CSDB: Search results

References to other databases: GTC:G80513FH, CCSD:5808, CBank-STR:14603
Structural formula & atomic coordinates
Sweet-II 3D model
Show glycosyltransferases

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

Suspension-cultured cells of rice secrete α-amylase into the culture medium. It has been shown that the mature form of the α-amylase contains xylose-bearing N-linked oligosaccharide: (formula; see text) We demonstrate that suspension-cultured cells of rice secrete α-amylase containing oligomannose-type oligosaccharides in the presence of 1-deoxymannojirimycin or tris(hydroxymethyl)aminomethane. On the other hand, α-amylase purified from germinated rice seedlings contains several kinds of oligomannose-type and N-acetyllactosamine-type oligosaccharides. The processing pathway of oligosaccharide moieties in rice cells is discussed on the basis of a comparison of these oligosaccharides structures.

NCBI PubMed ID: 2143471
Publication DOI: 10.1111/j.1432-1033.1990.tb19122.x
Journal NLM ID: 0107600
Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Research Institute for Biochemical Regulation, School of Agriculture, Nagoya University, Japan, Department of Agricultural Chemistry, Faculty of Agriculture, Niigata University, Japan, Nagoya City University, College of Nursing, Nagoya, Japan, Faculty of Pharmaceutical Science, University of Tokyo, Japan
Methods: 1H NMR, SDS-PAGE, HPLC, enzymatic digestion, pulse-labeling assay

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

Primary structures of the N-glycans of two major pollen allergens (Lol p 11 and Ole e 1) and a major peanut allergen (Ara h 1) were determined. Ole e 1 and Ara h 1 carried high mannose and complex N-glycans, whereas Lol p 11 carried only the complex. The complex structures all had a β(1,2)-xylose linked to the core mannose. Substitution of the proximalN-acetylglucosamine with an α(1,3)-fucose was observed on Lol p 11 and a minor fraction of Ole e 1 but not on Ara h 1. To elucidate the structural basis for IgE recognition of plantN-glycans, radioallergosorbent test analysis with protease digests of the three allergens and a panel of glycoproteins with knownN-glycan structures was performed. It was demonstrated that both α(1,3)-fucose and β(1,2)-xylose are involved in IgE binding. Surprisingly, xylose-specific IgE antibodies that bound to Lol p 11 and bromelain did not recognize closely related xylose-containing structures on horseradish peroxidase, phytohemeagglutinin, Ole e 1, and Ara h 1. On Lol p 11 and bromelain, the core β-mannose is substituted with just an α(1,6)-mannose. On the other xylose-containingN-glycans, an additional α(1,3)-mannose is present. These observations indicate that IgE binding to xylose is sterically hampered by the presence of an α(1,3)-antenna.

allergy, N-glycans, peanut, pollen, IgE binding

NCBI PubMed ID: 10753962
Publication DOI: 10.1074/jbc.275.15.11451
Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: r_van_ree@clb.nl
Institutions: Department of Allergy, Central Laboratory of The Netherlands Red Cross Blood Transfusion Service and Laboratory for Experimental and Clinical Immunology, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands, Laboratoire des Transports Intracellulaires, CNRS-ESA 6037, Spectrométrie de Masse Bio-organique, Centre Régional Universitaire de Spectroscopie, Institut Fédératif de Recherche Multidisciplinaire sur les Peptides 23, Université de Rouen, Mont Saint Aignan, France, Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense, Madrid, Spain, Toegepast Natuurwetenschappelijk Onderzoek Nutrition and Food Research Institute, Zeist, The Netherlands
Methods: biological assays