functional Diversity of Mammalian Sialyltransferases". Trends in Glycoscience and Glycotechnology 23, nr 132 (2011): 178–93. http://dx.doi.org/10.4052/tigg.23.178.

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21

Kajiwara, Hitomi, Toshiki Mine i Takeshi Yamamoto. "Sialyltransferases Obtained from Marine Bacteria". Journal of Applied Glycoscience 56, nr 2 (2009): 77–82. http://dx.doi.org/10.5458/jag.56.77.

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Harduin-Lepers, Anne, Marie-Ange Recchi i Philippe Delannoy. "1994, the year of sialyltransferases". Glycobiology 5, nr 8 (1995): 741–58. http://dx.doi.org/10.1093/glycob/5.8.741.

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23

Hinou, Hiroshi, Xue-Long Sun i Yukishige Ito. "Bisubstrate-type inhibitor of sialyltransferases". Tetrahedron Letters 43, nr 50 (grudzień 2002): 9147–50. http://dx.doi.org/10.1016/s0040-4039(02)02272-4.

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24

Paulson, J. C., J. Weinstein i A. Schauer. "Tissue-specific Expression of Sialyltransferases". Journal of Biological Chemistry 264, nr 19 (lipiec 1989): 10931–34. http://dx.doi.org/10.1016/s0021-9258(18)60407-7.

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25

Paulson, J. C. "S8.1 Selectins, sialosides, and sialyltransferases". Glycoconjugate Journal 10, nr 4 (sierpień 1993): 266. http://dx.doi.org/10.1007/bf01209943.

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26

Rao, Francesco V., Jamie R. Rich, Bojana Rakić, Sai Buddai, Marc F. Schwartz, Karl Johnson, Caryn Bowe i in. "Structural insight into mammalian sialyltransferases". Nature Structural & Molecular Biology 16, nr 11 (11.10.2009): 1186–88. http://dx.doi.org/10.1038/nsmb.1685.

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27

Dall'Olio, Fabio. "Sialyltransferases of developing rat brain". Glycoconjugate Journal 7, nr 4 (1990): 301–10. http://dx.doi.org/10.1007/bf01073374.

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28

Broquet, Pierre, Hélene Baubichon-Cortay, Pascal George i Pierre Louisot. "Glycoprotein sialyltransferases in eucaryotic cells". International Journal of Biochemistry 23, nr 4 (styczeń 1991): 385–89. http://dx.doi.org/10.1016/0020-711x(91)90164-i.

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Lee, Ho Jun, Luke L. Lairson, Jamie R. Rich, Emilie Lameignere, Warren W. Wakarchuk, Stephen G. Withers i Natalie C. J. Strynadka. "Structural and Kinetic Analysis of Substrate Binding to the Sialyltransferase Cst-II from Campylobacter jejuni". Journal of Biological Chemistry 286, nr 41 (5.08.2011): 35922–32. http://dx.doi.org/10.1074/jbc.m111.261172.

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Sialic acids play important roles in various biological processes and typically terminate the oligosaccharide chains on the cell surfaces of a wide range of organisms, including mammals and bacteria. Their attachment is catalyzed by a set of sialyltransferases with defined specificities both for their acceptor sugars and the position of attachment. However, little is known of how this specificity is encoded. The structure of the bifunctional sialyltransferase Cst-II of the human pathogen Campylobacter jejuni in complex with CMP and the terminal trisaccharide of its natural acceptor (Neu5Ac-α-2,3-Gal-β-1,3-GalNAc) has been solved at 1.95 Å resolution, and its kinetic mechanism was shown to be iso-ordered Bi Bi, consistent with its dual acceptor substrate specificity. The trisaccharide acceptor is seen to bind to the active site of Cst-II through interactions primarily mediated by Asn-51, Tyr-81, and Arg-129. Kinetic and structural analyses of mutants modified at these positions indicate that these residues are critical for acceptor binding and catalysis, thereby providing significant new insight into the kinetic and catalytic mechanism, and acceptor specificity of this pathogen-encoded bifunctional GT-42 sialyltransferase.

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Ellies, Lesley G., Markus Sperandio, Gregory H. Underhill, James Yousif, Michael Smith, John J. Priatel, Geoffrey S. Kansas, Klaus Ley i Jamey D. Marth. "Sialyltransferase specificity in selectin ligand formation". Blood 100, nr 10 (15.11.2002): 3618–25. http://dx.doi.org/10.1182/blood-2002-04-1007.

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Selectin ligands are glycan structures that participate in leukocyte trafficking and inflammation. At least 6 ST3Gal sialyltransferases (I-VI) have been identified that may contribute to selectin ligand formation. However, it is not known which of these sialyltransferases are involved in vivo and whether they may differentially regulate selectin function. We have produced and characterized mice genetically deficient in ST3Gal-I, ST3Gal-II, ST3Gal-III, and ST3Gal-IV. Unlike mice bearing severe defects in selectin ligand formation, there was no finding of leukocytosis with these single ST3Gal deficiencies. Among neutrophils, only ST3Gal-IV was found to play a role in the synthesis of selectin ligands. In vitro rolling of marrow-derived neutrophils on E- or P-selectins presented by Chinese hamster ovary cells was reduced in the absence of ST3Gal-IV. However, in a tumor necrosis factor α (TNF-α)–induced inflammation model in vivo, no defect among P-selectin ligands was observed. Nevertheless, the number of leukocytes rolling on postcapillary venules in an E-selectin–dependent manner was decreased while E-selectin–dependent rolling velocity was increased. We propose that multiple ST3Gal sialyltransferases contribute to selectin ligand formation, as none of these ST3Gal deficiencies recapitulated the degree of E- and P-selectin ligand deficit observed on neuraminidase treatment of intact neutrophils. Our findings indicate a high degree of functional specificity among sialyltransferases and a substantial role for ST3Gal-IV in selectin ligand formation.

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Powell, L. D., S. W. Whiteheart i G. W. Hart. "Cell surface sialic acid influences tumor cell recognition in the mixed lymphocyte reaction." Journal of Immunology 139, nr 1 (1.07.1987): 262–70. http://dx.doi.org/10.4049/jimmunol.139.1.262.

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Abstract The Ia+ B cell lymphoma, AKTB-1b, fails to stimulate thymic lymphocytes in a one-way mixed lymphocyte reaction unless pretreated with sialidase or inhibitors of N-linked oligosaccharide processing. A comparison of different sialidases and sialyltransferases suggests that the removal of only a subset of total surface sialic acid, rather than net desialylation of the cell surface, is required. Three sialidases were compared, including Vibrio cholerae (VC) and Clostridium perfringens (CP), which will cleave alpha 2-3, alpha 2-6, and alpha 2-8, sialic acid linkages, and Newcastle Disease virus (NDV), which will remove only alpha 2-3 and alpha 2-8 linked sialic acid. When treated with equivalent units of sialidase, CP-, VC-, and NDV-treated cells were 24-fold, sixfold, and threefold better stimulators than untreated cells. In contrast, VC released 1.3-fold and 2.5-fold more sialic acid per cell than did CP or NDV, respectively. Furthermore, VC was superior in reducing the levels of binding of the sialic acid-specific lectin, Limulus polyphemus agglutinin, in exposing Gal beta 1-3GalNAc and Gal beta 1-4GlcNAc residues, and in desialylating gangliosides. Two-dimensional gel analysis indicated that VC and CP were both equal and superior to NDV in the desialylation of iodinatable cell-surface proteins, including H-2Kk, I-A beta k, and a highly sialylated 65,000 dalton protein of unknown identity. Maximal resialylation of CP-treated cells with exogenously added CMP-NANA and either the alpha 2-3(Gal beta 1-3GalNAc) or alpha 2-6(Gal beta 1-4GlcNAc) sialyltransferase did not reduce the stimulatory capacity of these cells. However, resialylation of VC-treated cells with just CMP-NANA alone resulted in 49% reversal of their stimulatory capacity, and no additional reversal could be achieved with either of the sialyltransferases. Although the alpha 2-6(Gal beta 1-4GlcNAc) sialyltransferase was capable of adding back approximately 10% of the sialic acid removed, the endogenous activity added back approximately 0.1% of the total sialic acid removed. SDS-PAGE gels of the sialylated cells indicated that the exogenously added sialyltransferase labeled many different proteins, whereas the endogenous activity labeled far fewer proteins, predominantly in 46,000 and 25,000 m.w. range. Both the desialylation and resialylation data suggest that the sialidase-dependent stimulation is due to the desialylation of specific membrane structures. Together with previous studies, these data suggest that the sialic acids involved are probably alpha 2-6 linked to N-linked glycosyl moieties.

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Houeix, Benoit, i Michael T. Cairns. "Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases". PeerJ 7 (11.02.2019): e5788. http://dx.doi.org/10.7717/peerj.5788.

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Background Sialyltransferases (SIATs) are a family of enzymes that transfer sialic acid (Sia) to glycan chains on glycoproteins, glycolipids, and oligosaccharides. They play key roles in determining cell–cell and cell-matrix interactions and are important in neuronal development, immune regulation, protein stability and clearance. Most fully characterized SIATs are of mammalian origin and these have been used for in vitro and in vivo modification of glycans. Additional versatility could be achieved by the use of animal SIATs from other species that live in much more variable environments. Our aim was to generate a panel of stable CHO cell lines expressing a range of vertebrate SIATs with different physicochemical and functional properties. Methods The soluble forms of various animal ST6Gal and ST3Gal enzymes were stably expressed from a Gateway-modified secretion vector in CHO cells. The secreted proteins were IMAC-purified from serum-free media. Functionality of the protein was initially assessed by lectin binding to the host CHO cells. Activity of purified proteins was determined by a number of approaches that included a phosphate-linked sialyltransferase assay, HILIC-HPLC identification of sialyllactose products and enzyme-linked lectin assay (ELLA). Results A range of sialyltransferase from mammals, birds and fish were stably expressed in CHO Flp-In cells. The stable cell lines expressing ST6Gal1 modify the glycans on the surface of the CHO cells as detected by fluorescently labelled lectin microscopy. The catalytic domains, as isolated by Ni Sepharose from culture media, have enzymatic activities comparable to commercial enzymes. Sialyllactoses were identified by HILIC-HPLC on incubation of the enzymes from lactose or whey permeate. The enzymes also increased SNA-I labelling of asialofetuin when incubated in a plate format. Conclusion Stable cell lines are available that may provide options for the in vivo sialylation of glycoproteins. Proteins are active and should display a variety of biological and physicochemical properties based on the animal source of the enzyme.

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Kuhn, Bernd, Jörg Benz, Michael Greif, Alfred Engel, Harald Sobek i Markus Rudolph. "Crystal Structure of Human α-2,6 Sialyltransferase". Acta Crystallographica Section A Foundations and Advances 70, a1 (5.08.2014): C307. http://dx.doi.org/10.1107/s2053273314096922.

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Human β-galactoside α-2,6 sialyltransferase I (ST6Gal-I) establishes the final glycosylation pattern of many glycoproteins by transferring a sialyl moiety to a terminal galactose. Complete sialylation of therapeutic immunoglobulins is essential for their anti-inflammatory activity and for protein stability. However, a complete glycan tree is difficult to achieve in vitro due to limited activity of ST6Gal-I for some galactose acceptors. No structural information on ST6Gal-I that could help to improve the enzymatic properties of ST6Gal-I for biotechnological purposes was previously available. We describe the crystal structure of human ST6Gal-I, which allows rationalizing the inhibitory activity of cytosine-based nucleotides. ST6Gal-I differs from related sialyltransferases by several large insertions and deletions that determine its regio- and substrate specificity. Excitingly, a large glycan binds to the active site in a catalytically competent orientation, representing the general binding mode of any substrate glycoprotein. This binding mode also rationalizes why some galactose acceptors are incompletely sialylated. Comparison with a bacterial sialyltransferase lends first insight into the Michaelis complex. The results support an SN2 mechanism with inversion of configuration at the sialyl residue and suggest substrate-assisted catalysis with a charge relay mechanism that bears conceptual similarity to serine proteases.

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Miró, Laura, Júlia López, Pedro E. Guerrero, Neus Martínez-Bosch, Noemí Manero-Rupérez, Mireia Moreno, M. Rosa Ortiz, Esther Llop, Pilar Navarro i Rosa Peracaula. "Sialyltransferase Inhibitor Ac53FaxNeu5Ac Reverts the Malignant Phenotype of Pancreatic Cancer Cells, and Reduces Tumor Volume and Favors T-Cell Infiltrates in Mice". Cancers 14, nr 24 (12.12.2022): 6133. http://dx.doi.org/10.3390/cancers14246133.

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Hypersialylation is a feature of pancreatic ductal adenocarcinoma (PDA) and it has been related to tumor malignancy and immune suppression. In this work, we have evaluated the potential of the sialyltransferase inhibitor, Ac53FaxNeu5Ac, to decrease tumor sialoglycans in PDA and to revert its malignant phenotype. Sialoglycans on PDA cells were evaluated by flow cytometry, and the functional impact of Ac53FaxNeu5Ac was assessed using E-selectin adhesion, migration, and invasion assays. PDA tumors were generated in syngeneic mice from KC cells and treated with Ac53FaxNeu5Ac to evaluate tumor growth, mice survival, and its impact on blocking sialic acid (SA) and on the tumor immune component. Ac53FaxNeu5Ac treatment on human PDA cells decreased α2,3-SA and sialyl-Lewisx, which resulted in a reduction in their E-selectin adhesion, and in their migratory and invasive capabilities. Subcutaneous murine tumors treated with Ac53FaxNeu5Ac reduced their volume, their SA expression, and modified their immune component, with an increase in CD8+ T-lymphocytes and NK cells. In conclusion, Ac53FaxNeu5Ac treatment weakened PDA cells’ malignant phenotype, thereby reducing tumor growth while favoring anti-tumor immune surveillance. Altogether, these results show the positive impact of reducing SA expression by inhibiting cell sialyltransferases and open the way to use sialyltransferase inhibitors to target this dismal disease.

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Antonova, E. N., O. V. Glazova, A. V. Gaponova, N. A. Volkova i P. Y. Volchkov. "111 Inhibition of Avian Influenza Virus by Blocking Specific Sialyltransferases". Reproduction, Fertility and Development 30, nr 1 (2018): 195. http://dx.doi.org/10.1071/rdv30n1ab111.

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It is known that avian influenza penetrates into the host cell by binding with sialic acids, the terminal residues of oligosaccharides. Avian influenza A virus preferably recognises α(2,3)-linked sialic acid residues as a receptor for penetration whereas human influenza A virus preferably binds with α(2,6)-linked sialic acids. Prevention of transfer of sialic acids to sugar bond or removal of it could be a defensive strategy against viral infection. There are 6 known sialyltransferases (ST3Gal1-6) that transfer α(2,3)-linked sialic acid residues to sugar branches. Most avian influenza virus isolates bind strongly to a sugar chain containing Neu5Aca(2,3) residues. In our study, we have shown that knockout of sialyltransferases leads to inhibition of viral infection. To find the expressed sialyltransferases in respiratory and digestive tracts, we used RT-qPCR. Tissue samples were taken from 3 chickens of Haisex white cross. Expression of mRNA was measured by RT-qPCR in 3 repeats and serial dilutions. Data analysis was carried out using the 2−ΔΔCt method. The amount of total RNA was normalised using GAPDH mRNA. For CRISPR/Cas9 targeting sialyltransferases, 3 guide RNAs for each gene were designed. We confirmed knockout (KO) of ST3GAL1 and ST3GAL6 by T7E assay. To estimate sialylation level on the cell surface, we performed a lectin-binding assay. For the assay, cells were incubated with fluorescein isothiocyanate (FITC)-labelled Maackia amurensis lectins and then subjected to flow-cytometry analysis to quantify the percentage of α(2,3)-sialylated cells in DF1 knockout (KO) v. DF1 wild type (wt) cell line. To estimate resistance to viral infection, a hemagglutinin binding assay was done, using fluorescein isothiocyanate (FITC)-labelled HA1 from H5N1 (A/Vietnam/1203/2004). To quantify the percentage of agglutinated HA1 molecules, DF1 KO and DF1 wt cells were analysed by flow cytometry. We found that mainly ST3GAL4 and ST3GAL5 are expressed in the chicken intestine (3-fold and 20-fold less compared with GAPDH level, respectively; other STs were not detected), and mainly ST3GAL1 and ST3GAL6 are expressed in the chicken respiratory tract (5-fold and 1.2-fold more compared with GAPDH level respectively; other STs were not detected). The expression profile of α(2,3)-sialyltransferases in the DF1 chicken cell line showed the noticeable expression of ST3GAL1 and ST3GAL6 compared with others as has been shown for the respiratory tract (500- and 1000-fold less compared with GAPDH respectively; other STs were not detected). In this study, we adopted the CRISPR/Cas9 system to knock out ST3GAL1 and ST3GAL6 genes in the chicken DF1 cell line. We confirmed that knockout of the genes leads to extinction of α(2,3)-sialic residues from the cell surface (7% v. 100% for DF1 KO v. DF1 wt cell line). Finally, we showed that knockout of sialyltransferases in the DF1 cells increases resistance against influenza A infection (16% v. 100% for DF1 KO v. DF1 wt cell line). Thus, creation of transgenic poultry with tissue-specific knockout of the α(2,3) sialyltransferases might protect domestic birds against influenza virus and block possible transfer of avian flu to human population.

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Skacel, PO, AJ Edwards, CT Harrison i WM Watkins. "Enzymic control of the expression of the X determinant (CD15) in human myeloid cells during maturation: the regulatory role of 6- sialytransferase". Blood 78, nr 6 (15.09.1991): 1452–60. http://dx.doi.org/10.1182/blood.v78.6.1452.1452.

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Abstract To establish the basis for the reduced expression of the X determinant on leukemic blasts and the changes in antigenic expression that occur during myeloid maturation, the presence on myeloid cells of X and related structures was examined in conjunction with studies on the activities of the glycosyltransferases involved in their biosynthesis. Expression of X and sialyl-X was weak on blasts in comparison with neutrophils despite the presence of the requisite precursor structures. Much higher levels of 3-fucosyltransferase activity were found in blasts than in neutrophils when nonsialylated substrates were used, but, whereas the enzyme in neutrophils reacted equally well with 3′- sialylated and nonsialylated acceptors, the enzyme in blasts showed a marked preference for nonsialylated substrates. 6′-Sialyltransferase activity was strong in blasts but was not detectable in neutrophils, whereas a much lower level of 3′-sialyltransferase activity was present in both blasts and neutrophils. Dimethyl sulfoxide-induced maturation of HL60 cells was associated with (1) a decrease in both 6′- sialyltransferase and 3-fucosyltransferase activities, (2) a change in the substrate specificity of 3-fucosyltransferase towards that found in mature cells, and (3) increased cell surface expression of sialyl-X. These results suggest that the reduced expression of X in myeloblasts is related to the presence of the strong 6′-sialyltransferase, which uses the precursor substrate at the expense of the 3-fucosyltransferase and prevents the synthesis of X and sialyl-X. The developmental regulation of the levels of 3′- and 6′-sialyltransferases, and the level and specificity of the 3-fucosyltransferases, therefore controls the expression of X and its degree of sialylation.

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Skacel, PO, AJ Edwards, CT Harrison i WM Watkins. "Enzymic control of the expression of the X determinant (CD15) in human myeloid cells during maturation: the regulatory role of 6- sialytransferase". Blood 78, nr 6 (15.09.1991): 1452–60. http://dx.doi.org/10.1182/blood.v78.6.1452.bloodjournal7861452.

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To establish the basis for the reduced expression of the X determinant on leukemic blasts and the changes in antigenic expression that occur during myeloid maturation, the presence on myeloid cells of X and related structures was examined in conjunction with studies on the activities of the glycosyltransferases involved in their biosynthesis. Expression of X and sialyl-X was weak on blasts in comparison with neutrophils despite the presence of the requisite precursor structures. Much higher levels of 3-fucosyltransferase activity were found in blasts than in neutrophils when nonsialylated substrates were used, but, whereas the enzyme in neutrophils reacted equally well with 3′- sialylated and nonsialylated acceptors, the enzyme in blasts showed a marked preference for nonsialylated substrates. 6′-Sialyltransferase activity was strong in blasts but was not detectable in neutrophils, whereas a much lower level of 3′-sialyltransferase activity was present in both blasts and neutrophils. Dimethyl sulfoxide-induced maturation of HL60 cells was associated with (1) a decrease in both 6′- sialyltransferase and 3-fucosyltransferase activities, (2) a change in the substrate specificity of 3-fucosyltransferase towards that found in mature cells, and (3) increased cell surface expression of sialyl-X. These results suggest that the reduced expression of X in myeloblasts is related to the presence of the strong 6′-sialyltransferase, which uses the precursor substrate at the expense of the 3-fucosyltransferase and prevents the synthesis of X and sialyl-X. The developmental regulation of the levels of 3′- and 6′-sialyltransferases, and the level and specificity of the 3-fucosyltransferases, therefore controls the expression of X and its degree of sialylation.

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Sasaki, Katsutoshi. "Molecular Cloning and Characterization of Sialyltransferases." Trends in Glycoscience and Glycotechnology 8, nr 41 (1996): 195–215. http://dx.doi.org/10.4052/tigg.8.195.

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Schwardt, Oliver, Tamara Visekruna, Said Rabbani i Beat Ernst. "Minireview: Bacterial Sialyltransferases for Carbohydrate Synthesis". CHIMIA International Journal for Chemistry 60, nr 4 (28.04.2006): 234–40. http://dx.doi.org/10.2533/000942906777674787.

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Watanabe, Masaki, Katsuhide Miyake, Shin Yamamoto, Yohei Kataoka, Satoshi Koizumi, Tetsuo Endo, Akio Ozaki i Shinji Iijima. "Identification of sialyltransferases of Streptococcus agalactiae". Journal of Bioscience and Bioengineering 93, nr 6 (styczeń 2002): 610–13. http://dx.doi.org/10.1016/s1389-1723(02)80246-8.

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WATANABE, MASAKI, KATSUHIDE MIYAKE, SHIN YAMAMOTO, YOHEI KATAOKA, SATOSHI KOIZUMI, TETSUO ENDO, AKIO OZAKI i SHINJI IIJIMA. "Identification of Sialyltransferases of Streptococcus agalactiae." Journal of Bioscience and Bioengineering 93, nr 6 (2002): 610–13. http://dx.doi.org/10.1263/jbb.93.610.

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Dorst, J. A. L. M. van, J. P. Kamerling i J. F. G. Vliegenthart. "Exploring the substrate specificity of sialyltransferases". Pure and Applied Chemistry 69, nr 3 (1.01.1997): 537–42. http://dx.doi.org/10.1351/pac199769030537.

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Ko, Chou-Yuan, Tian-Huei Chu, Ching-Cheng Hsu, Hsin-Pao Chen, Shih-Chung Huang, Chen-Lin Chang, Shiow-Jyu Tzou i in. "Bioinformatics Analyses Identify the Therapeutic Potential of ST8SIA6 for Colon Cancer". Journal of Personalized Medicine 12, nr 3 (4.03.2022): 401. http://dx.doi.org/10.3390/jpm12030401.

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Sialylation of glycoproteins is modified by distinct sialyltransferases such as ST3Gal, ST6Gal, ST6GalNAc, or ST8SIA with α2,3-, α2,6-, or α2,8-linkages. Alteration of these sialyltransferases causing aberrant sialylation is associated with the progression of colon cancer. However, among the ST8- sialyltransferases, the role of ST8SIA6 in colon cancer remains poorly understood. In this study, we explored the involvement of ST8SIA6 in colon cancer using multiple gene databases. The relationship between ST8SIA6 expression and tumor stages/grades was investigated by UALCAN analysis, and Kaplan–Meier Plotter analysis was used to analyze the expression of ST8SIA6 on the survival outcome of colon cancer patients. Moreover, the biological functions of ST8SIA6 in colon cancer were explored using LinkedOmics and cancer cell metabolism gene DB. Finally, TIMER and TISMO analyses were used to delineate ST8SIA6 levels in tumor immunity and immunotherapy responses, respectively. ST8SIA6 downregulation was associated with an advanced stage and poorly differentiated grade; however, ST8SIA6 expression did not affect the survival outcomes in patients with colon cancer. Gene ontology analysis suggested that ST8SIA6 participates in cell surface adhesion, angiogenesis, and membrane vesicle trafficking. In addition, ST8SIA6 levels affected immunocyte infiltration and immunotherapy responses in colon cancer. Collectively, these results suggest that ST8SIA6 may serve as a novel therapeutic target towards personalized medicine for colon cancer.

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Hebbar, M., M. A. Krzewinski-Recchi, L. Hornez, A. Verdière, A. Harduin-Lepers, J. Bonneterre, P. Delannoy i J. P. Peyrat. "Prognostic value of Tumoral Sialyltransferase Expression and Circulating E-Selectin Concentrations in Node-Negative Breast Cancer Patients". International Journal of Biological Markers 18, nr 2 (kwiecień 2003): 116–22. http://dx.doi.org/10.1177/172460080301800204.

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Aims and Background A crucial step in the metastatic process is the interaction between the endothelial molecule E-selectin and its tumoral ligands sialyl-Lewisx and sialyl-Lewisa. Sialyltranferases are involved in the biosynthesis of these ligands. The aim of this study was to assess the prognostic value of tumoral sialyltransferase expression and of circulating soluble E-selectin (sE-selectin) in node-negative breast cancer patients. Methods Using a multiplex RT-PCR method, we measured the expression of five sialyltransferases (ST3Gal III, ST6Gal I, ST3Gal IV, ST3Gal I and ST3Gal II) in tumors of 135 surgically treated node-negative breast cancer patients. Circulating sE-selectin concentrations were measured by an ELISA method prior to surgery. We also analyzed tumor size, histoprognostic grading and steroid hormone receptor status. Results The median follow-up was 7.5 years. Expression of estrogen receptors was associated with a good prognosis for relapse-free survival in univariate analysis. A high ST3Gal III/ST6Gal I ratio and a high sE-selectin concentration were associated with a bad prognosis for relapse-free survival and overall survival in univariate and multivariate analysis. Conclusion In the present study, tumoral sialyltransferase expression and circulating sE-selectin concentrations had prognostic value in patients with node-negative breast cancer. This result provides further evidence for the important role of these agents in the metastatic process.

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Teintenier-Lelièvre, Mélanie, Sylvain Julien, Sylvie Juliant, Yann Guerardel, Martine Duonor-Cérutti, Philippe Delannoy i Anne Harduin-Lepers. "Molecular cloning and expression of a human hST8Sia VI (α2,8-sialyltransferase) responsible for the synthesis of the diSia motif on O-glycosylproteins". Biochemical Journal 392, nr 3 (6.12.2005): 665–74. http://dx.doi.org/10.1042/bj20051120.

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Based on BLAST analysis of the human and mouse genome databases using the human CMP sialic acid; α2,8-sialyltransferase cDNA (hST8Sia I; EC 2.4.99.8), a putative sialyltransferase gene, was identified on human chromosome 10. The genomic organization was found to be similar to that of hST8Sia I and hST8Sia V. Transcriptional expression analysis showed that the newly identified gene was constitutively expressed at low levels in various human tissues and cell lines. We have isolated a full-length cDNA clone from the breast cancer cell line MCF-7 that encoded a type II membrane protein of 398 amino acid residues with the conserved motifs of sialyltransferases. We have established a mammary cell line (MDA-MB-231) stably transfected with the full-length hST8Sia VI and the analysis of sialylated carbohydrate structures expressed at the cell surface clearly indicated the disappearance of Neu5Acα2-3-sialylated structures. The transient expression of a truncated soluble form of the enzyme in either COS-7 cells or insect Sf-9 cells led to the production of an active enzyme in which substrate specificity was determined. Detailed substrate specificity analysis of the hST8Sia VI recombinant enzyme in vitro, revealed that this enzyme required the trisaccharide Neu5Acα2-3Galβ1-3GalNAc (where Neu5Ac is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) to generate diSia (disialic acid) motifs specifically on O-glycans.

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KITAZUME, Shinobu, Kazuhiro NAKAGAWA, Naomasa YAMAMOTO, Makoto HIGUCHI, Takaomi SAIDO i Yasuhiro HASHIMOTO. "Pathophysiology of sialyltransferases cleavage by Alzheimer's · -secretase". Japanese Journal of Thrombosis and Hemostasis 17, nr 1 (2006): 78–82. http://dx.doi.org/10.2491/jjsth.17.78.

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GOTO, Takahiro. "Studies on sialyltransferases of fetal calf liver." Japanese Journal of Oral & Maxillofacial Surgery 31, nr 2 (1985): 230–39. http://dx.doi.org/10.5794/jjoms.31.230.

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Anne Harduin-Lepers. "Comprehensive Analysis of Sialyltransferases in Vertebrate Genomes". Glycobiology Insights 2 (2010): 29–61. http://dx.doi.org/10.4137/gbi.s3123.

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Tsuji, S. "Molecular Cloning and Functional Analysis of Sialyltransferases". Journal of Biochemistry 120, nr 1 (1.07.1996): 1–13. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021369.

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Wu, Zhengliang L., Anthony D. Person, Andrew J. Burton, Ravinder Singh, Barbara Burroughs, Dan Fryxell, Timothy J. Tatge i in. "Direct fluorescent glycan labeling with recombinant sialyltransferases". Glycobiology 29, nr 11 (30.07.2019): 750–54. http://dx.doi.org/10.1093/glycob/cwz058.

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Abstract Glycosylation is a common modification found on numerous proteins and lipids. However, direct detection of glycans on these intact biomolecules has been challenge. Here, utilizing enzymatic incorporation of fluorophore-conjugated sialic acids, dubbed as direct fluorescent glycan labeling, we report the labeling and detection of N- and O-glycans on glycoproteins. The method allows detection of specific glycans without the laborious gel blotting and chemiluminescence reactions used in Western blotting. The method can also be used with a variety of fluorescent dyes.

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