Efficient synthesis of 6′-sialyllactose, 6,6′-disialyllactose, and 6′-KDO-lactose by metabolically engineered E. coli expressing a multifunctional sialyltransferase from the Photobacterium sp. JT-ISH-224

Drouillard, S.; Mine, Toshiki; Kajiwara, Hitomi; Yamamoto, Takeshi; Samain, E.

doi:10.1016/j.carres.2010.02.018

Cited by 83 publications

(55 citation statements)

References 17 publications

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“…JT-ISH-224 is similar to that of the α2,6-sialyltransferase cloned from P. damselae JT0160. To date, it has been revealed that the α2,6-sialyltransferase cloned from JT-ISH-224 can transfer Neu5Ac to both O-6 and O-6′ hydroxyl groups of lactose simultaneously and gives 6,6′-disialyllactose, and transfers KDO (2-keto-3-deoxyoctonate) to the O-6′ hydroxyl group of lactose and gives KDO-lactose [53]. The structures of the reaction products described here are shown in Figure 4.…”

Section: Enzymatic Properties Of Marine Bacterial Sialyltransferasesmentioning

confidence: 99%

“…Very recently, it has been also reported that more than 25 g/L of both 6′-sialyllactose and 3′-sialyllactose have been produced by a high-density cell culture of E. coli strains overexpressing bacterial sialyltransferases of α2,6-sialyltransferase from Photobacterium sp. and α2,3-sialyltransferase from N. meningitidis , respectively [53,59]. In the case of the sialyllactose production system using the transformed bacterium by Photobacterium sp.…”

Section: Application Of Sialyltransferasesmentioning

confidence: 99%

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Marine Bacterial Sialyltransferases

Yamamoto

2010

Marine Drugs

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Sialyltransferases transfer N-acetylneuraminic acid (Neu5Ac) from the common donor substrate of these enzymes, cytidine 5′-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac), to acceptor substrates. The enzymatic reaction products including sialyl-glycoproteins, sialyl-glycolipids and sialyl-oligosaccharides are important molecules in various biological and physiological processes, such as cell-cell recognition, cancer metastasis, and virus infection. Thus, sialyltransferases are thought to be important enzymes in the field of glycobiology. To date, many sialyltransferases and the genes encoding them have been obtained from various sources including mammalian, bacterial and viral sources. During the course of our research, we have detected over 20 bacteria that produce sialyltransferases. Many of the bacteria we isolated from marine environments are classified in the genus Photobacterium or the closely related genus Vibrio. The paper reviews the sialyltransferases obtained mainly from marine bacteria.

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Section: Enzymatic Properties Of Marine Bacterial Sialyltransferasesmentioning

confidence: 99%

Section: Application Of Sialyltransferasesmentioning

confidence: 99%

Marine Bacterial Sialyltransferases

Yamamoto

2010

Marine Drugs

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“…6'-sialyllactose was produced with genetically engineered Escherichia coli expressing a2,6-sialyltransferase gene from Photobacterium sp. JT-ISH-224 and CMP-NeuAc synthase gene from Neisseria meningitides and purified according to the methods reported by Drouillard et al (2010). The purity and structure was confirmed by HPLC (Endo et al, 2009) and 1 H-NMR spectrum, respectively.…”

Section: Methodsmentioning

confidence: 99%

Sialyllactose ameliorates myopathic phenotypes in symptomatic GNE myopathy model mice

Yonekawa

Malicdan

Cho

et al. 2014

Brain

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Patients with GNE myopathy, a progressive and debilitating disease caused by a genetic defect in sialic acid biosynthesis, rely on supportive care and eventually become wheelchair-bound. To elucidate whether GNE myopathy is treatable at a progressive stage of the disease, we examined the efficacy of sialic acid supplementation on symptomatic old GNE myopathy mice that have ongoing, active muscle degeneration. We examined the therapeutic effect of a less metabolized sialic acid compound (6'-sialyllactose) or free sialic acid (N-acetylneuraminic acid) by oral, continuous administration to 50-week-old GNE myopathy mice for 30 weeks. To evaluate effects on their motor performance in living mice, spontaneous locomotion activity on a running wheel was measured chronologically at 50, 65, 72 and 80 weeks of age. The size, force production, and pathology of isolated gastrocnemius muscle were analysed at the end point. Sialic acid level in skeletal muscle was also measured. Spontaneous locomotion activity was recovered in 6'-sialyllactose-treated mice, while NeuAc-treated mice slowed the disease progression. Treatment with 6'-sialyllactose led to marked restoration of hyposialylation in muscle and consequently to robust improvement in the muscle size, contractile parameters, and pathology as compared to NeuAc. This is due to the fact that 6'-sialyllactose is longer working as it is further metabolized to free sialic acid after initial absorption. 6'-sialyllactose ameliorated muscle atrophy and degeneration in symptomatic GNE myopathy mice. Our results provide evidence that GNE myopathy can be treated even at a progressive stage and 6'-sialyllactose has more remarkable advantage than free sialic acid, providing a conceptual proof for clinical use in patients.

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“…Using chemical-and/or enzymatic-methods, different HMOs have been synthesized, e.g. fucosyllactose [7][8][9][10][11][12][13], sialyllactose [14][15][16][17], or lacto-N-neotetraose [18][19][20].…”

Section: Introductionmentioning

confidence: 99%