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PubMed2000

Structure/thermodynamics relationships of lectin-saccharide complexes: the Erythrina corallodendron case.

Molecular dynamics (MD) simulations of Erythrina corallodendron lectin binding to a monosaccharide, alpha-galactose, and a disaccharide, N-acetyl lactosamine, have been performed in order to investigate the relationship between structure and thermodynamics. A simulated annealing protocol has been used to generate ensembles of structures for the two complexes, from which both qualitative and quantitative information on binding dynamics have been extracted. The ensembled averaged lectin-saccharide interaction enthalpy is equivalent for both sugars, whereas the calculation based on the X-ray structures does show a difference. Within large statistical errors, the calculated 'binding enthalpy' is also the same for the two systems. These errors arise largely from terms involving solvent and are a typical limitation of current MD simulations. Significant qualitative differences in binding between the two complexes are, however, observed over the ensembles. These could be important for unraveling the structure/thermodynamic relationship. Stated simply, there are a greater number of binding options available to the disaccharide compared to the monosaccharide. The implications of alternative binding states on thermodynamic parameters and the 'breaking of enthalpy-entropy compensation' are discussed. The role of solvent in lectin-saccharide complex formation is suggested to be significant.

Amino Sugars↗
PubMed2001

Thermodynamic analysis of saccharide binding to snake gourd (Trichosanthes anguina) seed lectin. Fluorescence and absorption spectroscopic studies.

The interaction of different saccharides with the snake gourd (Trichosanthes anguina) seed lectin (SGSL) was investigated by fluorescence spectroscopy. Binding of 4-methylumbelliferyl-beta-D-galactopyranoside (MeUmb beta Gal) to SGSL resulted in a significant increase in the fluorescence emission intensity of the sugar at 376 nm, and this change was used to estimate the association constants for the binding interaction. Interestingly, the increase in emission intensity changed with a change in temperature, increasing from 19.2% at 20 degrees C to 80.2% at 40 degrees C. At 20 degrees C the association constant, K(a), for the MeUmb beta Gal-SGSL interaction was found by fluorescence titration to be 5.8 x 10(4) M(-1). From the temperature dependence of the association constants, the changes in enthalpy (Delta H) and entropy (Delta S) associated with binding of MeUmb beta Gal to SGSL were estimated to be -80.85 kJ.mol(-1) and -184.0 J.mol(-1).K(-1), respectively. Binding of unlabeled sugars was investigated by monitoring the decrease in fluorescence intensity when they were added to a mixture of SGSL and MeUmb beta Gal. The Ka values for different sugars were determined at several temperatures, and Delta H and Delta S were determined from the van't Hoff plots. Enthalpy-entropy compensation was noticed in all cases. The results indicate that saccharide binding to SGSL is enthalpy-driven and the negative contribution from entropy is, in general, quite high.

Agglutination↗
PubMed1995

Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides.

O-Sulfation at C-3 of N-sulfated GlcN units concludes polymer modification and the formation of antithrombin binding regions in the biosynthesis of heparin/heparan sulfate. The resulting GlcNSO3(3-OSO3) units are largely restricted to heparin chains with high affinity for antithrombin (HA heparin). Low affinity (LA) heparin fails to serve as a substrate in the 3-O-sulfotransferase reaction yet contains potential 3-O-sulfate acceptor sites (Kusche, M., Torri, G., Casu, B., and Lindahl, U. (1990) J. Biol. Chem. 265, 7292-7300), as verified in the present study using a novel sequencing procedure. O-Desulfated, re-N-sulfated LA heparin, as well as an octasaccharide fraction isolated after heparinase I digestion of LA heparin, both yielded labeled HA components following incubation with solubilized mouse mastocytoma microsomal enzymes and [35S]adenosine 3'-phosphate 5'phosphosulfate (PAPS), suggesting that the 3-O-sulfo-transferase may be inhibited by sulfated saccharide sequences outside the 3-O-sulfate acceptor region. Indeed, the addition of LA heparin precluded enzymatic 3-O-sulfation of a synthetic pentasaccharide substrate. The Km for the pentasaccharide was determined to approximately be 6 microM. Incubations of mixed pentasaccharide substrate and saccharide inhibitors revealed Ki values for intact LA heparin and for a heparin octasaccharide fraction of approximately 1.3 and approximately 0.7 microM, respectively. Inhibition experiments with selectively desulfated heparin indicated that both IdoA 2-O-sulfate and GlcN 6-O-sulfate groups contributed to the inhibition of the 3-O-sulfotransferase. By contrast, chondroitin sulfate or dermatan sulfate showed no significant inhibitory activity. It is proposed that the regulation of GlcN 3-O-sulfation during biosynthesis of heparin/heparan sulfate depends on the topological organization of the membrane-bound enzyme machinery in the intact cell.

Animals↗
PubMed2006

Cryoprotective effects of saccharides on the freeze-drying of sonicated vesicles of the novel lipid A analog, E5531.

A sonicated dispersion of the novel lipid A analog, E5531, was feeze-dried in the presence of various additives such as saccharides and polyalcohols, and their cryoprotective effects were investigated. Fusion of the vesicles was examined by measuring fluorescence energy transfer and size distribution. Cryoprotective ability differed among the addtive species. The addition of polyalcohols led to considerable fusion. Although monosaccharides, similar to disaccharides, completely prevented the fusion of the vesicles during lyophilization, they showed far less ability to retain the entrapped calcein in the vesicles compared to disaccharides. Differential scanning calorimetry heating profiles of vesicles that had been lyophilized with various additives were obtained. Disaccharides and monosaccharides again resulted in markedly different thermal properties of the vesicles. This variety in cryoprotective ability of saccharide species can be attributed to differences in their interaction with the E5531 head group.

Calorimetry, Differential Scanning↗
PubMed1998

Saccharide-assisted delivery of cytotoxic liposomes to human malignant cells.

The overexpression of lectins by malignant cells was applied for in vitro targeting of liposomes equipped with a saccharide vector and loaded in the lipid phase with a lipid derivative of anticancer agent sarcolysine. The lectin specificity of human leukemia HL-60 and human lung adenocarcinoma ACL cells was revealed by tests with fluorescein-labeled sugar probes. With the help of fluorescent lipid dye it was shown that active saccharide ligands increased the level of the vectored liposome binding to malignant cells by 50-80% as compared to liposomes without vector or with inactive one. The degree of liposome/cell membrane fusion was monitored fluorometrically and was shown to be complete and independent of the vectors. The targeted drug-loaded liposomes had the cytotoxic activity 2-4 times higher as compared to the vector-free ones.

Acrylic Resins↗
PubMed1990

Carbohydrate binding activities of Bradyrhizobium japonicum. I. Saccharide-specific inhibition of homotypic and heterotypic adhesion.

Bradyrhizobium japonicum (R110d) exhibited four saccharide-specific binding activities: (a) adsorption to Sepharose beads containing covalently coupled lactose; (b) homotypic agglutination through one pole of the cell (star formation); (c) heterotypic adhesion to the cultured soybean cell line, SB-1; and (d) attachment to roots of soybean plants. Each of these binding activities can be inhibited by the addition of galactose or lactose, but not by derivatives such as N-acetyl-D-galactosamine or melibiose. Treatment of wild-type bacteria with N-methyl-N'-nitro-N-nitrosoguanidine followed by selection on the basis of reduced binding to SB-1 cells, resulted in two specific mutants, designated N4 and N6. Compared to wild type, these two mutants also exhibited decreased binding activity in: (a) adsorption to lactose-Sepharose beads; (b) homotypic star formation; and (c) heterotypic attachment to roots of soybeans plants. These results suggest that all four of the saccharide-inhibitable binding activities of Bradyrhizobium japonicum may be mediated by the same mechanism(s) or molecular component(s).

Agglutination↗
PubMed1980

Subcellular compartmentalization of saccharide moieties in cultured normal and malignant cells.

We studied subcellular localization of saccharide moieties in cultured normal and malignant cells fixed in paraformaldehyde and treated with a nonionic detergent, using lectins specific for various surgar residues as probes in fluorescence microscopy. In normal cells, concanavalin A and Lens culinaris agglutinin, specific for mannose-rich carbohydrate cores in glycoproteins, labeled the endoplasmic reticulum as a wide perinuclear region. Other lectins, on the other hand, stained the Golgi apparatus as a juxtanuclear reticular structure. A similar compartmentalization was also seen in all malignant cells studied, although the Golgi apparatus in these cells was distinctly vesicular in appearance. Our results indicate that saccharide moieties in both normal and malignant cells are similarly compartmentalized, and thus speak in favor of a unidirectional subcellular flow for both membrane and secreted glycoconjugates.

Animals↗
PubMed1997

Infant immunization with pneumococcal CRM197 vaccines: effect of saccharide size on immunogenicity and interactions with simultaneously administered vaccines.

Six pentavalent pneumococcal conjugate vaccines (Pn-CRM197) were evaluated among 400 infants. The vaccines differed in saccharide chain length (oligosaccharide [OS] or polysaccharide [PS]) and saccharide quantity (0.5, 2, or 5 microg). Subjects were randomized into groups 1-6 (Pn-CRM197 recipients) or 7 (controls) for immunization at 2, 4, and 6 months of age. Pn-CRM197 were well tolerated and elicited mean antibody concentrations that exceeded those in controls for all 5 capsular serotypes. PS formulations were generally more immunogenic than their OS counterparts. For PS vaccines, a dose-response was documented (5 microg > 2 microg > 0.5 microg), but the differences between the 5- and 2-microg formulations were insignificant. The mean anti-PRP antibody concentration was significantly higher among Pn-CRM197 recipients. It is concluded that PS vaccines are more immunogenic than OS vaccines. The improved immunogenicity from Haemophilus type b oligosaccharide conjugate (HbOC) vaccine when given with Pn-CRM197 suggests that a decreased dose of HbOC vaccine may be sufficient to elicit protection.

Antibodies, Bacterial↗
PubMed1987

Selecting the most effective filtration media for HPLC analysis of saccharides.

Saccharides of known standard solutions of high purity are analyzed on a carbohydrate high-performance liquid chromatographic (HPLC) column. Standards filtered through membranes with wetting agents and other additives have different compositional results from those filtered through membranes without additives. The selection of a filter membrane to remove insolubles from the sample prior to HPLC analysis of saccharides is an important consideration of the analysis.

Carbohydrates↗
PubMed2006

An invertebrate TNF functional analogue activates macrophages via lectin-saccharide interaction with ion channels.

The invertebrate pattern-recognition protein named coelomic cytolytic factor (CCF) and the mammalian cytokine tumor necrosis factor (TNF) share functional analogies that are based on a similar saccharide recognition specificity. In particular, CCF and TNF have been shown to interact with ion channels on the surface of vertebrate cells via N,N'-diacetylchitobiose lectin-like activity. In the present study, we show that CCF-induced membrane depolarization results in the release of TNF, IL-6 and nitric oxide (NO) by macrophages via nuclear factor-kappaB signaling. Interestingly, our data suggest that TNF contributes, through lectin-saccharide interaction, to the secretion of IL-6 and NO induced by CCF. This experimental non-physiological setting based on the interaction of an invertebrate defense lectin with vertebrate cells involved in the innate immune response may have highlighted an evolutionarily ancient mechanism of macrophage activation in vertebrates.

Animals↗
PubMed1981

Increased activity of rat intestinal lactase due to increased intake of alpha-saccharides (starch, sucrose) in isocaloric diets.

The adaptability of intestinal microvillar alpha-disaccharidases to the variation of alpha-saccharide content in the diets is well established, but the influence of these sugars on the activity of microvillar lactase (neutral beta-galactosidase) has heretofore been considered negligible or non-existing. In two experiments rats were fed isocaloric diets where the carbohydrate (starch or sucrose) content versus fat content was varied. (High carbohydrate diets: 71% of calories as carbohydrate and 5% of calories as fat; low carbohydrate diets: 6 and 73% calories, respectively). Experiment 1: male and female rats had access to experimental diets only from day 12 postnatally and were killed at age 56 days. Experiment 2: male rats were fed experimental diets starting on day 73 postnatally and killed 3, 7, 14 and 28 days later. Rats fed the high carbohydrate diets exhibited a significant increase in activity (specific and total per segment) of lactase in all three intestinal segments compared to rats fed the low carbohydrate diets. Changes in the activity of sucrase and maltase paralleled those of lactase activity. These experiments have thus demonstrated clearly the influence of variation in alpha-saccharide content in the diet upon lactase activity. Further experiments are needed to determine the active principle of this dietary adaptation.

Adaptation, Physiological↗
PubMed1999

Trehalose can be used as a parenteral saccharide source in rabbits.

Trehalose is a saccharide that possesses no reducing group and so has possible use in parenteral nutrition, especially because it can be stored with amino acids without undergoing the Maillard reaction. To evaluate this possibility, a series of experiments were conducted. The activity of trehalase, an enzyme that metabolizes trehalose to glucose, was measured in rabbit serum and kidney. Conversion of trehalose to glucose and excretion of trehalose in the urine were measured in rabbits administered 10% trehalose intravenously. The effects on nutritional indices as indicators of its use as an energy source were also measured in rabbits infused with 8.23 g.kg-1.d-1 (4. 12 g.kg-1 on d 1) of trehalose for 5 d. Trehalase activity resembled maltase activity, both being high in the renal cortex (2.04 +/- 0.71 and 2.93 +/- 0.26 micromol.g-1.min-1, respectively), weak in the medulla, and undetectable in the serum. Serum glucose and insulin concentrations were increased significantly by trehalose infusion. Significant elevations were observed in serum glucose but not insulin levels by maltose infusion. On the other hand, urinary excretion of trehalose (1.1 +/- 2.1% of dose) was significantly lower than that of maltose (10.1 +/- 4.9% of dose). Similar effects of trehalose and maltose infusions as seen in normal rabbits occurred in rabbits with alloxan diabetes (urinary excretion rate, 3. 8 +/- 3.0% of the infused trehalose dose and 35.6 +/- 9.7% of the infused maltose dose). Nitrogen balance was positive in the trehalose- and glucose-infused normal rabbits with significant difference from the control group infused with saline, suggesting that trehalose was used as an energy source. These results suggest that trehalose has the potential for use as a saccharide source for parenteral nutrition.

Animal Nutritional Physiological Phenomena↗
PubMed1981

Studies on the specific interaction of concanavalin A and saccharides by affinity chromatography. Application of quantitative affinity chromatography to a multivalent system.

Quantitative affinity chromatography of concanavalin A (Con A) was studied in order to clarify its mechanism of saccharide binding. Another aim of this work was to confirm the validity of frontal affinity chromatography, which we have developed for the study of specific interactions, for multivalent systems. Since Cona A exists as either a dimer or a tetramer, it is a suitable multivalent test system. Immobilized p-aminophenyl-beta-D-glucopyranoside (AP beta-Glc Sepharose) was prepared and the interactions of homogeneous preparations of Con A with this affinity adsorbent were analyzed. Experiments were carried out under conditions where Con a exists as the dimer (5 degrees C, pH 7.9, I=0.19). The intrinsic dissociation constant of Con A for the immobilized ligand (Kd) could be determined from the extent of retardation. alpha-Con A (intact Con A) had a stronger affinity than beta-Con A. Changes in pH and ionic strength had different effects on the affinity of alpha- and beta-Con A. The dissociation constants of soluble saccharides and their derivatives (counter ligands) for Con A (K1) could be determined from their ability to diminish the elution volume of Con A. K1 values of various monosaccharides for beta-Con A including those having very weak affinity, were determined. Further, the K1 values of a series of glucobioses were determined and compared. It was found that the binding mode of the reducing terminal glucose residue must be taken into account. The results are discussed in relation to their configurations. Frontal affinity chromatography proved to be very useful as a tool to analyze specific interactions in multivalent systems.

Carbohydrates↗
PubMed1985

A common linkage saccharide unit between teichoic acids and peptidoglycan in cell walls of Bacillus coagulans.

Teichoic acid-glycopeptide complexes were isolated from lysozyme digests of the cell walls of Bacillus coagulans AHU 1631, AHU 1634, and AHU 1638, and the structure of the teichoic acid moieties and their linkage regions was studied. On treatment with hydrogen fluoride, each of the complexes gave a hexosamine-containing disaccharide, which was identified to be glucosyl(beta 1----4)N-acetylglucosamine, in addition to dephosphorylated repeating units of the teichoic acids, namely, galactosyl(alpha 1----2)glycerol and either galactosyl(alpha 1----2)[glucosyl(alpha 1----1/3)]glycerol (AHU 1638) or galactosyl(alpha 1----2)[glucosyl(beta 1----1/3)]glycerol (AHU 1631 and AHU 1634). From the results of Smith degradation, methylation analysis, and partial acid hydrolysis, the teichoic acids from these strains seem to have the same backbone chains composed of galactosyl(alpha 1----2)glycerol phosphate units joined by phosphodiester bonds at C-6 of the galactose residues. The presence of the disaccharide, glucosyl(beta 1----4)N-acetylglucosamine, in the linkage regions between teichoic acids and peptidoglycan was confirmed by the isolation of a disaccharide-linked glycopeptide fragment from each complex after treatment with mild alkali and of a teichoic acid-linked saccharide from each cell wall preparation after treatment with mild acid. Thus, it is concluded that despite structural differences in the glycosidic branches, the teichoic acids in the cell walls of the three strains are linked to peptidoglycan through a common linkage saccharide, glucosyl (beta 1----4) N-acetylglucosamine.

Bacillus↗
PubMed1976

Chemical modification of the tryptophan residues of wheat-germ agglutinin. Effect on fluorescence and saccharide-binding properties.

The oxidation of the tryptophan residues of wheat germ agglutinin by N-bromosuccinimide was investigated under non-denaturing and denaturing conditions. All three tryptophan residues present in wheat germ agglutinin subunit (molecular weight 18 000) could be modified in 0.1 M acetic acid/8 M urea, pH 3.9. One of the residues failed, however, to react with N-bromosuccinimide when the modification was in 0.1 M citrate buffer, pH 6.0. Tryptophan fluorescence of the protein was quenched concomitantly with the oxidation of two tryptophan residues even when the modification was carried out in acetic acid urea. After oxidation of two tryptophan residues per subunit of wheat germ agglutinin, only 15% of the original tryptophan fluorescence remained; upon excitation at 280 nm, tyrosine fluorescence centered at 305 nm could be resolved. The results suggest that there are only two emitters in the protein and that the third tryptophan residue is buried in the native protein and can be modified only in acetic acid urea. This tryptophan residue is quenched in the native protein. Saturation of wheat germ agglutinin with tri-N-acetylchitotriose did not protect the tryptophan residues from oxidation by N-bromosuccinimide. Under these conditions, however, the reactivity of the tryptophan residues towards N-bromosuccinimide was reduced and a higher concentration of the reagent was required to achieve the same extent of oxidation as in the absence of the saccharide. Oxidation of one tryptophan residue per subunit in acetic acid urea led to almost complete loss (97%) of hemagglutinating activity, a 3.5-fold decrease in the affinity constant for tri-N-acetylchitotriose and loss of ability of the subunits (SO20,w = 2.0 S) to reassociate to the native dimer (So20,w = 3.5 S) after dialysis against a non-denaturing buffer. No significant changes in the circular dichroism spectrum of wheat germ agglutinin were observed after oxidation of the three tryptophan residues, suggesting that no gross conformational changes occurred. The steric relationships between the fluorescent tryptophan residues of wheat germ agglutinin and saccharides are discussed.

Binding Sites↗
PubMed1978

The poly(glycosyl) chains of glycoproteins. Characterisation of a novel type of glycoprotein saccharides from human erythrocyte membrane.

Glycopeptides with complex carbohydrate structure were isolated from delipidated human erythrocyte membranes after digestion with pronase. The poly(glycosyl)peptides isolated (apparent molecular weight 4000--13000) are suggested to contain 20--70 sugar residues in an alkali-stable saccharide chain linked through N-acetylglucosamine to asparagine. The main sugar components are galactose and N-acetylglucosamine, which together account for 80% of total sugars. That the compounds isolated are glycopeptides and not glycolipids is concluded from the following findings: only trace amounts of glucose and fatty acids were present, and no long-chain (sphingosine) bases could be detected; on the other hand, the amounts of mannose and amino acids found are compatible with an N-glycosidic poly(glycosyl)peptide structure. The structure of the poly(glycosyl)peptides was studied using methylation analysis, exoglycosidase treatments, acid hydrolysis of the native as well as the N-deacetylated glycopeptides, and chromium trioxide oxidation. The studies indicate that the poly(glycosyl)peptides contain a repeating-3)galactosyl(beta1-4)N-acetylglucosaminyl(beta1-structure with branch points at the C-6 of the galactose residues. The saccharide chains are terminated in N-acetylglucosaminyl, galactosyl, N-acetylneuraminyl(alpha2-3 and 6)galactosyl and fucosyl(alpha1-2)galactosyl residues, and they also contain blood group A and B determinants.

Amino Acids↗
PubMed1991

Heparinase II from Flavobacterium heparinum. HPLC analysis of the saccharides generated from chemically modified heparins.

Saccharides produced by the action of heparinase II on native pig mucosal heparin (heparin IS), de-N-sulphated heparin (heparin IH), N-acetylheparin (heparin IA), de-N/O-sulphated heparin (heparin IVH), de-O-sulphated heparin (heparin IVS) and de-O-sulphated N-acetylheparin (heparin IVA) were analysed by reversed-phase HPLC using Spherisorb ODS2. Fractions obtained by gel filtration with Bio-Gel P-4 were similarly examined. Heparin IS gave delta UA-2S----GlcNS-6S (IS) as the major unsaturated disaccharide and lesser amounts of delta UA----GlcNS-6S (IIS), delta UA-2S----GlcNS (IIIS), delta UA----GlcNS (IVS), delta UA-2S----GlcNAc-6S (IA), delta UA----GlcNAc-6S (IIA), delta UA-2S----GlcNAc (IIIA) and delta UA----GlcNAc (IVA). Heparins IA, IVA and IVS gave as the predominant unsaturated disaccharide that corresponding to the major repeat structure of the polymer. These were respectively delta UA-2S----GlcNAc-6S (IA), delta UA-GlcNAc (IVA) and delta UA----GlcNS (IVS). Minor disaccharides from the heterogeneous structure in native pig heparin and from residual O-sulphates after the de-O-sulphating process were detected. Heparin IH was degraded more slowly than any of the N-substituted heparins. The predominant unsaturated disaccharide was IH, which was derived from the major repeating unit. In addition, disaccharides IIH, IIIH, IA, IIA and IVA were detected. Heparin IVH showed little degradation, the unsaturated disaccharide IVH not being detected after 24 h. Disaccharide IVA was obtained from the heterogeneous sequence in heparin IVH. Several higher oligosaccharides were identified in the gel-filtration fractions including saccharides from the linkage region (for heparin IS and IVA) and the anti-thrombin binding site (for heparin IS only). A tetrasaccharide and hexasaccharide, with the structures delta UA----GlcNAc----UA----GlcNAc and delta UA----GlcNAc----UA----GlcNAc----UA----GlcNAc, were present in the HPLC profiles of heparins IA and IVA.

Animals↗
PubMed2003

Effect of saccharide additives on response of ferrous-agarose-xylenol orange radiotherapy gel dosimeters.

Glucose, sucrose, starch, and locust bean gum have been used as additives to the ferrous-agarose-xylenol orange (FAX) gel dosimeter. The saccharide enhanced dosimeters were found to have a higher dose sensitivity over a standard FAX gel as measured by both optical density change and magnetic resonance imaging (MRI). With optical density measurement, OD-dose sensitivity increases were up to 55% for glucose, 122% for sucrose and 43% for starch, while locust bean gum did not give a consistent response. With MRI, R1-dose sensitivity increases were up to 178% with sucrose addition. The FAX gel with sucrose was studied in greatest detail. The OD-dose sensitivity dependence on cooling rate was reduced for the sucrose FAX gel over the standard FAX gel, which has significant implications for uniform dose sensitivity in large gel phantoms. The thermal oxidation rate in the sucrose FAX gel was up to 2.3 times higher than in the standard gel. The OD-dose sensitivity of oxygenated sucrose FAX gels was 4.3 times greater than standard FAX gels, while continued enhancement in OD-dose sensitivity with increased sucrose concentrations beyond 2.0 g/l was found only for the oxygenated sucrose FAX gels. Both the molar absorption coefficient of the ferric ion-xylenol orange complex at 543 nm and gel pH were not affected by the presence of sucrose, with the implication that the higher OD-dose sensitivity of gels with saccharides is due to increased chain reaction production of ferric ions.

Carbohydrates↗