Found 199 structures.
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Next 15 structure(s)
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1. Compound ID: 15512
a-D-Manp-(1-6)-+
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a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/2-aminopyridine/
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D-Xylp-(1-?)-+ |
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Structure type: structural motif or average structure
; 1121 [M+H]+
Aglycon: 2-aminopyridine
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 5989
Paschinger K, Hykollari A, Razzazi-Fazeli E, Greenwell P, Leitsch D, Walochnik J, Wilson IBH "The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications" -
Glycobiology 22(2) (2012) 300-313
Trichomonad species are widespread unicellular flagellated parasites of vertebrates which interact with their hosts through carbohydrate-lectin interactions. In the past, some data have been accumulated regarding their lipo(phospho)glycans, a major glycoconjugate on their cell surfaces; on the other hand, other than biosynthetic aspects, few details about their N-linked oligosaccharides are known. In this study, we present both mass spectrometric and high-performance liquid chromatography data about the N-glycans of different strains of Trichomonas vaginalis, a parasite of the human reproductive tract. The major structure in all strains examined is a truncated oligomannose form (Man(5)GlcNAc(2)) with α1,2-mannose residues, compatible with a previous bioinformatic examination of the glycogenomic potential of T. vaginalis. In addition, dependent on the strain, N-glycans modified by pentose residues, phosphate or phosphoethanolamine and terminal N-acetyllactosamine (Galβ1,4GlcNAc) units were found. The modification of N-glycans by N-acetyllactosamine in at least some strains is shared with the lipo(phospho)glycan and may represent a further interaction partner for host galectins, thereby playing a role in binding of the parasite to host epithelia. On the other hand, the variation in glycosylation between strains may be the result of genetic diversity within this species.
mass spectrometry, phosphoethanolamine, N-glycan, Trichomonas vaginalis, pentose, trichomonads
NCBI PubMed ID: 21983210Publication DOI: 10.1093/glycob/cwr149Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, Vienna, Austria, Vetomics Core Facility for Research, Veterinärmedizinische Universität, A-1210 Wien, Austria, School of Life Sciences, University of Westminster, London W1W 6UW, UK, Institut für spezifische Prophylaxe und Tropenmedizin, Medizinische Universität Wien, A-1090 Wien, Austria
Methods: gel filtration, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, RP-HPLC, pyridylamination
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2. Compound ID: 15514
D-Xylp-(1-?)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/2-aminopyridine/
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D-Xylp-(1-?)-+ |
Show graphically |
Structure type: structural motif or average structure
; 1121 [M+H]+
Aglycon: 2-aminopyridine
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 5989
Paschinger K, Hykollari A, Razzazi-Fazeli E, Greenwell P, Leitsch D, Walochnik J, Wilson IBH "The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications" -
Glycobiology 22(2) (2012) 300-313
Trichomonad species are widespread unicellular flagellated parasites of vertebrates which interact with their hosts through carbohydrate-lectin interactions. In the past, some data have been accumulated regarding their lipo(phospho)glycans, a major glycoconjugate on their cell surfaces; on the other hand, other than biosynthetic aspects, few details about their N-linked oligosaccharides are known. In this study, we present both mass spectrometric and high-performance liquid chromatography data about the N-glycans of different strains of Trichomonas vaginalis, a parasite of the human reproductive tract. The major structure in all strains examined is a truncated oligomannose form (Man(5)GlcNAc(2)) with α1,2-mannose residues, compatible with a previous bioinformatic examination of the glycogenomic potential of T. vaginalis. In addition, dependent on the strain, N-glycans modified by pentose residues, phosphate or phosphoethanolamine and terminal N-acetyllactosamine (Galβ1,4GlcNAc) units were found. The modification of N-glycans by N-acetyllactosamine in at least some strains is shared with the lipo(phospho)glycan and may represent a further interaction partner for host galectins, thereby playing a role in binding of the parasite to host epithelia. On the other hand, the variation in glycosylation between strains may be the result of genetic diversity within this species.
mass spectrometry, phosphoethanolamine, N-glycan, Trichomonas vaginalis, pentose, trichomonads
NCBI PubMed ID: 21983210Publication DOI: 10.1093/glycob/cwr149Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, Vienna, Austria, Vetomics Core Facility for Research, Veterinärmedizinische Universität, A-1210 Wien, Austria, School of Life Sciences, University of Westminster, London W1W 6UW, UK, Institut für spezifische Prophylaxe und Tropenmedizin, Medizinische Universität Wien, A-1090 Wien, Austria
Methods: gel filtration, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, RP-HPLC, pyridylamination
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3. Compound ID: 15517
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/2-aminopyridine/
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D-Xyl-(1-?)-+ |
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Structure type: structural motif or average structure
; 1648 [M+H]+
Aglycon: 2-aminopyridine
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153530,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_423128,IEDB_548907,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_195,SB_196,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: 5989
Paschinger K, Hykollari A, Razzazi-Fazeli E, Greenwell P, Leitsch D, Walochnik J, Wilson IBH "The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications" -
Glycobiology 22(2) (2012) 300-313
Trichomonad species are widespread unicellular flagellated parasites of vertebrates which interact with their hosts through carbohydrate-lectin interactions. In the past, some data have been accumulated regarding their lipo(phospho)glycans, a major glycoconjugate on their cell surfaces; on the other hand, other than biosynthetic aspects, few details about their N-linked oligosaccharides are known. In this study, we present both mass spectrometric and high-performance liquid chromatography data about the N-glycans of different strains of Trichomonas vaginalis, a parasite of the human reproductive tract. The major structure in all strains examined is a truncated oligomannose form (Man(5)GlcNAc(2)) with α1,2-mannose residues, compatible with a previous bioinformatic examination of the glycogenomic potential of T. vaginalis. In addition, dependent on the strain, N-glycans modified by pentose residues, phosphate or phosphoethanolamine and terminal N-acetyllactosamine (Galβ1,4GlcNAc) units were found. The modification of N-glycans by N-acetyllactosamine in at least some strains is shared with the lipo(phospho)glycan and may represent a further interaction partner for host galectins, thereby playing a role in binding of the parasite to host epithelia. On the other hand, the variation in glycosylation between strains may be the result of genetic diversity within this species.
mass spectrometry, phosphoethanolamine, N-glycan, Trichomonas vaginalis, pentose, trichomonads
NCBI PubMed ID: 21983210Publication DOI: 10.1093/glycob/cwr149Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, Vienna, Austria, Vetomics Core Facility for Research, Veterinärmedizinische Universität, A-1210 Wien, Austria, School of Life Sciences, University of Westminster, London W1W 6UW, UK, Institut für spezifische Prophylaxe und Tropenmedizin, Medizinische Universität Wien, A-1090 Wien, Austria
Methods: gel filtration, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, RP-HPLC, pyridylamination
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4. Compound ID: 15537
D-Xylp-(1-?)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc
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D-Xylp-(1-?)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 5996
Schiller B, Hykollari A, Yan S, Paschinger K, Wilson IBH "Complicated N-linked glycans in simple organisms" -
Biological Chemistry 393(8) (2012) 661-673
Although countless genomes have now been sequenced, the glycomes of the vast majority of eukaryotes still present a series of unmapped frontiers. However, strides are being made in a few groups of invertebrate and unicellular organisms as regards their N-glycans and N-glycosylation pathways. Thereby, the traditional classification of glycan structures inevitably approaches its boundaries. Indeed, the glycomes of these organisms are rich in surprises including a multitude of modifications of the core regions of N-glycans and unusual antennae. From the actually rather limited glycomic information we have, it is nevertheless obvious that the biotechnological, developmental and immunological relevance of these modifications, especially in insect cell lines, model organisms and parasites means that deciphering unusual glycomes is of more than just academic interest.
N-linked oligosaccharides, protozoa, insects, molluscs, nematodes, trematodes
NCBI PubMed ID: 22944671Publication DOI: 10.1515/hsz-2012-0150Journal NLM ID: 9700112Publisher: Berlin: Walter De Gruyter
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, 1190 Wien, Austria
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5. Compound ID: 15588
a-D-Manp-(1-3)-+
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b-D-Xylp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/Asn/
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a-D-Manp-(1-6)-+ |
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Structure type: oligomer
Aglycon: Asn
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 6019
Veríssimo CD, Graeff-Teixeira C, Jones MK, Morassutti AL "Glycans in the roles of parasitological diagnosis and host-parasite interplay" -
Parasitology 146(10) (2019) 1217-1232
The investigation of the glycan repertoire of several organisms has revealed a wide variation in terms of structures and abundance of glycan moieties. Among the parasites, it is possible to observe different sets of glycoconjugates across taxa and developmental stages within a species. The presence of distinct glycoconjugates throughout the life cycle of a parasite could relate to the ability of that organism to adapt and survive in different hosts and environments. Carbohydrates on the surface, and in excretory-secretory products of parasites, play essential roles in host-parasite interactions. Carbohydrate portions of complex molecules of parasites stimulate and modulate host immune responses, mainly through interactions with specific receptors on the surface of dendritic cells, leading to the generation of a pattern of response that may benefit parasite survival. Available data reviewed here also show the frequent aspect of parasite immunomodulation of mammalian responses through specific glycan interactions, which ultimately makes these molecules promising in the fields of diagnostics and vaccinology.
immune response, glycoconjugate, glycans, Parasite, protozoa, helminth
NCBI PubMed ID: 31057132Publication DOI: 10.1017/S0031182019000465Journal NLM ID: 0401121Publisher: London, New York, Cambridge University Press
Correspondence: Alessandra Loureiro Morassutti
Institutions: Escola de Ciências, Pontifícia Universidade Católica do Rio Grande do Sul, Av. Ipiranga 6681, Porto Alegre RS 90619-900 Rio Grande do Sul, Brazil, School of Biological Sciences, Queen's University Belfast, 2017, University Road, Belfast, BT7 1NN, Northern Ireland, UK, School of Veterinary Science, University of Queensland, St Lucia, Qld, 4072 Brisbane, Australia
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6. Compound ID: 19195
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
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{{{-a-D-Manp-(1-6)-}}}a-D-Manp-(1-6)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-2)-+ | |
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b-D-Xyl-(1--P--?)--a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcNAc-(1-4)-b-D-GlcNAc
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b-D-Xyl-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_140942,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_164046,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_187201,IEDB_429156,IEDB_474450,IEDB_540671,IEDB_548907,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 7560
Harvey DJ "Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2011-2012" -
Mass Spectrometry Reviews 36(3) (2017) 255-422
This review is the seventh update of the original article published in 1999 on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2012. General aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, and fragmentation are covered in the first part of the review and applications to various structural types constitute the remainder. The main groups of compound are oligo- and poly-saccharides, glycoproteins, glycolipids, glycosides, and biopharmaceuticals. Much of this material is presented in tabular form. Also discussed are medical and industrial applications of the technique, studies of enzyme reactions, and applications to chemical synthesis.
carbohydrates, MALDI, glycolipids, glycoproteins, biopharmaceuticals
NCBI PubMed ID: 26270629Publication DOI: 10.1002/mas.21471Journal NLM ID: 8219702Publisher: Wiley
Correspondence: Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, Oxford, UK
Institutions: david.harvey@bioch.ox.ac.uk
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7. Compound ID: 21398
a-D-Manp-(1-3)-+
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Xylp-(1--P--?)--+ |
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?%a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-+ ?%a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
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{{{-a-D-Manp-(1-6)-}}}/n=2/-?%a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Man-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
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Xylp-(1-?)-+ |
Show graphically |
Structure type: structural motif or average structure
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_140434,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_167188,IEDB_174332,IEDB_174840,IEDB_187201,IEDB_423157,IEDB_429156,IEDB_474450,IEDB_540671,IEDB_548907,IEDB_76933,IEDB_857734,IEDB_857735,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 8631
Thak EJ, Kim J, Lee DJ, Kim JY, Kang HA "Structural analysis of N-/O-glycans assembled on proteins in yeasts" -
Journal of Microbiology 56(1) (2018) 11-23
Protein glycosylation, the most universal and diverse post-translational modification, can affect protein secretion, stability, and immunogenicity. The structures of glycans attached to proteins are quite diverse among different organisms and even within yeast species. In yeast, protein glycosylation plays key roles in the quality control of secretory proteins, and particularly in maintaining cell wall integrity. Moreover, in pathogenic yeasts, glycans assembled on cell-surface glycoproteins can mediate their interactions with host cells. Thus, a comprehensive understanding of protein glycosylation in various yeast species and defining glycan structure characteristics can provide useful information for their biotechnological and clinical implications. Yeast-specific glycans are a target for glyco-engineering; implementing human-type glycosylation pathways in yeast can aid the production of recombinant glycoproteins with therapeutic potential. The virulenceassociated glycans of pathogenic yeasts could be exploited as novel targets for antifungal agents. Nowadays, several glycomics techniques facilitate the generation of species-and strain-specific glycome profiles and the delineation of modified glycan structures in mutant and engineered yeast cells. Here, we present the protocols employed in our laboratory to investigate the N-and O-glycan chains released from purified glycoproteins or cell wall mannoproteins in several yeast species.
protein glycosylation, structure analysis, yeast, N-/O-glycans
NCBI PubMed ID: 29299842Publication DOI: 10.1007/s12275-018-7468-xJournal NLM ID: 9703165Publisher: Seoul: Microbiological Society of Korea
Correspondence: Kang HA
Institutions: Department of Life Science, Chung-Ang University, Seoul, Republic of Korea, Department of Microbiology and Molecular Biology, Chungnam National University, Daejeon, Republic of Korea
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8. Compound ID: 22130
a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-2)-L-Asn
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D-Xylp-(1-?)-+ |
Show graphically |
Structure type: oligomer
Compound class: glycoprotein, mannan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 9094
Thak EJ, Lee SB, Xu-Vanpala S, Lee DJ, Chung SY, Bahn YS, Oh DB, Shinohara ML, Kang HA "Core N-glycan structures are critical for the pathogenicity of Cryptococcus neoformans by modulating host cell death" -
mBio 11(3) (2020) ID e00711-20
Cryptococcus neoformans is a human-pathogenic fungal pathogen that causes life-threatening meningoencephalitis in immunocompromised individuals. To investigate the roles of N-glycan core structure in cryptococcal pathogenicity, we constructed mutant strains of C. neoformans with defects in the assembly of lipid-linked N-glycans in the luminal side of the endoplasmic reticulum (ER). Deletion of ALG3 (alg3Δ), which encodes dolichyl-phosphate-mannose (Dol-P-Man)-dependent α-1,3-mannosyltransferase, resulted in the production of truncated neutral N-glycans carrying five mannose residues as a major species. Despite moderate or nondetectable defects in virulence-associated phenotypes in vitro, the alg3Δ mutant was avirulent in a mouse model of systemic cryptococcosis. Notably, the mutant did not show defects in early stages of host cell interaction during infection, including attachment to lung epithelial cells, opsonic/nonopsonic phagocytosis, and manipulation of phagosome acidification. However, the ability to drive macrophage cell death was greatly decreased in this mutant, without loss of cell wall remodeling capacity. Furthermore, deletion of ALG9 and ALG12, encoding Dol-P-Man-dependent α-1,2-mannosyltransferases and α-1,6-mannosyltransferases, generating truncated core N-glycans with six and seven mannose residues, respectively, also displayed remarkably reduced macrophage cell death and in vivo virulence. However, secretion levels of interleukin-1β (IL-1β) were not reduced in the bone marrow-derived dendritic cells obtained from Asc- and Gsdmd-deficient mice infected with the alg3Δ mutant strain, excluding the possibility that pyroptosis is a main host cell death pathway dependent on intact core N-glycans. Our results demonstrated N-glycan structures as a critical feature in modulating death of host cells, which is exploited by as a strategy for host cell escape for dissemination of C. neoformans. We previously reported that the outer mannose chains of N-glycans are dispensable for the virulence of C. neoformans, which is in stark contrast to findings for the other human-pathogenic yeast, Candida albicans Here, we present evidence that an intact core N-glycan structure is required for C. neoformans pathogenicity by systematically analyzing alg3Δ, alg9Δ, and alg12Δ strains that have defects in lipid-linked N-glycan assembly and in in vivo virulence. The alg null mutants producing truncated core N-glycans were defective in inducing host cell death after phagocytosis, which is triggered as a mechanism of pulmonary escape and dissemination of C. neoformans, thus becoming inactive in causing fatal infection. The results clearly demonstrated the critical features of the N-glycan structure in mediating the interaction with host cells during fungal infection. The delineation of the roles of protein glycosylation in fungal pathogenesis not only provides insight into the glycan-based fungal infection mechanism but also will aid in the development of novel antifungal agents.
Cryptococcus neoformans, fungal pathogenesis, ALG, N-linked protein glycosylation
NCBI PubMed ID: 32398313Publication DOI: 10.1128/mBio.00711-20Journal NLM ID: 101519231Publisher: Washington, DC: American Society for Microbiology
Correspondence: Kang HA
Institutions: Department of Life Science, Chung-Ang University, Seoul, South Korea, Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul, South Korea, Korea Research Institute of Bioscience and Biotechnology, Daejeon, South Korea, Department of Immunology, Duke University School of Medicine, Durham, USA, Department of Microbiology and Molecular Genetics, Duke University School of Medicine, Durham, USA
Methods: ELISA, biological assays, HPLC, enzymatic digestion, extraction, column chromatography, cell growth, gene expression, phagocytosis assay, fluorescent labeling, staining
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9. Compound ID: 22134
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-2)-L-Asn
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D-Xylp-(1-?)-+ |
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Structure type: oligomer
Compound class: glycoprotein, mannan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 9094
Thak EJ, Lee SB, Xu-Vanpala S, Lee DJ, Chung SY, Bahn YS, Oh DB, Shinohara ML, Kang HA "Core N-glycan structures are critical for the pathogenicity of Cryptococcus neoformans by modulating host cell death" -
mBio 11(3) (2020) ID e00711-20
Cryptococcus neoformans is a human-pathogenic fungal pathogen that causes life-threatening meningoencephalitis in immunocompromised individuals. To investigate the roles of N-glycan core structure in cryptococcal pathogenicity, we constructed mutant strains of C. neoformans with defects in the assembly of lipid-linked N-glycans in the luminal side of the endoplasmic reticulum (ER). Deletion of ALG3 (alg3Δ), which encodes dolichyl-phosphate-mannose (Dol-P-Man)-dependent α-1,3-mannosyltransferase, resulted in the production of truncated neutral N-glycans carrying five mannose residues as a major species. Despite moderate or nondetectable defects in virulence-associated phenotypes in vitro, the alg3Δ mutant was avirulent in a mouse model of systemic cryptococcosis. Notably, the mutant did not show defects in early stages of host cell interaction during infection, including attachment to lung epithelial cells, opsonic/nonopsonic phagocytosis, and manipulation of phagosome acidification. However, the ability to drive macrophage cell death was greatly decreased in this mutant, without loss of cell wall remodeling capacity. Furthermore, deletion of ALG9 and ALG12, encoding Dol-P-Man-dependent α-1,2-mannosyltransferases and α-1,6-mannosyltransferases, generating truncated core N-glycans with six and seven mannose residues, respectively, also displayed remarkably reduced macrophage cell death and in vivo virulence. However, secretion levels of interleukin-1β (IL-1β) were not reduced in the bone marrow-derived dendritic cells obtained from Asc- and Gsdmd-deficient mice infected with the alg3Δ mutant strain, excluding the possibility that pyroptosis is a main host cell death pathway dependent on intact core N-glycans. Our results demonstrated N-glycan structures as a critical feature in modulating death of host cells, which is exploited by as a strategy for host cell escape for dissemination of C. neoformans. We previously reported that the outer mannose chains of N-glycans are dispensable for the virulence of C. neoformans, which is in stark contrast to findings for the other human-pathogenic yeast, Candida albicans Here, we present evidence that an intact core N-glycan structure is required for C. neoformans pathogenicity by systematically analyzing alg3Δ, alg9Δ, and alg12Δ strains that have defects in lipid-linked N-glycan assembly and in in vivo virulence. The alg null mutants producing truncated core N-glycans were defective in inducing host cell death after phagocytosis, which is triggered as a mechanism of pulmonary escape and dissemination of C. neoformans, thus becoming inactive in causing fatal infection. The results clearly demonstrated the critical features of the N-glycan structure in mediating the interaction with host cells during fungal infection. The delineation of the roles of protein glycosylation in fungal pathogenesis not only provides insight into the glycan-based fungal infection mechanism but also will aid in the development of novel antifungal agents.
Cryptococcus neoformans, fungal pathogenesis, ALG, N-linked protein glycosylation
NCBI PubMed ID: 32398313Publication DOI: 10.1128/mBio.00711-20Journal NLM ID: 101519231Publisher: Washington, DC: American Society for Microbiology
Correspondence: Kang HA
Institutions: Department of Life Science, Chung-Ang University, Seoul, South Korea, Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul, South Korea, Korea Research Institute of Bioscience and Biotechnology, Daejeon, South Korea, Department of Immunology, Duke University School of Medicine, Durham, USA, Department of Microbiology and Molecular Genetics, Duke University School of Medicine, Durham, USA
Methods: ELISA, biological assays, HPLC, enzymatic digestion, extraction, column chromatography, cell growth, gene expression, phagocytosis assay, fluorescent labeling, staining
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10. Compound ID: 23286
b-D-Xylp-(1-2)-+
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b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc
|
a-D-Manp-(1-6)-+ |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 9522
Oxley D, Munro SLA, Craik DJ, Bacic A "structure and distribution of N-glycans on the S7-allele stylar self-incompatibility ribonuclease of Nicotiana alata" -
Journal of Biochemistry 123 (1998) 978-983
S-RNases are the stylar products of the self-incompatibility (S)-locus in solanaceous plants (including Nicotiana alata), and as such, are involved in the prevention of self-pollination. All cDNA sequences of S-RNase products of functional S-alleles contain potential N-glycosylation sites, with one site being conserved in all cases, suggesting that N-glycosylation is important in self-incompatibility. In this study, we report on the structure and localization of the N-glycans on the S7-allele RNase of N. alata. A total of nine N-glycans, belonging to the high-mannose- and xylosylated hybrid-classes, were identified and characterized by a combination of electrospray-ionization mass-spectrometry (ESI-MS), 1H-NMR spectroscopy, and methylation analyses. The glycosylation pattern of individual glycosylation sites was determined by ESI-MS of the glycans released from isolated chymotryptic glycopeptides. All three N-glycosylation sites showed microheterogeneity and each had a unique complement of N-glycans. The N-glycosylation pattern of the S7-RNase is significantly different to those of the S1- and S2-RNases.
microheterogeneity, N-glycan, Nicotiana alata, ribonuclease, self-incompatibility.
NCBI PubMed ID: 9562634Journal NLM ID: 0376600Publisher: Japanese Biochemical Society
Correspondence: d.oxley@botany.unimelb.edu
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia, Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia.
Methods: 1H NMR, IR, SDS-PAGE, ESI-MS, HPLC, methylation analysis, chymotrypsin digestion, peptide sequencing
- Article ID: 10050
Woodward JR, Craik D, Dell A, Khoo KH, Munro SLA, Clarke AE, Bacic A "Structural analysis of the N-linked glycan chains from a stylar glycoprotein associated with expression of self-incompatibility in Nicotiana alata" -
Glycobiology 2 (1992) 241-250
Self-incompatibility in flowering plants of the family Solanaceae is mediated by the product of the S-allele. The allelic products of the S-gene in the female sexual tissues of the pistil are glycoproteins in the mol. wt range 28-32 kDa. These S-glycoproteins have been isolated from styles of Nicotiana alata, homozygous for the S1- and S2-alleles. Earlier studies have indicated that the single potential N-glycosylation site on the S1-glycoprotein bears a glycan chain, whereas of the four potential N-glycosylation sites on the S2-glycoprotein, three are glycosylated. This paper describes the purification and characterization of the N-linked glycan chains from these two glycoproteins. Oligosaccharides were cleaved off the glycoproteins using peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F (N-glycanase F) and separated by anion-exchange HPLC. Four types of hybrid structure were defined by chemical techniques, fast atom bombardment-mass spectrometry (FAB-MS) and 1H-NMR. Although the relative amounts differed, all four structures were found on both the S1- and S2-glycoproteins, and are heterogeneous at some N-glycosylation sites. No O-linked glycans were detected on the S2-glycoprotein. These results are discussed in relation to the potential of the structural diversity residing in this array of glycoforms to play a rôle in allelic specificity.
NCBI PubMed ID: 1498421Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Australia
Methods: gel filtration, 1H NMR, FAB-MS, GC-MS, SDS-PAGE, HPLC, enzymatic digestion, methylation analysis, PC
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11. Compound ID: 23288
a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
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b-D-GlcNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcNAc-(1-4)-D-GlcNAc
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b-D-Xylp-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 9522
Oxley D, Munro SLA, Craik DJ, Bacic A "structure and distribution of N-glycans on the S7-allele stylar self-incompatibility ribonuclease of Nicotiana alata" -
Journal of Biochemistry 123 (1998) 978-983
S-RNases are the stylar products of the self-incompatibility (S)-locus in solanaceous plants (including Nicotiana alata), and as such, are involved in the prevention of self-pollination. All cDNA sequences of S-RNase products of functional S-alleles contain potential N-glycosylation sites, with one site being conserved in all cases, suggesting that N-glycosylation is important in self-incompatibility. In this study, we report on the structure and localization of the N-glycans on the S7-allele RNase of N. alata. A total of nine N-glycans, belonging to the high-mannose- and xylosylated hybrid-classes, were identified and characterized by a combination of electrospray-ionization mass-spectrometry (ESI-MS), 1H-NMR spectroscopy, and methylation analyses. The glycosylation pattern of individual glycosylation sites was determined by ESI-MS of the glycans released from isolated chymotryptic glycopeptides. All three N-glycosylation sites showed microheterogeneity and each had a unique complement of N-glycans. The N-glycosylation pattern of the S7-RNase is significantly different to those of the S1- and S2-RNases.
microheterogeneity, N-glycan, Nicotiana alata, ribonuclease, self-incompatibility.
NCBI PubMed ID: 9562634Journal NLM ID: 0376600Publisher: Japanese Biochemical Society
Correspondence: d.oxley@botany.unimelb.edu
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia, Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia.
Methods: 1H NMR, IR, SDS-PAGE, ESI-MS, HPLC, methylation analysis, chymotrypsin digestion, peptide sequencing
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12. Compound ID: 23303
b-D-Xylp-(1-2)-+ a-L-Fucp-(1-3)-+
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a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 9528
Ishihara H, Takahashi N, Oguri S, Tejima S "Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides" -
Journal of Biological Chemistry 254 (1979) 10715-10719
Asparagine-linked oligosaccharides of stem bromelain glycopeptides were quantitatively released by digestion with the almond glycopeptidase which cleaves β-aspartylglycosylamine linkage in glycopeptides with oligopeptide moieties. The primary structures of the two oligosaccharide components, (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)2-(Xyl)1(Fuc)1(GlcNAc)2 were elucidated as Man α1 leads to 6Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4GlcNAc β1 leads 4[Fuc α1 leads to 3]GlcNAc and Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4 GlcNAc β1 leads to 4[Fuc α1 leads to 3] GlcNAc, respectively.
NCBI PubMed ID: 500606Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan, Department of Biochemistry, School of Medicine, Nagoya City University, Nagoya, Japan
Methods: GLC, enzymatic digestion, methylation analysis, paper electrophoresis, PC
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13. Compound ID: 23304
a-D-Manp-(1-6)-+ a-L-Fucp-(1-3)-+
| |
b-D-Xylp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 9528
Ishihara H, Takahashi N, Oguri S, Tejima S "Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides" -
Journal of Biological Chemistry 254 (1979) 10715-10719
Asparagine-linked oligosaccharides of stem bromelain glycopeptides were quantitatively released by digestion with the almond glycopeptidase which cleaves β-aspartylglycosylamine linkage in glycopeptides with oligopeptide moieties. The primary structures of the two oligosaccharide components, (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)2-(Xyl)1(Fuc)1(GlcNAc)2 were elucidated as Man α1 leads to 6Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4GlcNAc β1 leads 4[Fuc α1 leads to 3]GlcNAc and Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4 GlcNAc β1 leads to 4[Fuc α1 leads to 3] GlcNAc, respectively.
NCBI PubMed ID: 500606Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan, Department of Biochemistry, School of Medicine, Nagoya City University, Nagoya, Japan
Methods: GLC, enzymatic digestion, methylation analysis, paper electrophoresis, PC
- Article ID: 9861
Kimura Y, Suehisa H, Yamaguchi O, Nakajima S, Takagi S "Structures of sugar chains of water-soluble glycoproteins in developing castor bean cotyledons" -
Agricultural and Biological Chemistry 54 (1990) 3259-3267
The structures of sugar chains from the water-soluble glycoproteins in developing castor beans have been identified. The structural analyses were done by a fluorescence method combined with exoglycosidase digestions and 1H-NMR spectroscopy. The identified structures fell into two categories; one was an oligomannose-type, the other xylomannose-type or xylose-containing type. Among these oligosaccharides, Man3Fuc1Xyl1GlcNAc2 (M3FX; 38%) and Man6GlcNAc2 (M6B; 22%) were the major structures. The higher mannose-content oligosaccharides (Man8-7GlcNAc2) were only 4.1%, and the further-modified structures (GNM3FX, M2FX) than M3FX were 22% of the total.
NCBI PubMed ID: 1368642Journal NLM ID: 0370452WWW link: http://ci.nii.ac.jp/naid/110006324732Publisher: Tokyo: Agricultural Chemical Society Of Japan
Institutions: Department of Agricultural Sciences, Faculty of Agriculture, Okayama University, Japan
Methods: 1H NMR, HPLC, enzymatic digestion, pyridylamination
- Article ID: 9884
Kimura Y, Nakagawa Y, Tokuda T, Yamai M, Nakajima S, Higashide E, Takagi S, Takagi SS "Structures of N-linked oligosaccharides of microsomal glycoproteins from developing castor bean endosperms" -
Bioscience, Biotechnology, and Biochemistry 56 (1992) 215-222
The structures of sugar chains of the glycoproteins from the microsomal fraction of developing castor bean endosperms have been analyzed. The structural analyses were done by a fluorescence method combined with component analysis, exoglycosidase digestions, partial acetolysis, Smith degradation, and 1H-NMR spectroscopy. The estimated structures fell into three categories; the first was oligomannose-type, the second xylomannose-type, the third complex-type. Among these oligosaccharides, Man3Fuc1Xyl1GlcNAc2 (M3FX) and Man6GlcNAc2 (M6B) were the major structures. The structures of Man4GlcNAc2 (M4C) and Man4Xyl1GlcNAc2 (M4X) have also been found in the microsomal glycoproteins of the developing bean endosperms. These results could indicate that the structures of M4C, M4X, and M3FX are formed in the stage of sugar chain processing in the microsomal fraction, in which oligomannose-type sugar chains are modified into complex-type ones by several kinds of processing enzymes.
NCBI PubMed ID: 1368297Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Institutions: Division of Bio-resource Science, Graduate School of Natural Science and Technology, Okayama University, Japan
Methods: 1H NMR, Smith degradation, enzymatic digestion, partial acetolysis
- Article ID: 9938
Takahashi N, Hitotsuya H, Hanzawa H, Arata Y, Kurihara Y "Structural study of asparagine-linked oligosaccharide moiety of taste- modifying protein, miraculin" -
Journal of Biological Chemistry 265 (1990) 7793-7798
The structures of the N-linked oligosaccharides of miraculin, which is a taste modifying glycoprotein isolated from miracle fruits, berries of Richadella dulcifica, are reported. Asparagine-linked oligosaccharides were released from the protein by glycopeptidase (almond) digestion. The reducing ends of the oligosaccharide chains thus obtained were aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of pyridylamino derivatives of the oligosaccharides was separated by high performance liquid chromatography (HPLC) on an ODS-silica column. More than five kinds of oligosaccharide fractions were separated by the one chromatographic run. The structure of each oligosaccharide thus isolated was analyzed by a combination of sequential exoglycosidase digestion and another kind of HPLC with an amidesilica column. Furthermore, high resolution proton nuclear magnetic resonance (1H NMR) measurements were carried out. It was found that 1) five oligosaccharides obtained are a series of compounds with xylose-containing common structural core, Xyl β1----2 (Man α1----6) Man β1----4-GlcNAc β1----4 (Fuca1----3)GlcNAc, 2) a variety of oligosaccharide structures are significant for two glycosylation sites, Asn-42 and Asn-186, and 3) two new oligosaccharides, B and D, with unusual structures containing monoantennary complex-type were characterized. (formula; see text)
NCBI PubMed ID: 2335505Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Faculty of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan, Department of Biochemistry, Nagoya City University College of Nursing, Japan, Department of Chemistry, Faculty of Education, Yokohama National University, Yokohama, Japan
Methods: gel filtration, 1H NMR, HPLC, enzymatic digestion
- Article ID: 10223
Kamerling JP "Xylose-containing carbohydrate chains derived from N-glycoproteins" -
Pure and Applied Chemistry 63 (1991) 465-472
Xylose-containing N-linked carbohydrate chains are integral parts of certain plant and animal glycoproteins. In all of the known structures, p-D-xylose is 1-2-linked to p-D-mannose of the trimannosyl-N,N'-diacetylchitobiose unit. If a-L-fucose is present at the asparagine-linked N-acetyl-D-glucosamine, then there are differences in the sites of its attachment, namely, a1-3- or a1-6-linked, depending on the biological origin. The a-D-mannose residues can be substituted with additional monosaccharides or 3-0-methylated. The state of the art with respect to structural analysis, organic synthesis, conformational analysis, biosynthesis, lectin binding, and immunological aspects is reviewed.
Publication DOI: 10.1351/pac199163040465Journal NLM ID: 0376514Publisher: Oxford: Blackwell Scientific Publications
Institutions: Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands
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14. Compound ID: 23338
a-D-Manp-(1-6)-+ a-L-Fucp-(1-3)-+
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b-D-Xylp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86
The structure is contained in the following publication(s):
- Article ID: 9545
van Kuik JA, Hoffmann RA, Mutsaers JHGM, van Halbeek H, Kamerling JP, Vliegenthart JFG "A 500-MHz 1H-NMR study on the N-linked carbohydrate chain of bromelain. 1H-NMR structural-reporter-groups of Fucose α(1-3)-linked to asparagine-bound N-acetylglucosamine" -
Glycoconjugate Journal 3 (1986) 27-34
The 500-MHz 1H-NMR characteristics of the N-linked carbohydrate chain Man-α(1-6)[Xyl-β(1-2)]Man-β(1-4)GlcNAc-β(1-4)[Fuc-α(1-3)]GlcNAc-β1-N-Asn of the proteolytic enzyme bromelain (EC 3.4.22.4) from pineapple stem were determined for the oligosaccharide and the glycopeptide, obtained by hydrazinolysis and Pronase digestion, respectively. The 1H-NMR structural-reporter-groups of the α(1-3)-linked fucose residue form unique sets of data for the alditol as well as for the glycopeptide.
bromelain, 500-MHz 1H-NMR spectroscopy, N-glycosidic glycan
Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Institutions: Department of Bio-Organic Chemistry, State University of Utrecht, Utrecht, The Netherlands
Methods: 1H NMR, hydrazinolysis, cation-exchange chromatography
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15. Compound ID: 23339
a-D-Manp-(1-3)-+
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b-D-Xylp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol
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a-D-Manp-(1-6)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_167188,IEDB_174332,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73
The structure is contained in the following publication(s):
- Article ID: 9545
van Kuik JA, Hoffmann RA, Mutsaers JHGM, van Halbeek H, Kamerling JP, Vliegenthart JFG "A 500-MHz 1H-NMR study on the N-linked carbohydrate chain of bromelain. 1H-NMR structural-reporter-groups of Fucose α(1-3)-linked to asparagine-bound N-acetylglucosamine" -
Glycoconjugate Journal 3 (1986) 27-34
The 500-MHz 1H-NMR characteristics of the N-linked carbohydrate chain Man-α(1-6)[Xyl-β(1-2)]Man-β(1-4)GlcNAc-β(1-4)[Fuc-α(1-3)]GlcNAc-β1-N-Asn of the proteolytic enzyme bromelain (EC 3.4.22.4) from pineapple stem were determined for the oligosaccharide and the glycopeptide, obtained by hydrazinolysis and Pronase digestion, respectively. The 1H-NMR structural-reporter-groups of the α(1-3)-linked fucose residue form unique sets of data for the alditol as well as for the glycopeptide.
bromelain, 500-MHz 1H-NMR spectroscopy, N-glycosidic glycan
Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Institutions: Department of Bio-Organic Chemistry, State University of Utrecht, Utrecht, The Netherlands
Methods: 1H NMR, hydrazinolysis, cation-exchange chromatography
- Article ID: 10307
Ashford DA, Dwek RA, Rademacher TW, Lis H, Sharon N "The glycosylation of glycoprotein lectins. Intra- and inter-genus variation in N-linked oligosaccharide expression" -
Carbohydrate Research 213 (1991) 215-227
Glycosylated lectins represent a series of glycoproteins with related activities and, in the case of the Leguminosae, related amino acid sequences. Therefore, they offer a model system in which to study the diversity of N-linked oligosaccharide structures of plant glycoproteins. The influence of the polypeptide on the type of oligosaccharide substitution and the problem of inter- and intra-genus variation in glycosylation can also be addressed. Analysis of the glycosylation of 18 lectins has shown that they can be classified into four qualitatively similar groups on the basis of the Bio-Gel P-4 elution profiles of the oligosaccharides released by hydrazinolysis: (a) The Erythrina cristagalli profile, with a major component at 8.8 glucose units (gu) and minor components at 8.0, 7.2, and 5.8 gu. The major component is the heptasaccharide, α-D-Manp-(1----3)-[α-D-Manp-(1----6)]-[β-D-Xylp-(1----2)]- β-D-Manp-β-D-GlcpNAc-(1----4)-[α-L-Fucp-(1----3)]- D-GlcNAc. (b) The Phaseolus vulgaris profile, which was characterized by peaks at 12.5, 11.7, 10.8, and 9.9 gu, in addition to the peaks at 8.8, 8.0, 7.2, and 5.8 gu mentioned above. These higher-mol.-wt. components were oligo-D-mannose oligosaccharides containing 9, 8, 7, and 6 D-mannose residues, respectively. (c) The Lonchocarpas capassa profile, which had a major peak at approximately 8 gu. (d) The soybean agglutinin profile, which has a single peak at 12.5 gu. This peak consisted solely of an oligomannose undecasaccharide containing 9 D-mannose residues. This lectin is unique in that it shows no microheterogeneity.
NCBI PubMed ID: 1933938Publication DOI: 10.1016/S0008-6215(00)90610-4Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Department of Biophysics, The Weizmann Institute of Science, Rehovot, Israel, Department of Biochemistry, University of Oxford, Great Britain
Methods: gel filtration, 1H NMR, HPLC, enzymatic digestion, paper electrophoresis
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