Show legend Show as text

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

• 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: 21983210
  Publication DOI: 10.1093/glycob/cwr149
  Journal NLM ID: 9104124
  Publisher: 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
  
   
  
  Trichomonas vaginalis C1 (ATCC 30001), Trichomonas vaginalis IR-78
  CSDB ID 8288 (all data & tools)

Show legend Show as text

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

• 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: 21983210
  Publication DOI: 10.1093/glycob/cwr149
  Journal NLM ID: 9104124
  Publisher: 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
  
   
  
  Trichomonas vaginalis C1 (ATCC 30001)
  CSDB ID 8290 (all data & tools)

Show legend Show as text

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

• 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: 21983210
  Publication DOI: 10.1093/glycob/cwr149
  Journal NLM ID: 9104124
  Publisher: 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
  
   
  
  Trichomonas vaginalis C1 (ATCC 30001)
  CSDB ID 8293 (all data & tools)

Show legend Show as text

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

• 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: 22944671
  Publication DOI: 10.1515/hsz-2012-0150
  Journal NLM ID: 9700112
  Publisher: Berlin: Walter De Gruyter
  Correspondence: iain.wilson@boku.ac.at
  Institutions: Department für Chemie, Universität für Bodenkultur, 1190 Wien, Austria
  
   
  
  Trichomonas vaginalis
  CSDB ID 8368 (all data & tools)

Show legend Show as text

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

• 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: 31057132
  Publication DOI: 10.1017/S0031182019000465
  Journal NLM ID: 0401121
  Publisher: 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
  
   
  
  Trypanosoma brucei
  CSDB ID 29170 (all data & tools)

Show legend Show as text

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

• 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: 26270629
  Publication DOI: 10.1002/mas.21471
  Journal NLM ID: 8219702
  Publisher: Wiley
  Correspondence: Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, Oxford, UK
  Institutions: david.harvey@bioch.ox.ac.uk
  
   
  
  Cryptococcus neoformans
  CSDB ID 44566 (all data & tools)

Show legend Show as text

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

• 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: 29299842
  Publication DOI: 10.1007/s12275-018-7468-x
  Journal NLM ID: 9703165
  Publisher: 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
  
   
  
  Cryptococcus neoformans
  CSDB ID 49088 (all data & tools)

Show legend Show as text

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

• 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: 32398313
  Publication DOI: 10.1128/mBio.00711-20
  Journal NLM ID: 101519231
  Publisher: 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
  
   
  
  Cryptococcus neoformans var. grubii H99 (Δcap59 mutant)
  CSDB ID 50760 (all data & tools)

Show legend Show as text

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

• 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: 32398313
  Publication DOI: 10.1128/mBio.00711-20
  Journal NLM ID: 101519231
  Publisher: 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
  
   
  
  Cryptococcus neoformans var. grubii H99 (Δcap59 Δoch1 mutant)
  CSDB ID 50764 (all data & tools)

Show legend Show as text

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

• 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: 9562634
  Journal NLM ID: 0376600
  Publisher: 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
  
   
  
  Nicotiana alata
  CSDB ID 133129 (all data & tools)
• 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: 1498421
  Journal NLM ID: 9104124
  Publisher: 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
  
   
  
  Nicotiana alata
  CSDB ID 126632 (all data & tools)

Show legend Show as text

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

• 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: 9562634
  Journal NLM ID: 0376600
  Publisher: 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
  
   
  
  Nicotiana alata
  CSDB ID 133131 (all data & tools)

Show legend Show as text

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

• 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: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Department of Bio-Organic Chemistry, State University of Utrecht, Utrecht, The Netherlands
  Methods: 1H NMR, hydrazinolysis, cation-exchange chromatography
  
   
  
  Ananas comosus
  CSDB ID 127884 (all data & tools)
• 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: 1933938
  Publication DOI: 10.1016/S0008-6215(00)90610-4
  Journal NLM ID: 0043535
  Publisher: 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
  
   
  
  Erythrina cristagalli
  CSDB ID 116183 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: 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_148492,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• 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: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Department of Bio-Organic Chemistry, State University of Utrecht, Utrecht, The Netherlands
  Methods: 1H NMR, hydrazinolysis, cation-exchange chromatography
  
   
  
  Ananas comosus
  CSDB ID 127885 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,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_148492,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

• Article ID: 9546
  Takahashi N, Hotta T, Ishihara H, Mori M, Tejima S, Bligny R, Akazawa T, Endo S, Arata Y "Xylose-containing common structural unit in N-linked oligosaccharides of laccase from sycamore cells" - Biochemistry 25(2) (1986) 388-395
  

  The structures of asparagine-linked oligosaccharides of laccase excreted by sycamore (Acer pseudoplatanus L.) cells are reported. Peptic glycopeptides obtained from the laccase were treated with N-oligosaccharide glycopeptidase (EC 3.5.1.52) to release the oligosaccharide moieties. The oligosaccharides thus obtained were fractionated into six components by gel filtration, thin-layer chromatography, and high-performance liquid chromatography. The structures of the isolated oligosaccharides were determined by sugar analysis, exoglycosidase digestion, and methylation analysis in combination with high-resolution proton nuclear magnetic resonance spectroscopy. It was found that (1) the six oligosaccharides are a series of compounds of xylose-containing biantennary complex types that share as the core a common structural unit, i.e., Xyl-β(l-2)[Man-α(l-6)]Man-β(l-4)GlcNAc-β(l-4)[Fuc-α(1-3)]GlcNAc, and (2) mannose, N-acetylglucosamine, galactose, and fucose residues are additionally linked to the core as the outer chain moieties.

  Publication DOI: 10.1021/bi00350a018
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan, Department of Biochemistry, Nagoya City University Medical School, Nagoya, Japan, Centre National de la Recherche Scientifique, CENG, Grenoble, France, Research Institute for Biological Regulation School of Agriculture, Nagoya University, Nagoya, Japan, Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Tokyo, Japan
  Methods: 1H NMR, TLC, acid hydrolysis, HPLC, enzymatic digestion, methylation analysis
  
   
  
  Acer pseudoplatanus
  CSDB ID 107206 (all data & tools)
• Article ID: 9930
  Priem B, Solokwan J, Wieruszeski JM, Strecker G, Nazih H, Morvan H "Isolation and characterization of free glycans of the oligomannoside type from the extracellular medium of a plant cell suspension" - Glycoconjugate Journal 7 (1990) 121-132
  

  The oligosaccharides Man5GlcNAc and Man3(Xyl)GlcNAc(Fuc)GlcNAc presumed to originate fromN-glycosyl proteins have been purified from an extracellular medium (concentration: 2–5 mg/l of 14 day cultures) of white campion (Silene alba) suspension culture. Their primary structures have been determined by1H-400-MHz NMR spectroscopy and FAB-MS spectrometry. They are probably the result of an autophagic process including protein catabolism due to sucrose starvation. Additional identification of digalactosylglycerol (galactolipid breakdown) argues for this hypothesis.

  oligosaccharide, glycan, glycoconjugate, white campion

  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Equipe Polysaccharides Pariétaux des Végétaux, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq Cédex, France, Laboratoire de Chimie-Biologique, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq Cédex, France
  Methods: gel filtration, 1H NMR, FAB-MS, TLC, GLC, permethylation, PE
  
   
  
  Silene alba
  CSDB ID 128195 (all data & tools)
• Article ID: 10051
  Lhernould S, Karamanos Y, Bourgerie S, Strecker G, Julien R, Morvan H "Peptide-N4-(N-acetylglucosaminyl)asparagine amidase (PNGase) activity could explain the occurrence of extracellular xylomannosides in a plant cell suspension" - Glycoconjugate Journal 9 (1992) 191-197
  

  We have previously isolated mannoside and xylomannoside oligosaccharides with one or two terminal reducing N-acetylglucosamine residues from the extracellular medium of white campion (Silene alba) suspension culture. We have now demonstrated the presence of peptide-N4-(N-acetylglucosaminyl)asparagine amidase (PNGase) activity in cell extracts as well in the culture medium that could explain the production of those compounds. An additional xylomannoside, (GlcNAc)Man3(Xyl)GlcNAc(Fuc)GlcNAc, was characterized, and 1H- and 13C-NMR assignments for the oligosaccharide Man3(Xyl)GlcNAc(Fuc)GlcNAc were obtained using homonuclear and heteronuclear spectroscopy (COSY).

  white campion, xylomannoside, PNGase

  NCBI PubMed ID: 1422139
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Laboratoire de Biologie Cellulaire Vegetale et Valorisation des Especes Ligneuses, Université de Limoges, Limoges, France
  Methods: 1H NMR, enzymatic digestion, PPC, 13C
  
   
  
  Silene alba
  CSDB ID 128413 (all data & tools)
• Article ID: 10301
  Ashford D, Dwek RA, Welply JK, Amatayakul S, Homans SW, Lis H, Taylor GN, Sharon N, Rademacher TW "The β-1-2-D-xylose and α-1-3-L-fucose substituted N-linked oligosaccharides from Erythrina crista-galli lectin. Isolation, characterization and comparison with other legume lectins" - European Journal of Biochemistry 166 (1987) 311-320
  

  The carbohydrate moieties of Erythrina cristagalli lectin were released as oligosaccharides by hydrazinolysis, followed by N-acetylation and reduction with NaB3H4. Fractionation of the tritium-labelled oligosaccharide mixture by Bio-Gel P-4 column chromatography and high-voltage borate electrophoresis revealed that it is composed of five neutral oligosaccharides. Structural studies by sequential exoglycosidase digestion in combination with methylation analysis and two-dimensional 1H-NMR showed that the major component was the fucose-containing heptasaccharide Man α 3(Man α 6)(Xyl β 2)Man β 4GlcNAc β 4(Fuc α 3)GlcNAcol. This is the first report of such a structure in plant lectins. Small amounts of the corresponding afucosyl hexasaccharide were also identified, as well as three other minor components. The structure of the heptasaccharide shows the twin characteristics of a newly established family of N-linked glycans, found to date only in plants. The characteristics are substitution of the common pentasaccharide core [Man α 3(Man α 6)Man β 4GlcNAc β 4GlcNAc] by a D-xylose residue linked β1----2 to the β-mannosyl residue and an L-fucose residue linked α1----3 to the reducing terminal N-acetylglucosamine residue. The oligosaccharide heterogeneity pattern for Erythrina cristagalli lectin was also found for the lectins from four other Erythrina species and the lectins of two other legumes, Sophora japonica and Lonchocarpus capassa.

  NCBI PubMed ID: 3609010
  Publication DOI: 10.1111/j.1432-1033.1987.tb13516.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Department of Biochemistry, University of Oxford, Oxford, UK, Department of Biophysics, The Weizmann Institute of Science, Rehovot, Israel
  Methods: gel filtration, 1H NMR, GC-MS, enzymatic digestion, methylation analysis, reduction, PC
  
   
  
  Erythrina crista-galli
  CSDB ID 123040 (all data & tools)
• Article ID: 10683
  Kimura Y, Hase S, Kobayashi Y, Kyogoku Y, Ikenaka T, Funatsu G "Structures of sugar chains of Ricinus communis agglutinin" - Biochimica et Biophysica Acta 966 (1988) 248-256
  

  The structures of sugar chains from Ricinus communis agglutinin were determined. Four glycopeptides were isolated from the lectin according to a published method (Kimura, Y. and Funatsu, G. (1988) Agric. Biol. Chem. 52, in press), and sugar chains of each glycopeptide were liberated by hydrazinolysis. Free amino groups were N-acetylated and the reducing-end residues were coupled with 2-aminopyridine. The resulting pyridylamino derivatives of sugar chains were purified by gel filtration and reversed-phase HPLC. The structures of thus-purified PA-sugar chains were determined by a combination of component analysis, stepwise exoglycosidase digestions, partial acetolysis, and 500 MHz 1H-NMR spectroscopy. These results indicate that R. communis agglutinin contains the sugar chains shown on page 249.

  lectin, glycoprotein, Sugar chain structure, Pyridylamino derivative, Sugar chain processing, Ricinus communis agglutinin

  Publication DOI: 10.1016/0304-4165(88)90118-3
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, Institute for Protein Research, Osaka University, Osaka Japan
  Methods: 1H NMR, HPLC, enzymatic digestion, partial acetolysis, RP-HPLC, CC
  
   
  
  Ricinus communis
  CSDB ID 109196 (all data & tools)
• Article ID: 10688
  Hase S, Koyama S, Daiyasu H, Takemoto H, Hara S, Kobayashi Y, Kyogoku Y, Ikenaka T "Structure of a sugar chain of a protease inhibitor isolated from Barbados pride (Caesalpinia pulcherrima Sw.) seeds" - Journal of Biochemistry 100 (1986) 1-10
  

  An asparagine-linked sugar chain of a protease inhibitor from barbados pride (Caesalpinia pulcherrima Sw.) was liberated by hydrazinolysis. After N-acetylation, the reducing end residue of this carbohydrate unit was coupled with 2-aminopyridine and the pyridylamino (PA-) derivative was purified by gel-filtration and reversed-phase HPLC. The structure of the resulting PA-sugar chain was determined mainly by stepwise exoglycosidase digestions and 500 MHz 1H-NMR spectroscopy and proved to be as follows: (formula; see text).

  NCBI PubMed ID: 3759923
  Journal NLM ID: 0376600
  Publisher: Japanese Biochemical Society
  
   
  
  Caesalpinia pulcherrima
  CSDB ID 132295 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,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_148492,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

• Article ID: 9546
  Takahashi N, Hotta T, Ishihara H, Mori M, Tejima S, Bligny R, Akazawa T, Endo S, Arata Y "Xylose-containing common structural unit in N-linked oligosaccharides of laccase from sycamore cells" - Biochemistry 25(2) (1986) 388-395
  

  The structures of asparagine-linked oligosaccharides of laccase excreted by sycamore (Acer pseudoplatanus L.) cells are reported. Peptic glycopeptides obtained from the laccase were treated with N-oligosaccharide glycopeptidase (EC 3.5.1.52) to release the oligosaccharide moieties. The oligosaccharides thus obtained were fractionated into six components by gel filtration, thin-layer chromatography, and high-performance liquid chromatography. The structures of the isolated oligosaccharides were determined by sugar analysis, exoglycosidase digestion, and methylation analysis in combination with high-resolution proton nuclear magnetic resonance spectroscopy. It was found that (1) the six oligosaccharides are a series of compounds of xylose-containing biantennary complex types that share as the core a common structural unit, i.e., Xyl-β(l-2)[Man-α(l-6)]Man-β(l-4)GlcNAc-β(l-4)[Fuc-α(1-3)]GlcNAc, and (2) mannose, N-acetylglucosamine, galactose, and fucose residues are additionally linked to the core as the outer chain moieties.

  Publication DOI: 10.1021/bi00350a018
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan, Department of Biochemistry, Nagoya City University Medical School, Nagoya, Japan, Centre National de la Recherche Scientifique, CENG, Grenoble, France, Research Institute for Biological Regulation School of Agriculture, Nagoya University, Nagoya, Japan, Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Tokyo, Japan
  Methods: 1H NMR, TLC, acid hydrolysis, HPLC, enzymatic digestion, methylation analysis
  
   
  
  Acer pseudoplatanus
  CSDB ID 107208 (all data & tools)