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PubMed1999

Protein conjugates of synthetic saccharides elicit higher levels of serum IgG lipopolysaccharide antibodies in mice than do those of the O-specific polysaccharide from Shigella dysenteriae type 1.

Our development of vaccines to prevent shigellosis is based on the hypothesis that a critical (protective) level of serum IgG to the O-specific polysaccharide (O-SP) domain of Shigella lipopolysaccharide (LPS) confers immunity. The O-SP is a hapten and must be conjugated to a protein to induce serum antibodies. The O-SP of Shigella dysenteriae type 1 (approximately 27 tetrasaccharide repeat units), prepared by acid hydrolysis of the LPS, was bound to human serum albumin (HSA) by multiple point attachment (O-SP-HSA): The molar ratio of HSA to O-SP was 1.0. Synthetic saccharides, composed of one or multiples of the O-SP tetrasaccharide, equipped with a spacer at their reducing end, were bound to HSA by a single point attachment: The average molar ratios of the saccharides to HSA ranged from 4 to 24. Serum IgG anti-LPS, elicited in mice by O-SP-HSA or synthetic tetra-, octa-, dodeca-, and hexadecasaccharide fragments, was measured by ELISA. Outbred 6-week-old female mice were injected s.c. three times at biweekly intervals with 2.5 micrograms of saccharide as a conjugate and were bled 7 days after the second and third injections. Excepting the tetramer, conjugates of the octamer, dodecamer and hexadecamer elicited IgG LPS antibodies after the second injection, a statistically significant rise (booster) after the third injection, and higher levels than those vaccinated with O-SP-HSA (P = 0.0001). The highest geometric mean levels of IgG anti-LPS were elicited by the hexadecamer with 9 chains or 9 moles of saccharide/HSA (15.5 ELISA units) followed by the octamer with 20 chains (11.1 ELISA units) and the dodecamer with 10 chains (9.52 ELISA units). Clinical evaluation of these synthetic saccharides bound to a medically useful carrier is planned.

Animals↗
PubMed1986

Identification of the tryptophan residue located at the low-affinity saccharide binding site of ricin D.

The saccharide binding ability of the low affinity (LA-) binding site of ricin D was abrogated by N-bromosuccinimide (NBS)-oxidation, while in the presence of lactose the number of tryptophan residues eventually oxidized decreased by 1 mol/mol and the saccharide binding ability was retained (Hatakeyama et al., (1986) J. Biochem. 99, 1049-1056). Based on these findings, the tryptophan residue located at the LA-binding site of ricin D was identified. Two derivatives of ricin D which were modified with NBS in the presence and absence of lactose were separated into their constituent polypeptide chains (A- and B-chains), respectively. The modified tryptophan residue or residues was/were found to be contained in the B-chain, but not in the A-chain. From lysylendopeptidase and chymotryptic digests, peptides containing oxidized tryptophan residues were isolated by gel filtration on Bio-Gel P-30 and HPLC. Analysis of the peptides containing oxidized tryptophan revealed that three tryptophan residues at positions 37, 93, and 160 on the B-chain were oxidized in the inactive derivative of ricin D, in which the saccharide binding ability of the LA-binding site was abrogated by NBS-oxidation. On the other hand, the modified residues were determined to be tryptophans at positions 93 and 160 in the active derivative of ricin D which was modified in the presence of lactose, indicating that upon binding with lactose, the tryptophan residue at position 37 of the B-chain was protected from NBS-oxidation. From these results, it is suggested that tryptophan at position 37 on the B-chain is the essential residue for saccharide binding at the LA-binding site of ricin D.

Amino Acids↗
PubMed1999

Structure of basic winged-bean lectin and a comparison with its saccharide-bound form.

The crystal structure of the saccharide-free form of the basic form of winged-bean agglutinin (WBAI) has been solved by the molecular-replacement method and refined at 2.3 A resolution. The final R factor is 19.7% for all data in the resolution range 8.0-2.3 A. The asymmetric unit contains two half-dimers, each located on a crystallographic twofold axis. The structure of the saccharide-free form is compared with that of the complex of WBAI with methyl-alpha-D-galactoside. The complex is composed of two dimers in the asymmetric unit. The intersubunit interactions in the dimer are nearly identical in the two structures. The binding site of the saccharide-free structure contains three ordered water molecules at positions similar to those of the hydroxyl groups of the carbohydrate which are hydrogen bonded to the protein. Superposition of the saccharide-binding sites of the two structures shows that the major changes involve expulsion of these ordered water molecules and a shift of about 0.6 A of the main-chain atoms of the variable loop.

Binding Sites↗
PubMed1985

Primary structures and Lewis blood-group-dependent expression of major sialylated saccharides from mucus glycoproteins of human seminal plasma.

The primary structures of four major sialylated saccharide alditols derived from mucus glycoproteins of human seminal plasma were established by fast-atom-bombardment mass spectrometry and methylation analysis. Anomeric configurations of the glycosidic bonds were determined by exoglycosidase digestion and CrO3 oxidation. (Formula: see text) Two minor components represent isomers of the major saccharide in A6, which are probably characterized by terminal sequences NeuAc(2----3)Gal(1----4)[Fuc(1----3)]GlcNAc(1---- and Fuc(1----2)Gal(1----4)[NeuAc(2----6)]GlcNAc(1----, respectively. Based on quantitative data from high-pressure liquid chromatography and on structural information, the biosynthetic pathways for neutral and sialylated saccharides related to the Lewis system were proposed. Expression of saccharides A6, A7 and A8 and their asialo counterparts, which are characterized by antigenic determinants H, Lex and Ley, respectively, is qualitatively and quantitatively dependent on the Lewis blood type of the respective donor and correlates with Ca 19-9 activity of its seminal plasma.

Carbohydrate Sequence↗
PubMed1991

Effect of carrier priming on immunogenicity of saccharide-protein conjugate vaccines.

Previous studies with saccharide-protein conjugates have demonstrated that antibody responses to the saccharide can be improved by the preexistence of carrier immunity. Here we report that prior exposure to the carrier protein can either enhance or suppress antibody response to polysaccharides administered in saccharide-protein conjugates. A dose-dependent role for carrier priming in the antisaccharide antibody response to three saccharide-protein conjugate vaccines, i.e., a Streptococcus pneumoniae type 4 polysaccharide-tetanus toxoid (TT) conjugate (PS4TT), a Neisseria meningitidis group C polysaccharide-TT conjugate (MenCTT), and a N. meningitidis group C oligosaccharide-diphtheria mutant toxin conjugate (MenCCRM), was investigated. The results showed that an increase in the antipolysaccharide antibody response could be obtained for both PS4TT and MenCTT but not for MenCCRM with low-dose carrier priming (0.025 to 0.25 microgram). However, suppression of the antipolysaccharide antibody response was observed with the PS4TT and MenCTT vaccines with high-dose (25-micrograms) carrier priming. There was no suppression effect with MenCCRM. The increase in the antipolysaccharide antibody response was shown to be restricted to the immunoglobulin G1 (IgG1) subclass, whereas suppression with high-dose carrier priming affected all antipolysaccharide subclass antibodies induced by PS4TT (IgG1, IgG2b, and IgG3) and only two of the four subclass antibodies induced by MenCTT (IgG2a and IgG2b). The increase in the antipolysaccharide antibody response was also present at the antipolysaccharide IgM antibody level but was not observed at the anti-carrier IgG antibody level.

Animals↗
PubMed1978

The nuclear magnetic resonance determination of the conformation of saccharides bound in subsite D of lysozyme.

The binding of the trisaccharide (2-acetamido-2-deoxy-D-muramic acid)-beta(1 leads to 4)-(2-aceta-mido-2-deoxy-D-glucosyl)-beta(1 leads to 4)-(2-acetamido-2-deoxy-D-muramic acid) to subsites B, C, and D in lysozyme has been studied by 1H nuclear magnetic resonance methods. In particular, the coupling constant between H1 and H2 of the reducing saccharide bound in subsite D has been determined. The coupling constant for the bound saccharide indicates that the dihedral angle between C1 and C2 for the reducing saccharide is not significantly changed upon binding to lysozyme. This result is discussed in terms of other evidence for the role of distortion of the saccharide bound in subsite D in the lysozyme-catalyzed hydrolysis of cell wall oligosaccharides.

Binding Sites↗
PubMed2005

Suppressive effect of trehalose on acrylamide formation from asparagine and reducing saccharides.

The influence of saccharides on the formation of acrylamide (AcA) was investigated. The reducing saccharides reacted with asaparagine to form AcA, but the non-reducing saccharides, except sucrose, gave no AcA. AcA formation from a mixture containing glucose and asaparagaine was suppressed by the non-reducing saccharides, especially trehalose (76% suppression) and neotrehalose (75% suppression). Glucose is heat-degraded into pyruvaldehyde and 5-hydroxymethyl-2-furfural in the water system. The degradation products react with asparagines to generate AcA. Trehalose appears to inhibit not only the formation of these intermediates and asparagines for AcA, but also the AcA formation from these intermediates.

Acrylamide↗
PubMed2005

[Dynamic change of soluble saccharides and amino acids during the growing period of Coptis chinensis].

OBJECTIVE: To study the changes of soluble saccharides and amino acids during the growing period of Coptis chinensis. METHOD: Amino acid contents were estimated by Indene tri-ketone colorimetric method; saccharide contents were determined by anthracene ketone method. RESULT AND CONCLUSION: The contents of soluble saccharides and amino acids in different organs were low in plants of 1-2 years old. And they were increased in plants of 3-4 years old. At maturation (5 years), the contents of amino acids kept on increasing in rhizome and flower stalk, while decreased in fibre and leaves, and the contents of soluble saccharides showed the downtrend in rhizome, leaves and fibre, except the uptrend in flower stalk.

Amino Acids↗
PubMed1991

Protection against Candida albicans gastrointestinal colonization and dissemination by saccharides in experimental animals.

Pre- or post-treatment of duodenal discs with mannose, N-acetylglucosamine or chitin soluble extracts (CSE) prevented the adherence of Candida albicans to gastrointestinal tract. CSE was the most effective in blocking the adherence of C. albicans. Treatment of infant mice with saccharides significantly reduced the systemic spread of C. albicans inoculated into the gut. The best protection was obtained when the saccharides were given 2 days prior to the infection and continued over the course of the infection. However, systemic spread was reduced with a single dose of saccharide 30 min before infection. The saccharides may bind to the gastrointestinal mucosa and block the attachment of C. albicans.

Acetylglucosamine↗
PubMed1982

Lipid-bound saccharides in Rhizobium meliloti.

The lipid-bound saccharides formed by incubation of uridine diphosphate glucose with a particulate enzyme of Rhizobium meliloti were studied. They behaved like polyprenyl diphosphate saccharides when treated with ammonia or hot phenol, when catalytically hydrogenated, and on DEAE-cellulose chromatography. The saccharide moieties obtained after heating at pH 2 for 10 min at 100 degrees C were separated with a gel filtration column. The following compounds were detected: galactose, glucosyl beta 1-3 galactose (Tolmasky, M. E., Staneloni, R. J., Ugalde, R. A., and Leloir, L. F. (1980) ARch. Biochem. Biophys. 203, 358-364), and some octasaccharides (I). These were compared by paper electrophoresis, thin layer and paper chromatography with an octasaccharide obtained from Alcaligenes faecalis var. myxogenes strain 11 (II). Furthermore, Compounds I and II were compared with the exopolysaccharide of Rhizobium meliloti (III) by partial acid hydrolysis and methylation analysis. The results were consistent with the identity of the repeating unit of Compound III with Compounds I and II except for differences in the substituents (acetyl or succinyl). Studies on the labeling of the lipid-bound saccharides have shown that the sequence is: first, galactose and glucosyl beta 1-3 galactose, then the rest of glucose residues, and finally, the substituents (acetyl and pyruvic acid).

Chromatography, Paper↗
PubMed1999

Effect of temperature on the saccharide composition obtained after alpha-amylolysis of starch

The hydrolysis of starch to low-molecular-weight products (normally characterised by their dextrose equivalent (DE), which is directly related to the number-average molecular mass) was studied at different temperatures. Amylopectin potato starch, lacking amylose, was selected because of its low tendency towards retrogradation at lower temperatures. Bacillus licheniformis alpha-amylase was added to 10% [w/w] gelatinised starch solutions. The hydrolysis experiments were done at 50, 70, and 90 degrees C. Samples were taken at defined DE values and these were analysed with respect to their saccharide composition. At the same DE the oligosaccharide composition depended on the hydrolysis temperature. This implies that at the same net number of bonds hydrolysed by the enzyme, the saccharide composition was different. The hydrolysis temperature also influenced the initial overall molecular-weight distribution. Higher temperatures led to a more homogenous molecular weight distribution. Similar effects were observed for alpha-amylases from other microbial sources such as Bacillus amyloliquefaciens and Bacillus stearothermophilus. Varying the pH (5.1, 6.2, and 7.6) at 70 degrees C did not significantly influence the saccharide composition obtained during B. licheniformis alpha-amylase hydrolysis. The underlying mechanisms for B. licheniformis alpha-amylase were studied using pure linear oligosaccharides, ranging from maltotriose to maltoheptaose as substrates. Activation energies for the hydrolysis of individual oligosaccharides were calculated from Arrhenius plots at 60, 70, 80, and 90 degrees C. Oligosaccharides with a degree of polymerisation exceeding that of the substrate could be detected. The contribution of these oligosaccharides increased as the degree of polymerisation of the substrate decreased and the temperature of hydrolysis increased. The product specificity decreased with increasing temperature of hydrolysis, which led to a more equal distribution between the possible products formed. Calculations with the subsite map as determined for the closely related alpha-amylase from B. amyloliquefaciens reconfirmed this finding of a decreased substrate specificity with increased temperature of hydrolysis. Copyright 1999 John Wiley & Sons, Inc.

Journal Article↗
PubMedDate not supplied

Study of chemobiological reactions. 1. Selectivity of aromatic amino compounds and saccharides in glycosylation reactions.

The reactivities between saccharides and primary amino compounds were studied by liquid chromatography on an amino-bonded column and by measurement of the reaction rates of aromatic amines with saccharides. The recoveries from the column and the reaction rates were correlated with their physicochemical properties calculated by the CAChe program. The reactivities between amines and saccharides correlated well with their hydrogen bonding energies calculated by molecular mechanics.

Amines↗
PubMed2003

Efficient transport of saccharides through a liquid membrane mediated by a cyclodextrin dimer.

A new efficient system for transporting saccharides through a liquid membrane has been constructed. The transport rates of saccharides were accelerated greatly by the cyclodextrin dimer 2; by contrast, the corresponding cyclodextrin monomer 1 was not effective at mediating saccharide transport. The transport rate of D-ribose through a chloroform liquid membrane was 17 times faster when the cyclodextrin dimer 2 was used as the transporter than when the cyclodextrin monomer 1 was used. Similarly the transport rate of methyl D-galactopyranoside was 16 times faster by 2 than by 1.

Biological Transport↗
PubMed2006

Helix formation in synthetic polymers by hydrogen bonding with native saccharides in protic media.

Water-soluble poly(m-ethynylpyridine)s were designed to realize saccharide recognition in protic media. UV/Vis, 1H NMR, and fluorescence measurements revealed that the polymer forms a helical higher order structure by solvophobic interactions between the ethynylpyridine units in the protic medium. The resulting pore in the helix behaves like a binding pocket in proteins, by taking advantage of inwardly directed hydrogen-bonding functional groups of the polymers. Molecular recognition of native saccharides by the polymers was investigated by circular dichroism (CD). The chirality of the saccharide was transferred to the helical sense of the polymers, accompanied by the appearance of induced CDs (ICDs) in the absorptive region of the polymers. In MeOH/water (10/1), mannose and allose showed intense ICDs, and the apparent association constant between the polymer and D-mannose was 14 M(-1).

Carbohydrate Conformation↗
PubMed1976

Humoral reactions in syngeneic hosts against tumor cell surface incomplete saccharide moieties.

Components on the surface of MM2 ascites mammary carcinoma cells induce agglutination factors in the serum of syngeneic host C3H/He mice, and bind the factors in vitro. These components have been classified into three groups: MM2-specific substances, mammary tumor virus (MTV)-associated substances and tumor-associated embryonic materials. The substances contained saccharide moieties and their terminal sugar residues were essential for the binding of the serum factors. These terminal saccharides were exposed during cell proliferation,but masked in stationary cells, at least partly, due to elongation of the saccahride moieits. The terminal structures of these polysaccharide moities of growing and stationary cells were studied by semiquantitative tumor cell agglutination using the agglutinating activities against MM2 cells of MM2-regressor serum and of FMA/R- and Ehrlich-regressor sera which had partial cross-agglutination activities. Agglutination by phytohemagglutinins, inhibition of the agglutination by saccharides or with isolated cell surface components and treatment of the cells with glycosidases were also used for this purpose.

Agglutination↗
PubMed1979

Lipid-saccharide intermediates and glycoprotein biosynthesis in a temperature-sensitive Chinese hamster cell mutant.

The characterization of a temperature-sensitive Chinese hamster cell mutant has been continued with the aim of localizing the apparent defect in glycoprotein synthesis (Tenner et al., '77). Although the mutation is lethal, a demonstration of the ability of the mutant cells to support proliferation of Mengo virus at the nonpermissive temperature indicates that the general metabolic processes of the cells remain intact at a time when glycoprotein synthesis is severely depressed. A quantitative study of protein synthesis on membrane-associated polysomes suggests that the synthesis of the polypeptide portion of the glycoproteins at 40.8 degrees C may be normal. The investigation of lipid-saccharide molecules which have been implicated in the formation and transfer of the oligosaccharide "core" to polypeptide acceptors shows that mutant cells at the nonpermissive temperature are capable of synthesizing these lipid saccharides normally, and that the pool of the dolichyl oligosaccharides is maintained at a constant level independent of the temperature. The rate of formation of the lipid-oligosaccharide, however, is reduced in intact mutant cells at the nonpermissive temperature. Further investigations show this decreased rate to be the result of an increased half life of the lipid-oligosaccharide at 40.8 degrees C. These data indicate that the temperature-sensitive step in glycoprotein biosynthesis is the transfer of the oligosaccharide core from the lipid-oligosaccharide intermediates to the nascent polypeptide chain. The data presented also provide evidence that the lipid-saccharide intermediates, previously described mainly in in vitro systems, are in fact involved in the glycosylation of a majority, if not all, of the mannose-containing glycoproteins in intact, growing hamster cells.

Animals↗
PubMed2001

Determination of saccharides in fruit juices by capillary electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

A fast method for the detection of cheap sweeteners is presented. Detecting the adulteration of foods rich in carbohydrates is complicated by the presence of variety of commercial sweeteners that are designed to match exactly the major carbohydrate profiles of these foods. Electrophoretic and mass spectrometric assays for the determination of fruit juice authenticity were developed. Capillary zone electrophoresis with indirect detection was employed to detect adulteration of juices demonstrated by the ratio of the concentrations of major low molecular mass saccharides (glucose, fructose and sucrose). Traces of oligosaccharides, which are not present in the sugar profiles of citrus fruits but are present in inexpensive sweeteners, were evaluated as the other group of target compounds. The fast determination of oligomeric starch hydrolysates in a complex matrix was tested by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and applied to orange juice. MALDI-TOFMS was shown to be a suitable method for the identification of adulteration of fruit juices by starch hydrolysates. The effects of the presence of salts and low molecular mass saccharides on the detection of oligosaccharides by MALDI-TOFMS were studied. Low molecular mass saccharides and organic acids decrease the detectability of oligosaccharides by MALDI-TOFMS, but the concentration of maltooligosaccharides present in juices sweetened with starch hydrolysates is high enough to be detected with good sensitivity.

Beverages↗
PubMed2002

Development of a gas chromatographic/ion trap mass spectrometric method for the determination of levoglucosan and saccharidic compounds in atmospheric aerosols. Application to urban aerosols.

We developed and validated a gas chromatographic/ion trap mass spectrometric method for the determination of levoglucosan and the related monosaccharide anhydrides, mannosan, galactosan and 1,6-anhydro-beta-D-glucofuranose in urban atmospheric aerosols collected on quartz fiber filters. The method is based on extraction with dichloromethane-methanol (80 : 20, v/v), trimethylsilylation, multiple reaction monitoring in the tandem mass spectrometric mode using the ion at m/z 217, and the use of an internal standard calibration procedure with the structurally related compound methyl beta-L-arabinopyranoside. In addition, the method allows the quantification of other saccharidic compounds, arabitol, mannitol, glucose, fructose, inositol and sucrose, which were found to be important in summer aerosols. The recovery of levoglucosan was estimated by spiking blank filters and was better than 90%. The precision evaluated by analyzing parts of the same filters was about 2% for the monosaccharide anhydrides and 7% for the other saccharidic compounds in the case of a winter aerosol sample, and the corresponding values for a summer aerosol sample were 5% and 8%. The method was applied to urban PM(10) (particulate matter of <10 microm aerodynamic diameter) aerosols collected at Ghent, Belgium, during a 2000-2001 winter and a 2001 summer episode and revealed interesting seasonal variations. While monosaccharide anhydrides were relatively more important during the winter season owing to wood burning, the other saccharidic compounds were more prevalent during the summer season, with some of them, if not all, originating from the vegetation.

Aerosols↗