8 results on '"Vliegenthart, Johannes F. G."'
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2. The Giardia intestinalis filamentous cyst wall contains a novel beta(1-3)-N-acetyl-D-galactosamine polymer: a structural and conformational study.
- Author
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Gerwig, Gerrit J, van Kuik, J Albert, Leeflang, Bas R, Kamerling, Johannis P, Vliegenthart, Johannes F G, Karr, Craig D, and Jarroll, Edward L
- Abstract
Assembly of a protective cyst wall by Giardia is essential for the survival of the parasite outside the host intestine and for transmission among susceptible hosts. The structure of the G. intestinalis filamentous cyst wall was studied by chemical methods, mass spectrometry, and (1)H nuclear magnetic resonance spectroscopy. Isolated cyst wall material contains carbohydrate and protein in a ratio of 3:2 (w/w), and the carbohydrate moiety is composed of a beta(1-3)-N-acetyl-D-galactopyranosamine homopolymer. Conformational analysis by molecular dynamics and persistence length calculations of GalNAc oligomers in solution demonstrated a flexible structure consisting of left- and right-handed helical elements. It is most likely that in the solid state, the polysaccharide forms ordered helices or possibly multiple helical structures having strong interchain interactions. The highly insoluble nature of the Giardia cyst wall must be due to these strong interchain interactions and, probably, a strong association between the carbohydrate and the protein moiety.
- Published
- 2002
- Full Text
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3. Symbol Nomenclature for Graphical Representations of Glycans.
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Varki, Ajit, Cummings, Richard D., Aebi, Markus, Packer, Nicole H., Seeberger, Peter H., Esko, Jeffrey D., Stanley, Pamela, Hart, Gerald, Darvill, Alan, Kinoshita, Taroh, Prestegard, James J., Schnaar, Ronald L., Freeze, Hudson H., Marth, Jamey D., Bertozzi, Carolyn R., Etzler, Marilynn E., Frank, Martin, Vliegenthart, Johannes F. G., Lütteke, Thomas, and Perez, Serge
- Published
- 2015
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4. Identification of carbohydrates binding to lectins by using surface plasmon resonance in combination with HPLC profiling
- Author
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Gutiérrez Gallego, Ricardo, Haseley, Simon R., van Miegem, Vincent F. L., Vliegenthart, Johannes F. G., and Kamerling, Johannis P.
- Abstract
A new, powerful method is presented for screening the binding in real time and taking place under dynamic conditions of oligosaccharides to lectins. The approach combines an SPR biosensor and HPLC profiling with fluorescence detection, and is applicable to complex mixtures of oligosaccharides in terms of ligand-fishing. Labeling the oligosaccharides with 2-aminobenzamide ensures a detection level in the fmol range. In an explorative study the binding of RNase B-derived oligomannose-type N-glycans to biosensor-immobilized concanavalin A (Con A) was examined, and an affinity ranking could be established for Man
5 GlcNAc2 to Man9 GlcNAc2 , as monitored by HPLC. In subsequent experiments and using well-defined labeled as well as nonlabeled oligosaccharides, it was found that the fluorescent tag does not interfere with the binding and that the optimum epitope for the interaction with Con A comprises the tetramannoside unit Manα2Manα6(Manα3)Man[D3 B(A)4′], rather than the generally accepted trimannoside Manα6 (Manα3)Man [B(A)4′ or 4(4′)3]. In a similar experimental setup, the interaction of various fucosylated human milk oligosaccharides with the fucose-binding lectin from Lotus tetragonolobus purpureaus was studied, and it appeared that oligosaccharides containing blood group H could selectively be retained and eluted from the lectin-coated surface. Finally, using the same lectin and a mixture of O-glycans derived from bovine submaxillary gland mucin, minor constituents but containing fucose could selectively be picked from the analyte solution as demonstrated by HPLC profiling.- Published
- 2004
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5. The structure of cell wall alpha-glucan from fission yeast.
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Grün CH, Hochstenbach F, Humbel BM, Verkleij AJ, Sietsma JH, Klis FM, Kamerling JP, and Vliegenthart JF
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- Carbohydrate Sequence, Cell Wall genetics, Cell Wall ultrastructure, Glucans genetics, Glucose metabolism, Magnetic Resonance Spectroscopy, Microscopy, Electron, Transmission, Molecular Sequence Data, Mutation genetics, Schizosaccharomyces genetics, Schizosaccharomyces ultrastructure, Cell Wall chemistry, Glucans chemistry, Schizosaccharomyces chemistry, Schizosaccharomyces cytology
- Abstract
Morphology and structural integrity of fungal cells depend on cell wall polysaccharides. The chemical structure and biosynthesis of two types of these polysaccharides, chitin and (1-->3)-beta-glucan, have been studied extensively, whereas little is known about alpha-glucan. Here we describe the chemical structure of alpha-glucan isolated from wild-type and mutant cell walls of the fission yeast Schizosaccharomyces pombe. Wild-type alpha-glucan was found to consist of a single population of linear glucose polymers, approximately 260 residues in length. These glucose polymers were composed of two interconnected linear chains, each consisting of approximately 120 (1-->3)-linked alpha-d-glucose residues and some (1-->4)-linked alpha-D-glucose residues at the reducing end. By contrast, alpha-glucan of an alpha-glucan synthase mutant with an aberrant cell morphology and reduced alpha-glucan levels consisted of a single chain only. We propose that alpha-glucan biosynthesis involves an ordered series of events, whereby two alpha-glucan chains are coupled to create mature cell wall alpha-glucan. This mature form of cell wall alpha-glucan is essential for fission-yeast morphogenesis.
- Published
- 2005
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6. Influence of lactation parameters on the N-glycosylation of recombinant human C1 inhibitor isolated from the milk of transgenic rabbits.
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Koles K, van Berkel PH, Mannesse ML, Zoetemelk R, Vliegenthart JF, and Kamerling JP
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- Animals, Animals, Genetically Modified, Carbohydrate Conformation, Carbohydrate Sequence, Complement C1 Inactivator Proteins, Complement C1 Inhibitor Protein, Female, Glycoproteins chemistry, Glycoproteins isolation & purification, Glycosylation, Humans, Mammary Glands, Animal physiology, Molecular Sequence Data, Rabbits, Recombinant Proteins chemistry, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Serpins isolation & purification, Glycoproteins metabolism, Lactation physiology, Milk chemistry, Serpins chemistry, Serpins metabolism
- Abstract
The large-scale production of recombinant biopharmaceutical glycoproteins in the milk of transgenic animals is becoming more widespread. However, in comparison with bacterial, plant cell, or cell culture production systems, little is known about the glycosylation machinery of the mammary gland, and hence on the glycosylation of recombinant glycoproteins produced in transgenic animals. Here the influence is presented of several lactation parameters on the N-glycosylation of recombinant C1 inhibitor (rhC1INH), a human serum glycoprotein, expressed in the milk of transgenic rabbits. Enzymatically released N-glycans of series of rhC1INH samples were fluorescently labeled and fractionated by HPLC. The major N-glycan structures on rhC1INH of pooled rabbit milk were similar to those on native human C1 inhibitor and recombinant human C1 inhibitor produced in transgenic mouse milk, with only the degree of sialylation and core fucosylation being lower. Analyses of individual animals furthermore showed slight interindividual differences; a decrease in the extent of sialylation, core fucosylation, and oligomannose-type glycosylation with the progress of lactation; and a positive correlation between expression level and oligomannose-type N-glycan content. However, when large quantities of rhC1INH were isolated for preclinical and clinical studies, highly consistent N-linked glycan profiles and monosaccharide compositions were found.
- Published
- 2004
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7. Donor specificity in the glycosylation of Tamm-Horsfall glycoprotein: conservation of the Sda determinant in pairs of twins.
- Author
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Rohfritsch PF, Rinnbauer M, Vliegenthart JF, and Kamerling JP
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- Amino Acid Motifs, Chromatography, High Pressure Liquid, Female, Glycoside Hydrolases metabolism, Glycosylation, Humans, Male, Mucoproteins isolation & purification, Mucoproteins urine, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Substrate Specificity, Uromodulin, Conserved Sequence, Mucoproteins chemistry, Mucoproteins metabolism, Protein Processing, Post-Translational
- Abstract
The content of the Sd(a) determinant in urinary human Tamm-Horsfall glycoprotein (THp) has been reported to be donor-specific. This feature was further addressed by investigating THp from genetically identical individuals. To this end, THp was isolated from the urine of two monozygotic pairs of twins (A and B). The four samples (THp A1, A2, B1, and B2) were subjected to endo-beta-galactosidase from Bacteroides fragilis leading to the liberation of the Neu5Ac(alpha2-3)Gal (beta1-4)GlcNAc(beta1-3)Gal and Neu5Ac(alpha2-3)[GalNAc(beta1-4)] Gal(beta1-4)GlcNAc(beta1-3)Gal (Sd(a) epitope) motifs, both located at the nonreducing termini of complex type N-glycans. The isolated mixtures of oligosaccharides were analyzed for the absolute and relative amounts of the two oligosaccharides. The obtained data clearly indicate that in THp A1 and A2, and in THp B1 and B2, the molar ratios of the tetra- and Sd(a) pentasaccharide are identical for a pair of twins. This conservation of molar ratios points to an identical relative expression of beta-1,4-N-acetylgalactosaminyltransferase activity involved in the biosynthesis of the Sd(a) determinant. Apparently, the degree of conversion of the tetrasaccharidic Sd(a) precursor into the final pentasaccharidic Sd(a) form can be considered to result from a very closely related pattern of glycosylation for genetically homogeneous individuals.
- Published
- 2004
- Full Text
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8. N- and O-glycans of recombinant human C1 inhibitor expressed in the milk of transgenic rabbits.
- Author
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Koles K, van Berkel PH, Pieper FR, Nuijens JH, Mannesse ML, Vliegenthart JF, and Kamerling JP
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- Animals, Animals, Genetically Modified, Carbohydrate Conformation, Carbohydrate Sequence, Chromatography, High Pressure Liquid methods, Complement C1 Inactivator Proteins chemistry, Complement C1 Inactivator Proteins isolation & purification, Female, Humans, Mammary Glands, Animal physiology, Molecular Sequence Data, Oligosaccharides chemistry, Rabbits, Recombinant Proteins chemistry, Recombinant Proteins isolation & purification, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Complement C1 Inactivator Proteins genetics, Milk chemistry, Polysaccharides chemistry, Recombinant Proteins metabolism
- Abstract
Human C1 inhibitor (hC1INH) is a therapeutic N, O-glycoprotein with a growing number of clinical applications, but the current natural supplies are not likely to meet the clinical demands. Therefore, recombinant approaches are of interest, whereby specific attention has to be paid to the generated glycosylation patterns. Here, the N,O-glycoprotein was expressed in the mammary gland of transgenic rabbits and subjected to glycan analysis. After release of the N-glycans of recombinant-rabbit human C1 inhibitor (rhC1INH) by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F, the oligosaccharides were separated from the O-glycoprotein by centrifugal filtration, then fractionated by a combination of anion-exchange, normal-phase, and high-pH anion-exchange liquid chromatography. The O-glycans, released from the O-glycoprotein by alkaline borohydride treatment, were fractionated by anion-exchange high-performance liquid chromatography (HPLC). The structures of individual components were analysed by 500 MHz 1H NMR spectroscopy, in most cases combined with MALDI-TOF MS. In contrast to the structural data reported for native serum hC1INH, rhC1INH contained a broad array of different N-glycans, made up of oligomannose-, hybrid-, and complex-type structures. In the case of complex-type N-glycans (partially) (alpha2-6)-sialylated (N-acetylneuraminic acid only), mono- and diantennary chains were found; part of the diantennary structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the lower or upper antenna (Lewis x). The manno-oligosaccharide pattern of part of the hybrid- and oligomannose-type structures indicates that besides the usual N-glycan processing route, also the alternative endo-mannosidase pathway is followed. The small core 1-type O-glycans showed the usual (alpha2-3)- and (alpha2-6)-sialylation pattern of O-glycoproteins of nonmucinous origin.
- Published
- 2004
- Full Text
- View/download PDF
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