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PubMed2006

Parasite glycoconjugates. Part 16: Synthesis of a disaccharide and phosphorylated di- and tri-saccharides from Leishmania lipophosphoglycan.

A neutral disaccharide beta-D-Galp-(1-->4)-alpha-D-Manp and phosphorylated di- and tri-saccharides beta-D-Galp-(1-->3)-[H(2)PO(3)-6]-beta-D-Galp-O[CH(2)](8)CHCH(2) and beta-D-Galp-(1-->3)-[H(2)PO(3)-6]-beta-D-Galp-(1-->4)-alpha-D-Manp, which are fragments of the phosphoglycan portion of the surface lipophosphoglycan from Leishmania donovani (the disaccharide) or Leishmania major (all three compounds), were prepared and used as TLC standards to help the identification and differentiation of the elongating and branching beta-D-galactosyl transferase activities in Leishmania. The phosphosaccharides were synthesised using the H-phosphonate method for phosphorylation.

Animals↗
PubMed2004

Rhodamine B amine as a highly sensitive fluorescence derivatization reagent for saccharides in reversed-phase liquid chromatography.

6-Rhodamine B amine functions as a highly sensitive fluorescence derivatization reagent for mono- and oligosaccharides; it reacts with the reducing end of saccharides under acidic conditions. The fluorescent derivatives of five monosaccharides can be separated within 25 min by reversed-phase liquid chromatography with isocratic elution. The detection limits (S/N = 3) for mono-, di-, and oligosaccharides are 7-51, 13, and 9-35 fmol/20 microl injection, which correspond to analyte concentrations of 35-255, 65, 45-175 nM, respectively. We have applied this derivatization method successfully to the analysis of the components of oligosaccharides in glycoproteins (ribonuclease B and fetuin) following their acidic or enzymatic hydrolysis. The results from these analyses are in good agreements with the reported values established previously.

Carbohydrate Sequence↗
PubMed2005

Surface modification of liposomes by saccharides: vesicle size and stability of lactosyl liposomes studied by photon correlation spectroscopy.

The cell glycocalyx is an attractive model for surface modification of liposomes, because its hydrated oligosaccharide layer inhibits nonspecific protein adsorption and can provide specificity towards desired sites. Here, we report on the use of lactose as a model saccharide to modify the liposome surface and examine the vesicle size and stability. Two kinds of lactosyl lipids, including lactosyl ether-lipid (6a) and lactosyl ester-lipid (6b), which contain octadecyl and octadecanoyl as the lipid tails, respectively, were synthesized and their liposomes were prepared by the extrusion method. The effects of glycolipid structure, concentration, and the pore size of the extrusion membrane on vesicle size and stability were investigated at room temperature by photon correlation spectroscopy (PCS). All liposomes with 5 or 10 mol% of lactosyl lipids had a narrow size distribution and remained stable at room temperature for at least one month, which is comparable to 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC)- and poly(ethylene glycol) (PEG)-liposomes. The maximum incorporation of lactosyl ester-lipid into liposomes was 15 mol%, compared with only 10 mol% for the lactosyl ether-lipid. The lactosyl ester-liposomes had better stability and exhibited less size change than the lactosyl ether-liposomes at 15 or 20 mol% of lactosyl lipids incorporated. This may be attributed to the better structural compatibility of lactosyl ester-lipid with DSPC. The PCS results show that the glycolipid structure and concentrations are major factors that affect vesicle stability, while the pore size of extrusion membranes has no influence.

Carbohydrate Conformation↗
PubMed2006

The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites.

Periplasmic binding proteins (PBPs) comprise a protein superfamily that is involved in prokaryotic solute transport and chemotaxis. These proteins have been used to engineer reagentless biosensors to detect natural or non-natural ligands. There is considerable interest in obtaining very stable members of this superfamily from thermophilic bacteria to use as robust engineerable parts in biosensor development. Analysis of the recently determined genome sequence of Thermus thermophilus revealed the presence of more than 30 putative PBPs in this thermophile. One of these is annotated as a glucose binding protein (GBP) based on its genetic linkage to genes that are homologous to an ATP-binding cassette glucose transport system, although the PBP sequence is homologous to periplasmic maltose binding proteins (MBPs). Here we present the cloning, over-expression, characterization of cognate ligands, and determination of the X-ray crystal structure of this gene product. We find that it is a very stable (apo-protein Tm value is 100(+/- 2) degrees C; complexes 106(+/- 3) degrees C and 111(+/- 1) degrees C for glucose and galactose, respectively) glucose (Kd value is 0.08(+/- 0.03) microM) and galactose (Kd value is 0.94(+/- 0.04) microM) binding protein. Determination of the X-ray crystal structure revealed that this T. thermophilus glucose binding protein (ttGBP) is structurally homologous to MBPs rather than other GBPs. The di or tri-saccharide ligands in MBPs are accommodated in long relatively shallow grooves. In the ttGBP binding site, this groove is partially filled by two loops and an alpha-helix, which create a buried binding site that allows binding of only monosaccharides. Comparison of ttGBP and MBP provides a clear example of structural adaptations by which the size of ligand binding sites can be controlled in the PBP super family.

Amino Acid Sequence↗
PubMed2006

Saccharide-mediated interactions of boar sperm surface proteins with components of the porcine oviduct.

The role of boar seminal plasma proteins attached to the sperm plasma membrane during ejaculation has been studied in saccharide-mediated events in the female reproductive tract. Heparin-binding (Hep(+)) proteins (DQH sperm surface protein, and AQN and AWN spermadhesins) and their aggregated forms (fractions II and III) interacted more strongly with both oviductal epithelium cells and fluid than non-heparin-binding (Hep(-)) proteins (PSP I and PSP II spermadhesins) and their heterodimer (fraction IV), and interactions correlate with affinity of these proteins to yeast mannan. Indirect immunofluorescence (IMF) showed that the AQN 1 spermadhesin and fraction II bind to the apical glycocalyx of the ampulla, as well as the isthmic and uterine tubal junction regions of the oviductal sections. IMF demonstrated the recognition of AQN 1 and fraction II and mannosyl components of oviductal epithelium. We suggest that Hep(+) proteins (especially AQN 1, fraction II) on sperm could enable sperm binding to oviductal epithelium and thus participate in formation of the sperm oviductal reservoir. Interactions of Hep(+) proteins to oviductal epithelium were inhibited by mannan, hyaluronic acid and sialylated O-glycoproteins. No or slight inhibition was observed with sulphated polysaccharides (heparin, chondroitin sulphate) and simple monosaccharides. Besides that, attachment of boar seminal plasma proteins to oviductal epithelium cells was affected by oviductal fluid, the natural environment in the oviduct. Moreover, the ability of hyaluronic acid to inhibit the interaction of sperm surface proteins to the oviduct might play a role in sperm release from the oviductal reservoir and in the capacitation process.

Animals↗
PubMed2003

Physicochemical and saccharide-binding studies on the galactose-specific seed lectin from Trichosanthes cucumerina.

Physicochemical and saccharide-binding studies have been performed on Trichosanthes cucumerina seed lectin (TCSL). The agglutination activity of TCSL is highest in the pH range 8.0-11.0, whereas below pH 7.0 it decreases quite rapidly, which is consistent with the involvement of imidazole side chains of His residues, which titrate in this pH range, in the sugar-binding activity of the lectin. The lectin activity is unaffected between 0 and 60 degrees C, but a sharp decline occurs at higher temperatures. Isoelectric focusing studies show that TCSL has three isoforms with pI values of 5.3, 6.2, and 7.1, with the isoform of pI 6.2 being the most abundant. Circular dichroism spectroscopic studies reveal that TCSL contains about 28.4% beta-sheet, 10.6% beta-turns, 7% polyproline type 2 structure, with the remainder comprising unordered structure; the alpha-helix content is negligible. Binding of 4-methylumbelliferyl-beta-D-galactopyranoside (MeUmbbetaGal) to TCSL results in a significant increase in the fluorescence intensity of the ligand, and this change has been used to obtain the association constant for the interaction. At 25 degrees C, the association constant, K(a), for the TCSL-MeUmbbetaGal interaction was determined as 6.9 x 10(4)M(-1). Binding of nonfluorescent, inhibitory sugars was studied by monitoring their ability to reverse the fluorescence changes observed when MeUmbbetaGal was titrated with TCSL.

Carbohydrate Metabolism↗
PubMed1992

A novel saccharide structure, Xyl 1----3 Gal 1----(SO3-)3,4 Fuc----, is present in acrosome reaction-inducing substance of the starfish, Asterias amurensis.

The jelly coat of echinoderm eggs contains a glycoconjugate, acrosome reaction-inducing substance (ARIS), that is essential for triggering the acrosome reaction in homologous spermatozoa. In the starfish, Asterias amurensis, ARIS is a sulfated glycoprotein of an apparent molecular size of greater than 10(7). Since its biological activity is dependent mostly on its sugar moiety, oligosaccharides liberated by hydrolysis with 10 mM H2SO4 for 60 min at 100 degrees C from pronase digests of ARIS (P-ARIS) were chemically analyzed. The main oligosaccharide purified by high-performance anion-exchange chromatography was determined to be Xyl1----3Gal1----(SO3-)3,4Fuc by compositional analysis and FAB mass spectrometry. This structure indicates that ARIS possesses a novel saccharide chain having sulfated fucose as an internal residue.

Acrosome↗
PubMed2001

Mean square fluctuations of hydrogen atoms and water-biopolymer interactions in hydrated saccharides.

We have used the elastic neutron scattering technique to investigate the dynamics of the two main saccharidic components of starch: amylose and amylopectin. The measurements were carried out in the temperature range of 20 to 320 K and at different hydration levels from the dry state up to 0.47 g saccharide/g D(2)O. In the dry samples, the atomic dynamics is harmonic up to approximately 300 K. In the hydrated samples a "glass-like" transition leading to an anharmonic dynamics is observed. The onset of the anharmonicity occurs at temperatures that increase from approximately 180 K to 260 K upon decreasing hydration from 0.5 to 0.1 g saccharide/g D(2)O. This behavior is qualitatively similar to that observed in hydrated globular proteins, but quantitative differences are present. Assuming a simple asymmetric double-well potential model, the temperature and hydration dependence of the transition have been described in terms of few physical parameters.

Amylopectin↗
PubMed2000

An improved model for calculating the optical rotation of simple saccharides.

A calculational model for the optical rotation (OR) at the sodium D-line of simple saccharides has been developed that eliminates deficiencies of a previous model. Conformational conclusions based on the earlier model are not affected, as established by a recalculation of the OR phi,psi-map of methyl 3-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside. The model relocates the strong long-wavelength sigma-sigma* circular dichroism (CD) component, which is mainly responsible for the NaD OR from 160 to below 130 nm, where it is now known to occur. That correction allows future modeling of CD bands of different origins that appear in the 150-190 nm region. In order to demonstrate the utility of the revised model, it was applied to calculating the OR of methyl 3-O-(alpha-L-rhamnopyranosyl)-alpha-L-rhamnopyranoside. The results provide experimental support for conformational conclusions derived from a molecular mechanics study of that molecule.

Carbohydrates↗
PubMed1976

A general survey of the proton spin-lattice relaxation-times of some oligo- and poly-saccharide derivatives.

A Fourier-transform method has been used to measure the spin-lattice relaxation-times (T1 values) of the anomeric protons of a selection of oligo- and poly-saccharide derivatives. Although systematic variations are found for the substances of lower molecular weight, these variations are essentially non-existent at higher molecular weights. Data for the disaccharides cellobiose, maltose, lactose, gentiobiose, and melibiose demonstrate that proton T1-values may provide a powerful method for evaluating conformations of oligosaccharides.

Electron Spin Resonance Spectroscopy↗
PubMed1978

Action of Pseudomonas isoamylase on various branched oligo and poly-saccharides.

Pseudomonas isoamylase (EC 3.2.1.68) hydrolyzes (1 linked to 6)-alpha-D-glucosidic linkages of amylopectin, glycogen, and various branched dextrins and oligosaccharides. The detailed structural requirements for the substrate are examined qualitatively and quantitatively in this paper, in comparison with the pullulanase of Klebsiella aerogenes. As with pullulanase, Ps. isoamylase is unable to cleave D-glucosyl stubs from branched saccharides. Ps. isoamylase differs from pullulanase in the following characteristics: (1) The favored substrates for Ps. isoamylase are higher-molecular-weight polysaccharides. Most of the branched oligosaccharides examined were hydrolyzed at a lower rate, 10% or less of the rate of hydrolysis of amylopectin. (2) Maltosyl branches are hydrolyzed off by Ps. isoamylase very slowly in comparison with maltotriosyl branches. (3) Ps. isoamylase requires a minimum of three D-glucose residues in the B- or C-chain.

Glycoside Hydrolases↗
PubMed1986

Lysosomal-enzyme targeting: the phosphorylation of synthetic D-mannosyl saccharides by UDP-N-acetyl-glucosamine:lysosomal-enzyme N-acetylglucosamine-phosphotransferase from rat-liver microsomes and fibroblasts.

Phosphorylation of the D-mannose residues of lysosomal enzymes is essential for the uptake and intracellular transport of these enzymes to lysosomes. The GlcNAc-P-transferase which is involved in the phosphorylation reaction seems to recognize a signal, probably a protein conformation, common to many lysosomal enzymes. To evaluate the role of the carbohydrate portion of the enzyme in these phosphorylation reactions, the acceptor specificity of GlcNAc-P-transferase from rat-liver microsomes and fibroblasts was examined with the aid of synthetic D-mannosyl disaccharides and derivatives that are closely related to the high-mannose type of oligosaccharides. Four methyl D-mannobiosides were synthesized, and their structures were established by 13C-n.m.r. spectroscopy. Of all the D-mannosyl saccharides tested, alpha-D-Man-(1----2)-alpha-D-Man-(1----OMe) was found to be the best acceptor, thereby suggesting that oligosaccharide structure may also have a role to play in recognition by this enzyme.

Animals↗
PubMed1992

Stereoselective syntheses of a di-, tri-, and tetra-saccharide fragment of Shigella dysenteriae type 1 O-antigen using 3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-glucopyranosyl chloride as a glycosyl donor.

Methyl 2,4-di-O-benzoyl-alpha-L-rhamnopyranoside (1) furnished a crystalline 3-O-bromoacetyl derivative that was treated with the dichloromethyl methyl ether-ZnCl2 reagent to give 2,4-di-O-benzoyl-3-O-bromoacetyl-alpha-L-rhamnopyranosyl chloride (3). Compounds 1 and 3 were condensed under the conditions of base-deficient, silver trifluoromethanesulfonate-mediated glycosylation to give a fully protected rhamnobioside, which on O-debromoacetylation afforded the disaccharide nucleophile 10. Similar condensation of 3 with methyl 3-O-benzoyl-4,6-O-benzylidene-alpha-D-galactopyranoside, followed by O-debromoacetylation and condensation of the thus formed methyl O-(2,4-di-O-benzoyl-alpha-L-rhamnopyranosyl)-(1----2)-4,6-O-benzylidene- 3-O-benzoyl-alpha-D-galactopyranoside again with 3, gave the trisaccharide glycoside. Subsequent O-debromoacetylation gave 17, having only HO-3(3) unsubstituted. Silver perchlorate-mediated glycosylations of 1, 10, and 17 with 3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-glucopyranosyl chloride afforded, with high alpha stereoselectivity, protected di-, tri-, and tetra-saccharide glycosides. Subsequent hydrogenation, followed by N-acetylation and O-deacylation, afforded three oligosaccharide glycosides having nonreducing terminal 2-acetamido-2-deoxy-alpha-D-glucopyranosyl residues and comprising successively larger portions of the repeating unit of Shigella dysenteriae type 1 O-antigen.

Azides↗
PubMed2001

A very efficient method to cleave Lipid A and saccharide components in bacterial lipopolysaccharides.

A novel mild procedure for the selective cleavage of ketosidic linkages is developed using ceric ammonium nitrate (CAN) in anhydrous N,N-dimethylformamide. Its application to lipopolysaccharides (LPS) is very significant because in the so far investigated LPS, the connection between the Lipid A region and the oligo(poly)saccharide part is always a keto-sugar. This procedure has been tested on LPS of Escherichia coli which contains Kdo as a linker between Lipid A and OPS and on Acinetobacter haemoliticus which contains D-glycero-D-talo-2-octulopyranosonic acid (Ko) as a linker and it performed efficiently in both cases.

Acinetobacter↗
PubMed1994

Synthetic studies toward pyruvate acetal-containing saccharides: en route to the efficient synthesis of Rhizobium-related exopolysaccharide fragments.

The disaccharide building block benzyl O-(2,3-di-O-benzoyl-4,6-O-[(R)-1-(methoxycarbonyl) ethylidene]-beta-D-galactopyranosyl)-(1-->3)-2-O-benzoyl-4,6-O-[(S)-1- (methoxycarbonyl)ethylidene]-alpha-D-glucopyranoside (13), related to a Rhizobium exopolysaccharide, was prepared by coupling various 4,6-O-[(R)-1-(methoxycarbonyl)ethylidene]-D-galactosyl donors (benzoyl-protected chloride 1, pivaloyl-protected chloride 2, and benzoyl-protected fluorides 3 and 4, and trichloroacetimidate 5) with benzyl 2-O-benzoyl-4,6-O-[(S)-1- (methoxycarbonyl)ethylidene]-alpha-D-glucopyranoside (10) and the corresponding 2,3-O-tetraisopropyldisiloxane-protected glucoside 12. The best results, with respect to beta-selectivity and yield of the coupling, were obtained with 5 and 10 in dichloromethane. The beta-linked (13) and alpha-linked (14) disaccharides were efficiently converted via the 1-OH derivatives 17 and 21 into the corresponding trichloroacetimidates 18 and 22. The latter were used for the synthesis of the disaccharide ligands 4,6-(R)-pyruvate-beta-D-Galp-(1-->3)-4,6-(S)-pyruvate-beta-D-Glcp-O(CH2) 5NH2 (20), and 4,6-(R)-pyruvate-alpha-D-Galp-(1-->3)-4,6-(S)-pyruvate-beta-D-Glcp-O (CH2)5NH2 (24). The corresponding tri- and tetra-saccharide derivatives 4,6-(R)-pyruvate-beta-D-Galp-(1-->3)-4,6-(S)-pyruvate-beta-D-Glcp-(1-->4 )-beta- D-Glcp-O(CH2)5NH2 (28) and 4,6-(R)-pyruvate-beta-D-Galp-(1-->3)-4,6-(S)-pyruvate-beta-D-Glcp-(1-->4 )-beta- D-Glcp-(1-->4)-beta-D-Glcp-O(CH2)25NH2 (36) were obtained similarly.

Carbohydrate Conformation↗
PubMed1996

The use of 2-deoxy-2-trichloroacetamido-D-glucopyranose derivatives in syntheses of hyaluronic acid-related tetra-, hexa-, and octa-saccharides having a methyl beta-D-glucopyranosiduronic acid at the reducing end.

Expeditious and stereocontrolled syntheses are reported of beta-D-Glc pNAc-(1-->4)-[beta-D-Glc pA-(1-->3)-beta-D-Glc pNAc-(1-->4)]n-beta-D-Glc pA-(1-->OMe), where n = 1, 2, and 3, which represent structural elements of the extracellular polysaccharide hyaluronic acid. Condensation of 4,6-O-benzylidene-3-O-chloroacetyl-2-deoxy-2-trichloroacetamido- alpha-D-glucopyranosyl trichloroacetimidate with methyl (4-methoxyphenyl 2,3-di-O-benzoyl-beta-D-glucopyranosid)uronate gave the disaccharide derivative 9, which was demethoxyphenylated and imidoylated to afford the pivotal disaccharide trichloroacetimidate 7. Condensation of 7 with methanol followed by O-dechloroacetylation gave the acceptor 8. Coupling of 7 with 8 gave the tetrasaccharide derivative 4. O-Dechloroacetylation of 4 followed by condensation with imidate 7 afforded hexasaccharide 5, which was transformed into octasaccharide 6 by a similar two-step procedure. Subsequent O-dechloroacetylation, transformation of the N-trichloroacetyl groups into N-acetyl, debenzylidenation, and saponification of 4-6 afforded the tetra- (1), hexa- (2), and octa-saccharide (3) derivatives in high yields, as their sodium salts.

Carbohydrate Conformation↗
PubMed2003

2-amino-3-phenylpyrazine, a sensitive fluorescence prelabeling reagent for the chromatographic or electrophoretic determination of saccharides.

2-Amino-3-phenylpyrazine is found to be a sensitive fluorescence labeling reagent for saccharides with a reducing end. The labeled monosaccharides show strong fluorescence under various pH conditions, and could be analyzed by both HPLC and HPCE techniques. Laser induced fluorescence detection is also applicable. Following derivatization with 2-amino-3-phenylpyrazine, six monosaccharides are separated by an HPCE system within 23 min in the calibration range of 5 or 10 fmol to 5 pmol (injection amount). The within-day and day-to-day precisions of the monosaccharide determinations are 3.83-4.86% (RSD) and 3.37-4.56% (RSD), respectively. This method was successfully applied to the determination of component monosaccharides in a glycoprotein, bovine serum fetuin.

Amines↗
PubMed2003

Overexpression of GDP-mannose pyrophosphorylase in Saccharomyces cerevisiae corrects defects in dolichol-linked saccharide formation and protein glycosylation.

Thermosensitive mutants of Saccharomyces cerevisiae, affected in the endoplasmic reticulum (ER) located glycosylation, i.e. in Dol-P-Man synthase (dpm1), in beta-1,4 mannosyl transferase (alg1) and in alpha-1,3 mannosyltransferase (alg2), were used to assess the role of GDP-Man availability for the synthesis of dolichol-linked saccharides. The mutants were transformed with the yeast gene MPG1 (PSA1/VIG9) encoding GDP-Man pyrophosphorylase catalyzing the final step of GDP-Man formation. We found that overexpression of MPG1 allows growth at non-permissive temperature and leads to an increase in the cellular content of GDP-Man. In the alg1 and alg2 mutants, complemented with MPG1 gene, N-glycosylation of invertase was in part restored, to a degree comparable to that of the wild-type control. In the dpm1 mutant, the glycosylation reactions that depend on the formation of Dol-P-Man, i.e. elongation of Man(5)GlcNAc(2)-PP-Dol, O-mannosylation of chitinase and synthesis of GPI anchor were normal when MPG1 was overexpressed. Our data indicate that an increased level of GDP-Man is able to correct defects in mannosylation reactions ascribed to the ER and to the Golgi.

Blotting, Northern↗