Found 17 structures.
Displayed structures from 1 to 15
Next 15 structure(s)
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1. Compound ID: 26946
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a-Fucp-(1-4)-+
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b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-6)-+
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a-Fucp-(1-4)-+ | a-Fucp-(1-3)-+
| | |
b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-3)-b-Manp-(1-4)-b-GlcpNAc-(1-4)-GlcpNAc
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b-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_241116,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10774
Fitchette-Laine AC, Gomord V, Cabanes M, Michalski JC, Foucher B, Cavelier B, Hawes C, Lerouge P, Faye L "N-glycans harboring the Lewis a epitope are expressed at the surface of plant cells" -
Plant Journal: for Cell and Molecular Biology 12(6) (1997) 1411-1417
In plants, N-linked glycans are processed in the Golgi apparatus to complex-type N-glycans of limited size containing a β(1,2)-xylose and/or an α(1,3)-fucose residue. Larger mono-and bi-antennary N-linked complex glycans have not often been described. This study has re-examined the structure of such plant N-linked glycans, and, through both immunological and structural data, it is shown that the antennae are composed of Lewis a (Le(a)) antigens, comprising the carbohydrate sequence Gal β 1-3[Fuc α 1-4]GlcNAc. Furthermore, a fucosyltransferase activity involved in the biosynthesis of this antigen was detected in sycamore cells. This is the first characterization in plants of a Lewis antigen that is usually found on cell-surface glycoconjugates in mammals and involved in recognition and adhesion processes. Le(a)-containing N-linked glycans are widely distributed in plants and highly expressed at the cell surface, which may suggest a putative function in cell/cell communication.
NCBI PubMed ID: 9450345Publication DOI: 10.1046/j.1365-313x.1997.12061411.xJournal NLM ID: 9207397Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
Correspondence: lfaye@crihan.fr
Institutions: Laboratoire des Transports Intracellulaires, ESA-CNRS 6037, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France
Methods: methylation, GLC-MS, SDS-PAGE, glycosyltransferase assays, ELISA, ESI-MS, immunoblotting
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2. Compound ID: 27009
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a-Fucp-(1-4)-+ b-Xylp-(1-2)-+ a-Fucp-(1-3)-+
| | |
b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-3)-b-Manp-(1-4)-b-GlcpNAc-(1-4)-b-GlcpNAc
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a-Manp-(1-6)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10794
Melo NS, Nimtz M, Conradt HS, Fevereiro PS, Costa J "Identification of the human Lewis(a) carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)" -
FEBS Letters 415(2) (1997) 186-191
This paper reports for the first time the presence of the human Lewis(a) type determinant in glycoproteins secreted by plant cells. A single glycopeptide was identified in the tryptic hydrolysis of the peroxidase VMPxC1 from Vaccinium myrtillus L. by HPLC/ESI-MS. The oligosaccharide structures were elucidated by ESI-MS-MS and by methylation analysis before and after removal of fucose by mild acid hydrolysis. The major structure determined is of the biantennary plant complex type containing the outer chain motif Lewis(a) [structure in text]. A corresponding fucosyltransferase activity catalyzing the formation of Lewis(a) type structures in vitro was identified in cellular extracts of the suspension culture
Extracellular glycoprotein, Lewisa, Peroxidase, Plant complex oligosaccharide, Vaccinium myrtillus
NCBI PubMed ID: 9350993Publication DOI: 10.1016/S0014-5793(97)01121-6Journal NLM ID: 0155157Publisher: Elsevier
Correspondence: jcosta@itqb.unl.pt
Institutions: ITQBIIBET, Apartado 12, P-2780 Oeiras, Portugal
Methods: methylation, SDS-PAGE, glycosyltransferase assays, ESI-MS, MALDI-TOF MS, HPLC, enzymatic digestion, hydrazinolysis
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3. Compound ID: 27010
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b-GlcpNAc-(1-2)-a-Manp-(1-6)-+
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a-Fucp-(1-4)-+ | a-Fucp-(1-3)-+
| | |
b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-3)-b-Manp-(1-4)-b-GlcpNAc-(1-4)-b-GlcpNAc
|
b-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10794
Melo NS, Nimtz M, Conradt HS, Fevereiro PS, Costa J "Identification of the human Lewis(a) carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)" -
FEBS Letters 415(2) (1997) 186-191
This paper reports for the first time the presence of the human Lewis(a) type determinant in glycoproteins secreted by plant cells. A single glycopeptide was identified in the tryptic hydrolysis of the peroxidase VMPxC1 from Vaccinium myrtillus L. by HPLC/ESI-MS. The oligosaccharide structures were elucidated by ESI-MS-MS and by methylation analysis before and after removal of fucose by mild acid hydrolysis. The major structure determined is of the biantennary plant complex type containing the outer chain motif Lewis(a) [structure in text]. A corresponding fucosyltransferase activity catalyzing the formation of Lewis(a) type structures in vitro was identified in cellular extracts of the suspension culture
Extracellular glycoprotein, Lewisa, Peroxidase, Plant complex oligosaccharide, Vaccinium myrtillus
NCBI PubMed ID: 9350993Publication DOI: 10.1016/S0014-5793(97)01121-6Journal NLM ID: 0155157Publisher: Elsevier
Correspondence: jcosta@itqb.unl.pt
Institutions: ITQBIIBET, Apartado 12, P-2780 Oeiras, Portugal
Methods: methylation, SDS-PAGE, glycosyltransferase assays, ESI-MS, MALDI-TOF MS, HPLC, enzymatic digestion, hydrazinolysis
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4. Compound ID: 27011
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b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-6)-+
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a-Fucp-(1-4)-+ | a-Fucp-(1-3)-+
| | |
b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-3)-b-Manp-(1-4)-b-GlcpNAc-(1-4)-b-GlcpNAc
|
b-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10794
Melo NS, Nimtz M, Conradt HS, Fevereiro PS, Costa J "Identification of the human Lewis(a) carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)" -
FEBS Letters 415(2) (1997) 186-191
This paper reports for the first time the presence of the human Lewis(a) type determinant in glycoproteins secreted by plant cells. A single glycopeptide was identified in the tryptic hydrolysis of the peroxidase VMPxC1 from Vaccinium myrtillus L. by HPLC/ESI-MS. The oligosaccharide structures were elucidated by ESI-MS-MS and by methylation analysis before and after removal of fucose by mild acid hydrolysis. The major structure determined is of the biantennary plant complex type containing the outer chain motif Lewis(a) [structure in text]. A corresponding fucosyltransferase activity catalyzing the formation of Lewis(a) type structures in vitro was identified in cellular extracts of the suspension culture
Extracellular glycoprotein, Lewisa, Peroxidase, Plant complex oligosaccharide, Vaccinium myrtillus
NCBI PubMed ID: 9350993Publication DOI: 10.1016/S0014-5793(97)01121-6Journal NLM ID: 0155157Publisher: Elsevier
Correspondence: jcosta@itqb.unl.pt
Institutions: ITQBIIBET, Apartado 12, P-2780 Oeiras, Portugal
Methods: methylation, SDS-PAGE, glycosyltransferase assays, ESI-MS, MALDI-TOF MS, HPLC, enzymatic digestion, hydrazinolysis
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5. Compound ID: 27012
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a-Fucp-(1-4)-+
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b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-6)-+
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a-Fucp-(1-4)-+ | a-Fucp-(1-3)-+
| | |
b-Galp-(1-3)-b-GlcpNAc-(1-2)-a-Manp-(1-3)-b-Manp-(1-4)-b-GlcpNAc-(1-4)-b-GlcpNAc
|
b-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_241116,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10794
Melo NS, Nimtz M, Conradt HS, Fevereiro PS, Costa J "Identification of the human Lewis(a) carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)" -
FEBS Letters 415(2) (1997) 186-191
This paper reports for the first time the presence of the human Lewis(a) type determinant in glycoproteins secreted by plant cells. A single glycopeptide was identified in the tryptic hydrolysis of the peroxidase VMPxC1 from Vaccinium myrtillus L. by HPLC/ESI-MS. The oligosaccharide structures were elucidated by ESI-MS-MS and by methylation analysis before and after removal of fucose by mild acid hydrolysis. The major structure determined is of the biantennary plant complex type containing the outer chain motif Lewis(a) [structure in text]. A corresponding fucosyltransferase activity catalyzing the formation of Lewis(a) type structures in vitro was identified in cellular extracts of the suspension culture
Extracellular glycoprotein, Lewisa, Peroxidase, Plant complex oligosaccharide, Vaccinium myrtillus
NCBI PubMed ID: 9350993Publication DOI: 10.1016/S0014-5793(97)01121-6Journal NLM ID: 0155157Publisher: Elsevier
Correspondence: jcosta@itqb.unl.pt
Institutions: ITQBIIBET, Apartado 12, P-2780 Oeiras, Portugal
Methods: methylation, SDS-PAGE, glycosyltransferase assays, ESI-MS, MALDI-TOF MS, HPLC, enzymatic digestion, hydrazinolysis
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6. Compound ID: 27735
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a-Fuc-(1-4)-+
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b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-Manp-(1-6)-+
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a-Fuc-(1-4)-+ | a-Fuc-(1-3)-+
| | |
b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-Manp-(1-3)-b-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn
|
b-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Trivial name: (FA)(FA)XF
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_44,SB_67,SB_7,SB_72,SB_73,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10946
Strasser R, Bondili JS, Vavra U, Schoberer J, Svoboda B, Glössl J, Léonard R, Stadlmann J, Altmann F, Steinkellner H, Mach L "A unique β1,3-galactosyltransferase is indispensable for the biosynthesis of N-glycans containing Lewis a structures in Arabidopsis thaliana" -
Plant Cell 19 (2007) 2278-2292
In plants, the only known outer-chain elongation of complex N-glycans is the formation of Lewis a [Fucα1-4(Galβ1-3)GlcNAc-R] structures. This process involves the sequential attachment of β1,3-galactose and α1,4-fucose residues by β1,3-galactosyltransferase and α1,4-fucosyltransferase. However, the exact mechanism underlying the formation of Lewis a epitopes in plants is poorly understood, largely because one of the involved enzymes, β1,3-galactosyltransferase, has not yet been identified and characterized. Here, we report the identification of an Arabidopsis thaliana β1,3-galactosyltransferase involved in the biosynthesis of the Lewis a epitope using an expression cloning strategy. Overexpression of various candidates led to the identification of a single gene (named GALACTOSYLTRANSFERASE1 [GALT1]) that increased the originally very low Lewis a epitope levels in planta. Recombinant GALT1 protein produced in insect cells was capable of transferring β1,3-linked galactose residues to various N-glycan acceptor substrates, and subsequent treatment of the reaction products with α1,4-fucosyltransferase resulted in the generation of Lewis a structures. Furthermore, transgenic Arabidopsis plants lacking a functional GALT1 mRNA did not show any detectable amounts of Lewis a epitopes on endogenous glycoproteins. Taken together, our results demonstrate that GALT1 is both sufficient and essential for the addition of β1,3-linked galactose residues to N-glycans and thus is required for the biosynthesis of Lewis a structures in Arabidopsis. Moreover, cell biological characterization of a transiently expressed GALT1-fluorescent protein fusion using confocal laser scanning microscopy revealed the exclusive location of GALT1 within the Golgi apparatus, which is in good agreement with the proposed physiological action of the enzyme.
Publication DOI: 10.1105/tpc.107.052985Journal NLM ID: 9208688Publisher: Rockville, MD: American Society of Plant Physiologists
Correspondence: richard.strasser@boku.ac.at
Institutions: Institute of Applied Genetics and Cell Biology, BOKU, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria, Department of Chemistry, BOKU, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria
Methods: biological assays, enzymatic digestion, LC-MS, enzymatic assay, genetic manipulations
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7. Compound ID: 27736
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/Variants 0/-a-Manp-(1-6)-+ a-Fuc-(1-3)-+
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/Variants 1/-a-Manp-(1-3)-b-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn
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b-Xylp-(1-2)-+
/Variants 0/ is:
a-Fuc-(1-4)-+
|
b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-
OR (exclusively)
b-D-GlcpNAc-(1-2)-
/Variants 1/ is:
b-D-GlcpNAc-(1-2)-
OR (exclusively)
a-Fuc-(1-4)-+
|
b-Galp-(1-3)-b-D-GlcpNAc-(1-2)- |
Show graphically |
Structure type: oligomer
Trivial name: (FA)GnXF/Gn(FA)XF
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_1394182,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_44,SB_67,SB_7,SB_72,SB_73,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10946
Strasser R, Bondili JS, Vavra U, Schoberer J, Svoboda B, Glössl J, Léonard R, Stadlmann J, Altmann F, Steinkellner H, Mach L "A unique β1,3-galactosyltransferase is indispensable for the biosynthesis of N-glycans containing Lewis a structures in Arabidopsis thaliana" -
Plant Cell 19 (2007) 2278-2292
In plants, the only known outer-chain elongation of complex N-glycans is the formation of Lewis a [Fucα1-4(Galβ1-3)GlcNAc-R] structures. This process involves the sequential attachment of β1,3-galactose and α1,4-fucose residues by β1,3-galactosyltransferase and α1,4-fucosyltransferase. However, the exact mechanism underlying the formation of Lewis a epitopes in plants is poorly understood, largely because one of the involved enzymes, β1,3-galactosyltransferase, has not yet been identified and characterized. Here, we report the identification of an Arabidopsis thaliana β1,3-galactosyltransferase involved in the biosynthesis of the Lewis a epitope using an expression cloning strategy. Overexpression of various candidates led to the identification of a single gene (named GALACTOSYLTRANSFERASE1 [GALT1]) that increased the originally very low Lewis a epitope levels in planta. Recombinant GALT1 protein produced in insect cells was capable of transferring β1,3-linked galactose residues to various N-glycan acceptor substrates, and subsequent treatment of the reaction products with α1,4-fucosyltransferase resulted in the generation of Lewis a structures. Furthermore, transgenic Arabidopsis plants lacking a functional GALT1 mRNA did not show any detectable amounts of Lewis a epitopes on endogenous glycoproteins. Taken together, our results demonstrate that GALT1 is both sufficient and essential for the addition of β1,3-linked galactose residues to N-glycans and thus is required for the biosynthesis of Lewis a structures in Arabidopsis. Moreover, cell biological characterization of a transiently expressed GALT1-fluorescent protein fusion using confocal laser scanning microscopy revealed the exclusive location of GALT1 within the Golgi apparatus, which is in good agreement with the proposed physiological action of the enzyme.
Publication DOI: 10.1105/tpc.107.052985Journal NLM ID: 9208688Publisher: Rockville, MD: American Society of Plant Physiologists
Correspondence: richard.strasser@boku.ac.at
Institutions: Institute of Applied Genetics and Cell Biology, BOKU, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria, Department of Chemistry, BOKU, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria
Methods: biological assays, enzymatic digestion, LC-MS, enzymatic assay, genetic manipulations
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8. Compound ID: 27880
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a-Fucp-(1-4)-+
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b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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b-Fucp-(1-4)-+ | a-Fuc-(1-3)-+
| | |
b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (protein)/
|
a-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Aglycon: (->4) Asn-X-Ser/Thr (protein)
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_123886,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10996
Rayon C, Lerouge P, Faye L "The protein N-glycosylation in plants" -
Journal of Experimental Botany 49(326) (1998) 1463–1472
In plants, most proteins of the extracellular compartment and the endomembrane system are glycosylated by N-linked oligosaccharides. The N-glycosylation of proteins has a great impact both on their physicochemical properties and on their biological functions. Over the last ten years, a number of laboratories have contributed considerably to the understanding of the structure, the biosynthesis and the function of plant N-linked glycans. In this review, data on this domain will be summarized and the recent results on the N-glycosylation of a vacuolar lectin, the bean phytohaemagglutinin (PHA) will also be included. This PHA, used as a model glycoprotein, was expressed in different plant systems and the N-glycosylation patterns of different recombinant PHA were compared. In addition to this study on plant-specific glycosylation, the same model glycoprotein was used to investigate whether or not N-glycosylation and N-glycan maturation is organ-specific in plants.
N-Linked oligosaccharide, biosynthesis and function, phytohaemagglutinin
Publication DOI: 10.1093/jxb/49.326.1463Journal NLM ID: 9882906Publisher: Oxford University Press
Correspondence: Faye L
Institutions: Laboratoire des Transports Intracellulaires, Université de Rouen, Mont Saint Aignan, France
Methods: NMR, column chromatography, PNGase A treatment, HPAED-PAD
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9. Compound ID: 27883
|
a-Fucp-(1-4)-+
|
b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
b-Fucp-(1-4)-+ | ?%a-Fuc-(1-3)-+
| | |
b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (protein)/
|
?%a-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Aglycon: (->4) Asn-X-Ser/Thr (protein)
Trivial name: Lewis (Le^a) antigens
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_123886,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10997
Lerouge P, Rayon C, Gomord V, Faye L "N-glycoprotein biosynthesis in plants: recent developments and future trends" -
Plant Molecular Biology 38(1-2) (1998) 31-48
N-glycosylation is a major modification of proteins in plant cells. This process starts in the endoplasmic reticulum by the co-translational transfer of a precursor oligosaccharide to specific asparagine residues of the nascent polypeptide chain. Processing of this oligosaccharide into high-mannose-type, paucimannosidic-type, hybrid-type or complex-type N-glycans occurs in the secretory pathway as the glycoprotein moves from the endoplasmic reticulum to its final destination. At the end of their maturation, some plant N-glycans have typical structures that differ from those found in their mammalian counterpart by the absence of sialic acid and the presence of beta(1,2)-xylose and alpha(1,3)-fucose residues. Glycosidases and glycosyltransferases that respectively catalyse the stepwise trimming and addition of sugar residues are generally considered as working in a co-ordinated and highly ordered fashion to form mature N-glycans. On the basis of this assembly line concept, fast progress is currently made by using N-linked glycan structures as milestones of the intracellular transport of proteins along the plant secretory pathway. Further developments of this approach will need to more precisely define the topological distribution of glycosyltransferases within a plant Golgi stack. In contrast with their acknowledged role in the targeting of lysosomal hydrolases in mammalian cells, N-glycans have no specific function in the transport of glycoproteins into the plant vacuole. However, the presence of N-glycans, regardless of their structures, is necessary for an efficient secretion of plant glycoproteins. In the biotechnology field, transgenic plants are rapidly emerging as an important system for the production of recombinant glycoproteins intended for therapeutic purposes, which is a strong motivation to speed up research in plant glycobiology. In this regard, the potential and limits of plant cells as a factory for the production of mammalian glycoproteins will be illustrated.
plant, Recombinant Proteins, Arabidopsis thaliana, N-glycosylation
NCBI PubMed ID: 9738959Publication DOI: 10.1023/A:1006012005654Journal NLM ID: 9106343Publisher: Dordrecht: Kluwer Academic
Correspondence: Faye L
Institutions: Laboratoire des Transports Intracellulaires, Université de Rouen, Mont Saint Aignan, France
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10. Compound ID: 30627
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b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
|
a-L-Fucp-(1-4)-+ | a-L-Fucp-(1-3)-+
| | |
b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
|
b-D-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan, glucomannan, oligosaccharide
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 11711
Bardor M, Cabanes-Macheteau M, Faye L, Lerouge P "Monitoring of N-glycosylation of plant glycoproteins by fluorophore-assisted carbohydrate electrophoresis" -
Electrophoresis 21(12) (2000) 2550-2556
We have evaluated the efficiency of a fast, simple and efficient method, fluorophore-assisted carbohydrate electrophoresis (FACE), for the characterization of plant N-linked glycans. After their enzymatic release from plant glycoproteins, N-glycans were reductively aminated to the charged fluorophore 8-aminonaphthalene-1, 3, 6-trisulfonic acid (ANTS) and separated using high resolution polyacrylamide gel electrophoresis. In addition, an affinity purification procedure using concanavalin A was developed for separation of ANTS-labeled high-mannose-type N-glycans from other plant oligosaccharides.
3, plant glycoproteins, 8-aminonaphthalene-1, 6-trisulfonic acid labeled plant N-glycans, fluorophore-assisted carbohydrate electrophoresis
NCBI PubMed ID: 10939471Publication DOI: 10.1002/1522-2683(20000701)21:12<2550::AID-ELPS2550>3.0.CO;2-GJournal NLM ID: 8204476Publisher: Wiley-VCH
Correspondence: plerouge@crihan.fr
Institutions: Laboratoire des Transports Intracellulaires, CNRS ESA, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France
Methods: MALDI-TOF MS, electrophoresis, FACE, PAGE, binding assays, fluorescence microscopy, fluorescence labeling, centrifugation
- Article ID: 12256
Olczak M, Watorek W "Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase" -
Biochimica et Biophysica Acta 1523(2-3) (2000) 236-245
N-linked oligosaccharide chains released by hydrazinolysis from yellow lupin seed diphosphonucleotide phosphatase/phosphodiesterase were fluorescence labeled and separated by high performance liquid chromatography (GlycoSep N and GlycoSep H columns). Exoglycosidase sequencing elucidated the structures of 24 separated N-glycans. Thirty percent of isolated glycans were found to be of high-mannose type (three to eight mannosyl residues), 42% were complex type and 26% belonged to paucimannosidic type. Among complex type glycans, structures with Lewis(a) epitope were identified. It is very unusual to find all types of plant N-glycans in one protein. Possible reasons for such a broad spectrum of N-glycan structures are discussed.
N-glycan, exoglycosidase sequencing, diphosphonucleotide phosphatase/phosphodiesterase, yellow lupin
NCBI PubMed ID: 11042390Publication DOI: 10.1016/s0304-4165(00)00128-8Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: watorek@bf.uni.wroc.pl
Institutions: Institute of Biochemistry and Molecular Biology, Wroclaw University, Wroclaw, Poland
Methods: HPLC, enzymatic digestion, extraction, fluorescence labeling, spectrometry
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11. Compound ID: 30628
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b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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a-L-Fucp-(1-4)-+ | a-L-Fucp-(1-3)-+
| | |
b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
|
b-D-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan, glucomannan, oligosaccharide
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 11711
Bardor M, Cabanes-Macheteau M, Faye L, Lerouge P "Monitoring of N-glycosylation of plant glycoproteins by fluorophore-assisted carbohydrate electrophoresis" -
Electrophoresis 21(12) (2000) 2550-2556
We have evaluated the efficiency of a fast, simple and efficient method, fluorophore-assisted carbohydrate electrophoresis (FACE), for the characterization of plant N-linked glycans. After their enzymatic release from plant glycoproteins, N-glycans were reductively aminated to the charged fluorophore 8-aminonaphthalene-1, 3, 6-trisulfonic acid (ANTS) and separated using high resolution polyacrylamide gel electrophoresis. In addition, an affinity purification procedure using concanavalin A was developed for separation of ANTS-labeled high-mannose-type N-glycans from other plant oligosaccharides.
3, plant glycoproteins, 8-aminonaphthalene-1, 6-trisulfonic acid labeled plant N-glycans, fluorophore-assisted carbohydrate electrophoresis
NCBI PubMed ID: 10939471Publication DOI: 10.1002/1522-2683(20000701)21:12<2550::AID-ELPS2550>3.0.CO;2-GJournal NLM ID: 8204476Publisher: Wiley-VCH
Correspondence: plerouge@crihan.fr
Institutions: Laboratoire des Transports Intracellulaires, CNRS ESA, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France
Methods: MALDI-TOF MS, electrophoresis, FACE, PAGE, binding assays, fluorescence microscopy, fluorescence labeling, centrifugation
- Article ID: 12256
Olczak M, Watorek W "Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase" -
Biochimica et Biophysica Acta 1523(2-3) (2000) 236-245
N-linked oligosaccharide chains released by hydrazinolysis from yellow lupin seed diphosphonucleotide phosphatase/phosphodiesterase were fluorescence labeled and separated by high performance liquid chromatography (GlycoSep N and GlycoSep H columns). Exoglycosidase sequencing elucidated the structures of 24 separated N-glycans. Thirty percent of isolated glycans were found to be of high-mannose type (three to eight mannosyl residues), 42% were complex type and 26% belonged to paucimannosidic type. Among complex type glycans, structures with Lewis(a) epitope were identified. It is very unusual to find all types of plant N-glycans in one protein. Possible reasons for such a broad spectrum of N-glycan structures are discussed.
N-glycan, exoglycosidase sequencing, diphosphonucleotide phosphatase/phosphodiesterase, yellow lupin
NCBI PubMed ID: 11042390Publication DOI: 10.1016/s0304-4165(00)00128-8Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: watorek@bf.uni.wroc.pl
Institutions: Institute of Biochemistry and Molecular Biology, Wroclaw University, Wroclaw, Poland
Methods: HPLC, enzymatic digestion, extraction, fluorescence labeling, spectrometry
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12. Compound ID: 30629
|
a-L-Fucp-(1-4)-+
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b-D-Galp-(1-3)-a-D-Manp2Ac-(1-6)-+
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a-L-Fucp-(1-4)-+ | a-L-Fucp-(1-3)-+
| | |
b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
|
b-D-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan, oligosaccharide
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149549,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 11711
Bardor M, Cabanes-Macheteau M, Faye L, Lerouge P "Monitoring of N-glycosylation of plant glycoproteins by fluorophore-assisted carbohydrate electrophoresis" -
Electrophoresis 21(12) (2000) 2550-2556
We have evaluated the efficiency of a fast, simple and efficient method, fluorophore-assisted carbohydrate electrophoresis (FACE), for the characterization of plant N-linked glycans. After their enzymatic release from plant glycoproteins, N-glycans were reductively aminated to the charged fluorophore 8-aminonaphthalene-1, 3, 6-trisulfonic acid (ANTS) and separated using high resolution polyacrylamide gel electrophoresis. In addition, an affinity purification procedure using concanavalin A was developed for separation of ANTS-labeled high-mannose-type N-glycans from other plant oligosaccharides.
3, plant glycoproteins, 8-aminonaphthalene-1, 6-trisulfonic acid labeled plant N-glycans, fluorophore-assisted carbohydrate electrophoresis
NCBI PubMed ID: 10939471Publication DOI: 10.1002/1522-2683(20000701)21:12<2550::AID-ELPS2550>3.0.CO;2-GJournal NLM ID: 8204476Publisher: Wiley-VCH
Correspondence: plerouge@crihan.fr
Institutions: Laboratoire des Transports Intracellulaires, CNRS ESA, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France
Methods: MALDI-TOF MS, electrophoresis, FACE, PAGE, binding assays, fluorescence microscopy, fluorescence labeling, centrifugation
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13. Compound ID: 31395
|
b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
|
a-Fucp-(1-4)-+ | a-Fucp-(1-3)-+
| | |
b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
|
b-D-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: oligosaccharide
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 12049
Lemoine J, Cabanes-Macheteau M, Bardor M, Michalski J-C, Faye L, Lerouge P "Analysis of 8-aminonaphthalene-1,3,6-trisulfonic acid labelled N-glycans by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry" -
Rapid Communications in Mass Spectrometry 14(2) (2000) 100-104
Fluorophore-assisted carbohydrate electrophoresis (FACE) is a fast and efficient analytical method which is now widely used in glycobiology for the separation and quantification of free or glycoprotein-released oligosaccharides. However, since identification by FACE of N-glycan structures is only based on their electrophoretic mobility after labelling with 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS), co-migration of derived glycans on gel could occur which may result in erroneous structural assignments. As a consequence, a protocol was developed for the fast and efficient matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometric analysis of ANTS-labelled N-glycans. N-Glycans were isolated from plant and mammalian glycoproteins, reductively aminated with the charged fluorophore 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS) and separated using high resolution polyacrylamide gel electrophoresis. The ANTS-labelled glycans were eluted from FACE gel slices and then analysed by MALDI-TOF mass spectrometry in negative ion mode. Using 3-aminoquinoline containing 2.5 mM citrate NH4+ as matrix, neutral N-linked N-glycans, as well as labelled sialylated oligosaccharides, were found to be easily detected in the 2-10 picomole range giving rise to [M-H]- ions.
MALDI-TOF MS, N-glycans, derivatives, FACE
NCBI PubMed ID: 10623937Publication DOI: 10.1002/(SICI)1097-0231(20000130)14:2<100::AID-RCM845>3.0.CO;2-WJournal NLM ID: 8802365Publisher: John Wiley And Sons Ltd
Correspondence: jerome.lemoine@univ-lille1.fr
Institutions: Laboratoire de Chimie Biologique, CNRS UMR 8576, Université de Lille, Villeneuve d’Ascq, France, Laboratoire des Transports Intracellulaires, CNRS ESA 6037, IFRMP 23, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France
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14. Compound ID: 31396
|
a-Fucp-(1-4)-+
|
b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
a-Fucp-(1-4)-+ | a-Fucp-(1-3)-+
| | |
b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
|
b-D-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: oligosaccharide
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_241116,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 12049
Lemoine J, Cabanes-Macheteau M, Bardor M, Michalski J-C, Faye L, Lerouge P "Analysis of 8-aminonaphthalene-1,3,6-trisulfonic acid labelled N-glycans by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry" -
Rapid Communications in Mass Spectrometry 14(2) (2000) 100-104
Fluorophore-assisted carbohydrate electrophoresis (FACE) is a fast and efficient analytical method which is now widely used in glycobiology for the separation and quantification of free or glycoprotein-released oligosaccharides. However, since identification by FACE of N-glycan structures is only based on their electrophoretic mobility after labelling with 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS), co-migration of derived glycans on gel could occur which may result in erroneous structural assignments. As a consequence, a protocol was developed for the fast and efficient matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometric analysis of ANTS-labelled N-glycans. N-Glycans were isolated from plant and mammalian glycoproteins, reductively aminated with the charged fluorophore 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS) and separated using high resolution polyacrylamide gel electrophoresis. The ANTS-labelled glycans were eluted from FACE gel slices and then analysed by MALDI-TOF mass spectrometry in negative ion mode. Using 3-aminoquinoline containing 2.5 mM citrate NH4+ as matrix, neutral N-linked N-glycans, as well as labelled sialylated oligosaccharides, were found to be easily detected in the 2-10 picomole range giving rise to [M-H]- ions.
MALDI-TOF MS, N-glycans, derivatives, FACE
NCBI PubMed ID: 10623937Publication DOI: 10.1002/(SICI)1097-0231(20000130)14:2<100::AID-RCM845>3.0.CO;2-WJournal NLM ID: 8802365Publisher: John Wiley And Sons Ltd
Correspondence: jerome.lemoine@univ-lille1.fr
Institutions: Laboratoire de Chimie Biologique, CNRS UMR 8576, Université de Lille, Villeneuve d’Ascq, France, Laboratoire des Transports Intracellulaires, CNRS ESA 6037, IFRMP 23, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France
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15. Compound ID: 31898
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b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
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a-L-Fucp-(1-4)-+ | a-L-Fucp-(1-3)-+
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b-D-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
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b-D-Xylp-(1-2)-+ |
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Structure type: oligomer
Compound class: glucomannan, oligosaccharide
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 12256
Olczak M, Watorek W "Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase" -
Biochimica et Biophysica Acta 1523(2-3) (2000) 236-245
N-linked oligosaccharide chains released by hydrazinolysis from yellow lupin seed diphosphonucleotide phosphatase/phosphodiesterase were fluorescence labeled and separated by high performance liquid chromatography (GlycoSep N and GlycoSep H columns). Exoglycosidase sequencing elucidated the structures of 24 separated N-glycans. Thirty percent of isolated glycans were found to be of high-mannose type (three to eight mannosyl residues), 42% were complex type and 26% belonged to paucimannosidic type. Among complex type glycans, structures with Lewis(a) epitope were identified. It is very unusual to find all types of plant N-glycans in one protein. Possible reasons for such a broad spectrum of N-glycan structures are discussed.
N-glycan, exoglycosidase sequencing, diphosphonucleotide phosphatase/phosphodiesterase, yellow lupin
NCBI PubMed ID: 11042390Publication DOI: 10.1016/s0304-4165(00)00128-8Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: watorek@bf.uni.wroc.pl
Institutions: Institute of Biochemistry and Molecular Biology, Wroclaw University, Wroclaw, Poland
Methods: HPLC, enzymatic digestion, extraction, fluorescence labeling, spectrometry
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