Toshihiko Katoh
Laboratory of Molecular Biology
GlycomicsGlycoproteinChemical synthesisGolgi apparatusMutantCell signalingMolecular biologySulfationEndoplasmic reticulumMass spectrometryMucinEnzymeChemistryEpitopeGlycoside hydrolaseImmunologyGlycobiologyGlycanMucor hiemalisFucoseGlycosylationOligosaccharideGlycosynthaseLeuconostoc mesenteroidesSIGLECBifidobacterium bifidumEndoglycosidaseChromatographyBiochemistryStrain (chemistry)StereochemistryMedicineBiologyImmune systemMicrobiologyCell biologyCytosol
25Publications
10H-index
488Citations
Publications 26
Newest
#1Yusuke MimuraH-Index: 14
#2Toshihiko Katoh (LMB: Laboratory of Molecular Biology)H-Index: 10
Last. Pauline M. RuddH-Index: 28
view all 11 authors...
Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to Asn297 of the Fc is essential for antibody effector functions, fucose and outer-arm sugars attached to the core heptasaccharide that generate structural heterogeneity (glycoforms) exhibit unique biological activities. Hence, efficient and quantitative glycan analysis techniques have been increasingly important fo...
75 CitationsSource
#1Takayuki Higashiyama (Kyoto University)H-Index: 2
#2Midori Umekawa (Kyoto University)H-Index: 17
Last. Kenji Yamamoto (Kyoto University)H-Index: 57
view all 6 authors...
Abstract The chemo-enzymatic synthesis of an artificially N-glycosylated derivative of glucagon, a peptide hormone that regulates the blood sugar level, is described. We synthesized the glycosylated glucagon by chemical synthesis of an N-acetylglucosaminyl peptide and enzymatic transfer of an oligosaccharide using the transglycosylation activity of the glycosynthase-like mutant of Mucor hiemalis endo-β-N-acetylglucosaminidase (Endo-M) and sialo-oligosaccharide oxazoline as a donor substrate. The...
2 CitationsSource
#1Toshihiko Katoh (Ishikawa Prefectural University)H-Index: 10
#2Takako Maeshibu (Kyoto University)H-Index: 1
Last. Takane Katayama (Ishikawa Prefectural University)H-Index: 34
view all 11 authors...
Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by bifidobacteria remains fragmentary, especially regarding how they decompose sulfated glycans, which are abundantly found in mucin sugar-chains. Here, we examined the abilities of several Bifidobacterium strains to degrade a sulfated glycan substrate and ident...
10 CitationsSource
#1Yusuke Tomabechi (Ishikawa Prefectural University)H-Index: 8
#2Toshihiko Katoh (Ishikawa Prefectural University)H-Index: 10
Last. Kenji Yamamoto (Ishikawa Prefectural University)H-Index: 57
view all 5 authors...
For chemo-enzymatic synthesis of a glycosylated peptide, 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium chloride (DMT-MM) was used for the synthesis of a N-acetylglucosaminyl peptide and a pseudoglycopeptide by solid-phase peptide synthesis without the requirement of protecting groups on the carbohydrate. We also performed transglycosylation of an N-glycan to the N-acetylglucosaminyl peptide using endo-β-N-acetylglucosaminidase from Mucor hiemalis (Endo-M) to synthesize a glycopeptide...
3 CitationsSource
#1Yuta Sugiyama (Ishikawa Prefectural University)H-Index: 8
#2Toshihiko Katoh (Ishikawa Prefectural University)H-Index: 10
Last. Takane Katayama (Ishikawa Prefectural University)H-Index: 34
view all 8 authors...
We have recently generated a highly efficient 1,2-α-l-fucosynthase (BbAfcA N423H mutant) by protein engineering of 1,2-α-l-fucosidase from Bifidobacterium bifidum JCM 1254. This synthase could specifically introduce H-antigens (Fucα1-2Gal) into the non-reducing ends of oligosaccharides and in O-linked glycans in mucin glycoprotein. In the present study, we show an extended application of the engineered 1,2-α-l-fucosynthase by demonstrating its ability to insert Fuc residues into N- and O-glycans...
9 CitationsSource
#1Kouta Sakaguchi (Ishikawa Prefectural University)H-Index: 2
#2Toshihiko Katoh (Ishikawa Prefectural University)H-Index: 10
Last. Kenji Yamamoto (Ishikawa Prefectural University)H-Index: 57
view all 3 authors...
Glycan conversion of glycoprotein via the transglycosylation activity of endo-β-N-acetylglucosaminidase is a promising chemoenzymatic technology for the production of glycoproteins including bio-medicines with a homogeneous glycoform. Although Endo-M is a key enzyme in this process, its product undergoes rehydrolysis, which leads to a lower yield, and limits the practical application of this enzyme. We developed several Endo-M mutant enzymes including N175Q with glycosynthase-like activity and/o...
5 CitationsSource
#1Ryuichi Ishida (Ishikawa Prefectural University)H-Index: 1
#2Kouta Sakaguchi (Ishikawa Prefectural University)H-Index: 2
Last. Keiko HisaH-Index: 5
view all 7 authors...
Objectives A levansucrase from Leuconostoc mesenteroides NTM048 was cloned and expressed and its enzymatic product was characterized.
9 CitationsSource
#1Chiaki Matsuzaki (Ishikawa Prefectural University)H-Index: 8
#2Kenji Matsumoto (Ishikawa Prefectural University)H-Index: 3
Last. Keiko HisaH-Index: 5
view all 5 authors...
The effects of Leuconostoc mesenteroides strain NTM048 and type strain JCM6124T on the murine immune system were characterized. Although the bacterial cells and exopolysaccharides of each strain induced immunoglobulin A production in Peyer’s patch cells, the effects of NTM048 were more potent than those of JCM6124T. Oral administration of the cells of each strain increased the fecal immunoglobulin A content in NTM048-treated mice, but not in JCM6124T-treated mice. A flow cytometric analysis show...
3 CitationsSource
Leuconostoc mesenteroides strain NTM048 has been shown to have intestinal IgA-inducing ability. In this study, we investigated the immunostimulant potency of an exopolysaccharide secreted from strain NTM048 (NTM048 EPS) in vitro and in vivo in a murine model. NTM048 EPS ranges in size from 10 to 40 kDa and is speculated to be mainly composed of glucose and fructose. The in vitro study revealed that NTM048 EPS induced total and antigen-specific IgA production by Peyer′s patch cells and influenced...
33 CitationsSource
#1Aina Gotoh (Ishikawa Prefectural University)H-Index: 10
#2Toshihiko Katoh (Ishikawa Prefectural University)H-Index: 10
Last. Takane Katayama (Kyoto University)H-Index: 34
view all 11 authors...
Abstract We describe the novel substrate specificities of two independently evolved lacto-N-biosidases (LnbX and LnbB) towards the sugar chains of globo- and ganglio-series glycosphingolipids. LnbX, a non-classified member of the glycoside hydrolase family, isolated from Bifidobacterium longum subsp. longum , was shown to liberate galacto-N-biose (GNB: Galβ1-3GalNAc) and 2′-fucosyl GNB (a type-4 trisaccharide) from Gb5 pentasaccharide and globo H hexasaccharide, respectively. LnbB, a member of t...
10 CitationsSource