Found 9 structures.
Displayed structures from 1 to 9
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1. Compound ID: 53
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-D-Gal |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_151528,IEDB_151531,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_190606,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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2. Compound ID: 832
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-D-GlcNAc |
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Structure type: oligomer
Trivial name: antigen type I
Contained glycoepitopes: IEDB_130646,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_150939,IEDB_151531,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158548,IEDB_158550,IEDB_190606,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 230
Feizi T "Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium" -
Glycoconjugate Journal 17(7-9) (2000) 553-565
The closing years of the second millennium have been uplifting for carbohydrate biology. Optimism that oligosaccharide sequences are bearers of crucial biological information has been borne out by the constellation of efforts of carbohydrate chemists, biochemists, immunochemists, and cell- and molecular biologists. The direct involvement of specific oligosaccharide sequences in protein targeting and folding, and in mechanisms of infection, inflammation and immunity is now unquestioned. With the emergence of families of proteins with carbohydrate-binding activities, assignments of information content for defined oligosaccharide sequences will become more common, but the pinpointing and elucidation of the bioactive domains on oligosaccharides will continue to pose challenges even to the most experienced carbohydrate biologists. The neoglycolipid technology incorporates some of the key requirements for this challenge: namely the resolution of complex glycan mixtures, and ligand binding coupled with sequence determination by mass spectrometry.
monoclonal antibodies, mass spectrometry, blood group antigen, carbohydrate ligands, differentiation antigens, embryonic development, galectins, inflammation, leukocyte adhesion, neoglycolipids, oligosaccharide ligands, oligosaccharid probes, selectins
NCBI PubMed ID: 11421348Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: t.feizi@ic.ac.uk
Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
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3. Compound ID: 15178
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+
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{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=6/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ {{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=3/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=7/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/Asn-X-Ser/Thr/ |
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Structure type: structural motif or average structure
Aglycon: Asn-X-Ser/Thr
Trivial name: poly-LacNAc-containing N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158550,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5913
Damerow M, Graalfs F, Guther MLS, Mehlert A, Izquierdo L, Ferguson MA "A Gene of the beta3-Glycosyltransferase Family Encodes N-Acetylglucosaminyltransferase II Function in Trypanosoma brucei" -
Journal of Biological Chemistry 291(26) (2016) 13834-13845
The bloodstream form of the human pathogen Trypanosoma brucei expresses oligomannose, paucimannose, and complex N-linked glycans, including some exceptionally large poly-N-acetyllactosamine-containing structures. Despite the presence of complex N-glycans in this organism, no homologues of the canonical N-acetylglucosaminyltransferase I or II genes can be found in the T. brucei genome. These genes encode the activities that initiate the elaboration of the Manα1-3 and Manα1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Previously, we identified a highly divergent T. brucei N-acetylglucosaminyltransferase I (TbGnTI) among a set of putative T. brucei glycosyltransferase genes belonging to the β3-glycosyltransferase superfamily (Damerow, M., Rodrigues, J. A., Wu, D., Güther, M. L., Mehlert, A., and Ferguson, M. A. (2014) J. Biol. Chem. 289, 9328-9339). Here, we demonstrate that TbGT15, another member of the same β3-glycosyltransferase family, encodes an equally divergent N-acetylglucosaminyltransferase II (TbGnTII) activity. In contrast to multicellular organisms, where GnTII activity is essential, TbGnTII null mutants of T. brucei grow in culture and are still infectious to animals. Characterization of the large poly-N-acetyllactosamine containing N-glycans of the TbGnTII null mutants by methylation linkage analysis suggests that, in wild-type parasites, the Manα1-6 arm of the conserved trimannosyl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manα1-3 arm may carry predominantly branched poly-N-acetyllactosamine chains. These results provide further detail on the structure and biosynthesis of complex N-glycans in an important human pathogen and provide a second example of the adaptation by trypanosomes of β3-glycosyltransferase family members to catalyze β1-2 glycosidic linkages.
glycosyltransferase, N-acetylglucosamine, glycobiology, Parasite, Trypanosoma brucei, post-translational modification (PTM)
NCBI PubMed ID: 27189951Publication DOI: 10.1074/jbc.M116.733246Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: From the Division of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Methods: methylation, GC-MS, DNA techniques, glycosyltransferase assays, ESI-MS, Western blotting, composition analysis, genetic methods, Southern blotting, RT-PCR, HPTLC, LC-MS, NaBD4 reduction, lectin blotting, RNA extraction, SEM
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4. Compound ID: 15179
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ {{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=3/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+ | a-D-Manp-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=4/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/Asn-X-Ser/Thr/ |
Show graphically |
Structure type: structural motif or average structure
Aglycon: Asn-X-Ser/Thr
Trivial name: poly-LacNAc-containing N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158550,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5913
Damerow M, Graalfs F, Guther MLS, Mehlert A, Izquierdo L, Ferguson MA "A Gene of the beta3-Glycosyltransferase Family Encodes N-Acetylglucosaminyltransferase II Function in Trypanosoma brucei" -
Journal of Biological Chemistry 291(26) (2016) 13834-13845
The bloodstream form of the human pathogen Trypanosoma brucei expresses oligomannose, paucimannose, and complex N-linked glycans, including some exceptionally large poly-N-acetyllactosamine-containing structures. Despite the presence of complex N-glycans in this organism, no homologues of the canonical N-acetylglucosaminyltransferase I or II genes can be found in the T. brucei genome. These genes encode the activities that initiate the elaboration of the Manα1-3 and Manα1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Previously, we identified a highly divergent T. brucei N-acetylglucosaminyltransferase I (TbGnTI) among a set of putative T. brucei glycosyltransferase genes belonging to the β3-glycosyltransferase superfamily (Damerow, M., Rodrigues, J. A., Wu, D., Güther, M. L., Mehlert, A., and Ferguson, M. A. (2014) J. Biol. Chem. 289, 9328-9339). Here, we demonstrate that TbGT15, another member of the same β3-glycosyltransferase family, encodes an equally divergent N-acetylglucosaminyltransferase II (TbGnTII) activity. In contrast to multicellular organisms, where GnTII activity is essential, TbGnTII null mutants of T. brucei grow in culture and are still infectious to animals. Characterization of the large poly-N-acetyllactosamine containing N-glycans of the TbGnTII null mutants by methylation linkage analysis suggests that, in wild-type parasites, the Manα1-6 arm of the conserved trimannosyl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manα1-3 arm may carry predominantly branched poly-N-acetyllactosamine chains. These results provide further detail on the structure and biosynthesis of complex N-glycans in an important human pathogen and provide a second example of the adaptation by trypanosomes of β3-glycosyltransferase family members to catalyze β1-2 glycosidic linkages.
glycosyltransferase, N-acetylglucosamine, glycobiology, Parasite, Trypanosoma brucei, post-translational modification (PTM)
NCBI PubMed ID: 27189951Publication DOI: 10.1074/jbc.M116.733246Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: From the Division of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Methods: methylation, GC-MS, DNA techniques, glycosyltransferase assays, ESI-MS, Western blotting, composition analysis, genetic methods, Southern blotting, RT-PCR, HPTLC, LC-MS, NaBD4 reduction, lectin blotting, RNA extraction, SEM
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5. Compound ID: 15202
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{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=2/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/-Asn-XSer/Thr-/ |
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Structure type: structural motif or average structure
Aglycon: -Asn-XSer/Thr-
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5919
Duncan SM, Nagar R, Damerow M, Yashunsky DV, Bruzzi B, Nikolaev AV, Ferguson MAJ "A Trypanosoma brucei β3 glycosyltransferase superfamily gene encodes a β1-6 GlcNAc-transferase mediating N-glycan and GPI anchor modification" -
Journal of Biological Chemistry 294(4) (2021) 101153
The parasite Trypanosoma brucei exists in both a bloodstream form (BSF) and a procyclic form (PCF), which exhibit large carbohydrate extensions on the N-linked glycans and glycosylphosphatidylinositol (GPI) anchors, respectively. The parasite's glycoconjugate repertoire suggests at least 38 glycosyltransferase (GT) activities, 16 of which are currently uncharacterized. Here, we probe the function(s) of the uncharacterized GT67 glycosyltransferase family and a β3 glycosyltransferase (β3GT) superfamily gene, TbGT10. A BSF-null mutant, created by applying the diCre/loxP method in T. brucei for the first time, showed a fitness cost but was viable in vitro and in vivo and could differentiate into the PCF, demonstrating nonessentiality of TbGT10. The absence of TbGT10 impaired the elaboration of N-glycans and GPI anchor side chains in BSF and PCF parasites, respectively. Glycosylation defects included reduced BSF glycoprotein binding to the lectin ricin and monoclonal antibodies mAb139 and mAbCB1. The latter bind a carbohydrate epitope present on lysosomal glycoprotein p67 that we show here consists of (-6Galβ1-4GlcNAcβ1-)≥4 poly-N-acetyllactosamine repeats. Methylation linkage analysis of Pronase-digested glycopeptides isolated from BSF wild-type and TbGT10 null parasites showed a reduction in 6-O-substituted- and 3,6-di-O-substituted-Gal residues. These data define TbGT10 as a UDP-GlcNAc:βGal β1-6 GlcNAc-transferase. The dual role of TbGT10 in BSF N-glycan and PCF GPI-glycan elaboration is notable, and the β1-6 specificity of a β3GT superfamily gene product is unprecedented. The similar activities of trypanosome TbGT10 and higher-eukaryote I-branching enzyme (EC 2.4.1.150), which belong to glycosyltransferase families GT67 and GT14, respectively, in elaborating N-linked glycans, are a novel example of convergent evolution.
N-acetylglucosaminyltransferase, Glycosylphosphatidylinositol, N-glycosylation, GPI, N-glycan, Trypanosoma brucei glycosyltransferase
NCBI PubMed ID: 34478712Publication DOI: 10.1016/j.jbc.2021.101153Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom
Methods: methylation, PCR, GC-MS, DNA techniques, Western blotting, genetic methods, enzymatic digestion, conjugation, lectin blotting, biolayer interferometry (BLI) measurements
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6. Compound ID: 15208
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+ |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/-Asn-XSer/Thr-/ |
Show graphically |
Structure type: structural motif or average structure
Aglycon: -Asn-XSer/Thr-
Trivial name: VSG, variant surface glycoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5919
Duncan SM, Nagar R, Damerow M, Yashunsky DV, Bruzzi B, Nikolaev AV, Ferguson MAJ "A Trypanosoma brucei β3 glycosyltransferase superfamily gene encodes a β1-6 GlcNAc-transferase mediating N-glycan and GPI anchor modification" -
Journal of Biological Chemistry 294(4) (2021) 101153
The parasite Trypanosoma brucei exists in both a bloodstream form (BSF) and a procyclic form (PCF), which exhibit large carbohydrate extensions on the N-linked glycans and glycosylphosphatidylinositol (GPI) anchors, respectively. The parasite's glycoconjugate repertoire suggests at least 38 glycosyltransferase (GT) activities, 16 of which are currently uncharacterized. Here, we probe the function(s) of the uncharacterized GT67 glycosyltransferase family and a β3 glycosyltransferase (β3GT) superfamily gene, TbGT10. A BSF-null mutant, created by applying the diCre/loxP method in T. brucei for the first time, showed a fitness cost but was viable in vitro and in vivo and could differentiate into the PCF, demonstrating nonessentiality of TbGT10. The absence of TbGT10 impaired the elaboration of N-glycans and GPI anchor side chains in BSF and PCF parasites, respectively. Glycosylation defects included reduced BSF glycoprotein binding to the lectin ricin and monoclonal antibodies mAb139 and mAbCB1. The latter bind a carbohydrate epitope present on lysosomal glycoprotein p67 that we show here consists of (-6Galβ1-4GlcNAcβ1-)≥4 poly-N-acetyllactosamine repeats. Methylation linkage analysis of Pronase-digested glycopeptides isolated from BSF wild-type and TbGT10 null parasites showed a reduction in 6-O-substituted- and 3,6-di-O-substituted-Gal residues. These data define TbGT10 as a UDP-GlcNAc:βGal β1-6 GlcNAc-transferase. The dual role of TbGT10 in BSF N-glycan and PCF GPI-glycan elaboration is notable, and the β1-6 specificity of a β3GT superfamily gene product is unprecedented. The similar activities of trypanosome TbGT10 and higher-eukaryote I-branching enzyme (EC 2.4.1.150), which belong to glycosyltransferase families GT67 and GT14, respectively, in elaborating N-linked glycans, are a novel example of convergent evolution.
N-acetylglucosaminyltransferase, Glycosylphosphatidylinositol, N-glycosylation, GPI, N-glycan, Trypanosoma brucei glycosyltransferase
NCBI PubMed ID: 34478712Publication DOI: 10.1016/j.jbc.2021.101153Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom
Methods: methylation, PCR, GC-MS, DNA techniques, Western blotting, genetic methods, enzymatic digestion, conjugation, lectin blotting, biolayer interferometry (BLI) measurements
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7. Compound ID: 15213
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ b-D-GlcpNAc-(1-3)-+ a-D-Manp-(1-2)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-3)-a-D-Galp-(1-3)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-myoIno-(?--/-Asn-XSer/Thr-/ |
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Structure type: structural motif or average structure
Aglycon: -Asn-XSer/Thr-
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_150939,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_190606,IEDB_983930,SB_136,SB_165,SB_166,SB_173,SB_187,SB_191,SB_195,SB_196,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 5919
Duncan SM, Nagar R, Damerow M, Yashunsky DV, Bruzzi B, Nikolaev AV, Ferguson MAJ "A Trypanosoma brucei β3 glycosyltransferase superfamily gene encodes a β1-6 GlcNAc-transferase mediating N-glycan and GPI anchor modification" -
Journal of Biological Chemistry 294(4) (2021) 101153
The parasite Trypanosoma brucei exists in both a bloodstream form (BSF) and a procyclic form (PCF), which exhibit large carbohydrate extensions on the N-linked glycans and glycosylphosphatidylinositol (GPI) anchors, respectively. The parasite's glycoconjugate repertoire suggests at least 38 glycosyltransferase (GT) activities, 16 of which are currently uncharacterized. Here, we probe the function(s) of the uncharacterized GT67 glycosyltransferase family and a β3 glycosyltransferase (β3GT) superfamily gene, TbGT10. A BSF-null mutant, created by applying the diCre/loxP method in T. brucei for the first time, showed a fitness cost but was viable in vitro and in vivo and could differentiate into the PCF, demonstrating nonessentiality of TbGT10. The absence of TbGT10 impaired the elaboration of N-glycans and GPI anchor side chains in BSF and PCF parasites, respectively. Glycosylation defects included reduced BSF glycoprotein binding to the lectin ricin and monoclonal antibodies mAb139 and mAbCB1. The latter bind a carbohydrate epitope present on lysosomal glycoprotein p67 that we show here consists of (-6Galβ1-4GlcNAcβ1-)≥4 poly-N-acetyllactosamine repeats. Methylation linkage analysis of Pronase-digested glycopeptides isolated from BSF wild-type and TbGT10 null parasites showed a reduction in 6-O-substituted- and 3,6-di-O-substituted-Gal residues. These data define TbGT10 as a UDP-GlcNAc:βGal β1-6 GlcNAc-transferase. The dual role of TbGT10 in BSF N-glycan and PCF GPI-glycan elaboration is notable, and the β1-6 specificity of a β3GT superfamily gene product is unprecedented. The similar activities of trypanosome TbGT10 and higher-eukaryote I-branching enzyme (EC 2.4.1.150), which belong to glycosyltransferase families GT67 and GT14, respectively, in elaborating N-linked glycans, are a novel example of convergent evolution.
N-acetylglucosaminyltransferase, Glycosylphosphatidylinositol, N-glycosylation, GPI, N-glycan, Trypanosoma brucei glycosyltransferase
NCBI PubMed ID: 34478712Publication DOI: 10.1016/j.jbc.2021.101153Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom
Methods: methylation, PCR, GC-MS, DNA techniques, Western blotting, genetic methods, enzymatic digestion, conjugation, lectin blotting, biolayer interferometry (BLI) measurements
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8. Compound ID: 15304
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ | |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc |
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Structure type: oligomer
Trivial name: VSG complex N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158548,IEDB_158550,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5943
Heng J, Naderer T, Ralph SA, McConville MJ "Glycosylated compounds of parasitic protozoa" -
Book: Microbial Glycobiology (series: Structures, Relevance and Applications) (2010) 203-231
This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.
O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation
Publication DOI: 10.1016/B978-0-12-374546-0.00012-2Publisher: Amsterdam: Elsevier
Correspondence: malcolmm@unimelb.edu.au
Editors: Moran A
Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
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9. Compound ID: 15305
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/Variants 0/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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/Variants 1/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc
/Variants 0/ is:
a-D-Galp-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-
OR (exclusively)
a-D-Galp-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-
/Variants 1/ is:
a-D-Galp-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-
OR (exclusively)
a-D-Galp-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)- |
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Structure type: oligomer
Trivial name: VSG complex N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_115013,IEDB_123886,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_146694,IEDB_149558,IEDB_150939,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_190606,IEDB_418918,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_689191,IEDB_918314,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_40,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_87,SB_88
The structure is contained in the following publication(s):
- Article ID: 5943
Heng J, Naderer T, Ralph SA, McConville MJ "Glycosylated compounds of parasitic protozoa" -
Book: Microbial Glycobiology (series: Structures, Relevance and Applications) (2010) 203-231
This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.
O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation
Publication DOI: 10.1016/B978-0-12-374546-0.00012-2Publisher: Amsterdam: Elsevier
Correspondence: malcolmm@unimelb.edu.au
Editors: Moran A
Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
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Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
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