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PubMed1986

Oxidative degradation of glycosphingolipids revisited: a simple preparation of oligosaccharides from glycosphingolipids.

In order to cleave gangliosides and isolate the oligosaccharide portion, the allylic nature of OH-3 of the sphingenine base was utilized in its selective oxidation to a ketone group by 2,3-dichloro-5,6-dicyanobenzoquinone. Triethylamine treatment of the oxidation products resulted in the beta-elimination of the intact oligosaccharide. The isolation of the pure oligosaccharide from the modified ceramide residue and unreacted ganglioside was obtained by liquid chromatography. Preliminary investigations suggest that the same reaction conditions can be used for an analogous elimination of oligosaccharides linked to the serine or threonine residues of glycoproteins.

Animals↗
PubMed1986

Affinity of four immobilized Erythrina lectins toward various N-linked glycopeptides and related oligosaccharides.

The behavior of N-acetyllactosamine-type oligosaccharides and glycopeptides on columns of four different Erythrina agglutinins immobilized on Sepharose was examined. The sugar-binding specificity of the four lectins is very similar and is directed toward unmasked N-acetyllactosamine sequences, the main difference between the four lectins being the relative strength of interaction of the lectins with a given glycan. Substitution of the N-acetyllactosamine sequences by sialic acid residues, either at O-3 or O-6 of galactose completely abolishes the affinity of the lectins for the saccharides. The presence of one or several alpha-Fuc-(1----3)-GlcNAc groups decreases or completely inhibits the interaction between the glycopeptides and the Erythrina lectins. Substitution of the beta-mannose residue by an additional bisecting beta-(1----4)-N-acetylglucosamine residue decreases the affinity of the lectins for these structures as compared to the unsubstituted ones. Surprisingly, the affinity of the lectins for the oligosaccharides tested is higher than for the corresponding glycopeptides. Our findings show that, after careful calibration with well-defined oligosaccharides and glycopeptides, the immobilized Erythrina agglutinin-Sepharose columns provide valuable tools for the fractionation of N-acetyllactosamine-containing oligosaccharides and glycopeptides.

Carbohydrate Conformation↗
PubMed1991

The glycosylation of glycoprotein lectins. Intra- and inter-genus variation in N-linked oligosaccharide expression.

Glycosylated lectins represent a series of glycoproteins with related activities and, in the case of the Leguminosae, related amino acid sequences. Therefore, they offer a model system in which to study the diversity of N-linked oligosaccharide structures of plant glycoproteins. The influence of the polypeptide on the type of oligosaccharide substitution and the problem of inter- and intra-genus variation in glycosylation can also be addressed. Analysis of the glycosylation of 18 lectins has shown that they can be classified into four qualitatively similar groups on the basis of the Bio-Gel P-4 elution profiles of the oligosaccharides released by hydrazinolysis: (a) The Erythrina cristagalli profile, with a major component at 8.8 glucose units (gu) and minor components at 8.0, 7.2, and 5.8 gu. The major component is the heptasaccharide, alpha-D-Manp-(1----3)-[alpha-D-Manp-(1----6)]-[beta-D-Xyl p-(1----2)]- beta-D-Manp-beta-D-GlcpNAc-(1----4)-[alpha-L-Fucp-(1----3)]- D-GlcNAc. (b) The Phaseolus vulgaris profile, which was characterized by peaks at 12.5, 11.7, 10.8, and 9.9 gu, in addition to the peaks at 8.8, 8.0, 7.2, and 5.8 gu mentioned above. These higher-mol.-wt. components were oligo-D-mannose oligosaccharides containing 9, 8, 7, and 6 D-mannose residues, respectively. (c) The Lonchocarpas capassa profile, which had a major peak at approximately 8 gu. (d) The soybean agglutinin profile, which has a single peak at 12.5 gu. This peak consisted solely of an oligomannose undecasaccharide containing 9 D-mannose residues. This lectin is unique in that it shows no microheterogeneity.

Carbohydrate Conformation↗
PubMed2001

NMR studies of mannitol-terminating oligosaccharides derived by reductive alkaline hydrolysis from brain glycoproteins.

Interest in the characterisation of O-mannosyl glycan structures has been stimulated following the identification of mannitol-terminating oligosaccharides among the chains released from mammalian proteins in nervous and muscle tissues, and by the discovery of a putative human O-mannosyl transferase. Several mass spectrometry methods have been applied to structure elucidation particularly when low amounts of oligosaccharide are available for analysis. However, when sufficient amounts are available, a combination of through-bond homo- and heteronuclear, and of through-space homonuclear NMR experiments permit the complete identification of these oligosaccharide sequences. We describe here the assignment of 1H and 13C NMR chemical shifts from such experiments for four mannitol-terminating oligosaccharide alditols, GlcNAcbeta-(1-->2)Manol, Galbeta-(1-->4)GlcNAcbeta-(1-->2)Manol, Galbeta-(1-->4)[Fucalpha-(1-->3)]GlcNAcbeta-(1-->2)Manol and NeuAcalpha-(2-->3)Galbeta-(1-->4)GlcNAcbeta-(1-->2)Manol, that were released from brain glycopeptides by alkaline borohydride treatment.

Animals↗
PubMed2001

Negative-ion electrospray ionisation-mass spectrometry (ESI-MS) as a tool for analysing structural heterogeneity in kappa-carrageenan oligosaccharides.

Oligosaccharides, enzymically produced from kappa-carrageenan, have been investigated by electrospray ionisation mass spectrometry (ESI-MS). The technique was used without prior derivatisation of the oligosaccharide originally obtained by size-exclusion chromatography (SEC). The structure of the oligosaccharides was mainly 4-sulphated neocarrabiose (A-G4S) with an increasing length ranging from di- to dodecasaccharides. However, in the larger oligosaccharides, structural motifs deviating from the perfect alternating A-G4S structure were detected, i.e. (A2S-G4S). Although resulting in reduced signal intensity, samples to which NaCl was added also gave rise to reliable mass spectra. Desulphation was induced at elevated cone voltages and in acidic or alkaline salt solutions.

Carbohydrate Sequence↗
PubMed2002

Structural studies on kappa-carrageenan derived oligosaccharides.

Oligosaccharides were prepared through mild hydrochloric acid hydrolysis of kappa-carrageenan from Kappaphycus striatum carrageenan. Three oligosaccharides were purified by strong-anion exchange high-performance chromatography. Their structure was elucidated using mass spectral and NMR data. Negative-ion electrospray ionization (ESI) mass spectra at different fragmentor voltages provided the molecular weight of the compounds and unraveled the fragmentation pattern of the kappa-carrageenan oligosaccharides. 2D NMR techniques, including 1H-(1)H COSY, 1H-(1)H TOCSY and 13C-(1)H HMQC, were performed to determine the structure of a trisulfated pentasaccharide. 1D NMR and ESIMS were used to determine the structures of a kappa-carrageenan-derived pentasaccharide, heptasaccharide, and an undecasaccharide. All the oligosaccharides characterized have a 4-O-sulfo-D-galactopyranose residue at both the reducing and nonreducing ends.

Carbohydrate Conformation↗
PubMed2002

Heparin oligosaccharide sequence and size essential for inhibition of pulmonary artery smooth muscle cell proliferation.

Heparin has a wide range of important biological activities including inhibition of pulmonary artery smooth muscle cell proliferation. To determine the minimum size of the heparin glycosaminoglycan chain essential for antiproliferative activity, porcine intestinal mucosal heparin was partially depolymerized with heparinase and fractionated to give oligosaccharides of different sizes. The structure of these oligosaccharides was fully characterized by 1D and 2D 1H NMR spectroscopy. These oligosaccharides were assayed for antiproliferative effects on cultured bovine pulmonary artery smooth muscle cells (PASMCs). The tetrasaccharide (4-mer) exhibited no heparin-like activity. Decasaccharides (10-mers) and dodecasaccharides (12-mers) displayed a reduced level of activity when compared to full-length heparin. Little effect on activity was observed in deca- and dodecasaccharides with one less 2-O-sulfo group. The 14-, 16-, and 18-mers showed comparable growth-inhibition effects on PAMSC as porcine intestinal mucosal heparin. These data suggest that a 14-mer is the minimum size of oligosaccharide that is essential for full heparin-like antiproliferative activity. Since the 14- to 18-mers have no 3-O-sulfo groups in their glucosamine residues, their full activity confirms that these 3-O-sulfonated glucosamine residues, which are required for heparin's anticoagulant activity, are not an essential requirement for antiproliferative activity.

Animals↗
PubMed1996

Disulfated oligosaccharides derived from tracheobronchial mucous glycoproteins of a patient suffering from cystic fibrosis.

Twenty novel disulfated oligosaccharides were purified in nanomolar quantities from tracheo-bronchial mucous glycoproteins from a patient with cystic fibrosis via cleavage by alkaline borohydride treatment, followed by anion-exchange chromatography, size-exclusion chromatography, and high-performance liquid chromatography (HPLC). In addition to positive ion fast-atombombardment mass spectrometry (FABMS), proposed structures for the resulting purified disulfated oligosaccharides were also based on carbohydrate permethylation analyses, periodate oxidation, complete sequential exoglycosidase digestion, and parallel analysis of desulfated products. Sulfate esters were found to reside on C-3 or C-6 of terminal D-galactose and on C-6 of internal D-galactose or 2-acetamido-2-deoxy-D-glucose residues. For this group of oligosaccharides, ranging in size from tri- to undeca-saccharides and possessing linear, di- and tri-antennary forms, it was also observed that sulfate esters could be located on the same or on different branches and that branched oligosaccharides can possess sulfate esters on C-3 and C-6 of different terminal galactose residues within the same structure.

Bronchi↗
PubMed1997

Matrix-assisted laser desorption ionization mass spectrometry for the analysis of monosulfated oligosaccharides.

Sulfated oligosaccharides are an important class of compounds in the field of glycobiology. Mass spectrometric analysis of these molecules is challenging due to their readiness to dissociate in sample preparation and their tendency to fragment during ionization. Moreover, their presence in small quantity in biological systems poses additional problems. We report the development of a mass spectrometric method based on matrix-assisted laser desorption ionization (MALDI) in a time-lag focusing time-of-flight mass spectrometer for the analysis of monosulfated oligosaccharides. It is found that coumarin 120 is an excellent matrix for the analysis of monosulfated disaccharides, whereas the use of a mixture of coumarin 120 and 6-aza-2-thiothymine is very effective for the ionization of sulfated trisaccharides and tetrasaccharides including those containing N-acetylneuraminic acid. Molecular ions for a series of synthetic sulfo/sialo beta Gal(1-->3)GlcNAc and beta Gal(1-->4)GlcNAc structures can thus be observed with subpicomole detection sensitivity using a uniform microcrystal matrix/sample preparation procedure. It is demonstrated that, with this matrix formulation, the presence of a high amount of sodium chloride or sodium phosphate buffer, which is often the case for the HPLC fractionated samples, does not deteriorate the MALDI performance. The analysis of mixtures containing different types of oligosaccharides is also examined. It is found that different classes of oligosaccharides require different matrix preparation methods.

Azo Compounds↗
PubMed1998

The lipooligosaccharide (LOS) of Neisseria meningitidis serogroup B strain NMB contains L2, L3, and novel oligosaccharides, and lacks the lipid-A 4'-phosphate substituent.

The complete structure of the lipooligosaccharide (LOS) from Neisseria meningitidis strain NMB (serotype 2b:P1.2,5), a serogroup B cerebrospinal fluid isolate, was determined. Two oligosaccharide (OS) fractions and lipid-A were obtained following mild acid hydrolysis of the LOS. The structures in these fractions were determined using glycosyl composition and linkage analyses, N spectroscopy and mass spectrometry. One oligosaccharide fraction (OS1) consists of a molecule having a glycosyl sequence identical to that previously reported for the LOS from immunotype L2 N. meningitidis [A. Gamain, M. Beurret, F. Michon, J.-R. Brisson, and H.J. Jennings, J. Biol. Chem.,267,(112) 922-925] i.e., a lacto-N-neotetraose is attached to heptose I (Hep I), with terminally linked N-acetylglucosaminosyl and glucosyl residues attached to Hep II of the inner core. Approximately 70% of this structure is acetylated at O-6 of the terminally linked alpha-N-acetyl-glucosaminosyl residue. As with the L2 structure, the NMB LOS contained phosphoethanolamine (PEA) at O-6 or O-7 of the Hep II residue. The second oligosaccharide fraction (OS2) contains a a mixture of three different molecules, all of which vary from one another in their glycosyl substitution patterns of the Hep II residue. The most abundant molecule in OS2 has a structure identical to that of OSI, i.e., it has the L2 glycosyl sequence. A second molecule (OS2a) lacks the terminal glucosyl residue at O-3 of Hep II; i.e., it has a glycosyl sequence identical to that of the mild acid released oligosaccharide of N. meningitidis immunotype L3, L4, or L7 LOSs. The third molecule (OS2b) is a novel structure that lacks the terminal N-acetylglucosaminosyl residue linked to O-2 of Hep II. Overall, 76% of OS released from NMB LOS has the L2 structure, 15% is OS2a (L3), and 9% is OS2b. A portion (20%) of the molecules in the NMB LOS preparation also contained terminally linked sialic acid attached to O-3 of the lacto-N-neotetraose galactosyl residue, which is also consistent with the L3, or L4 LOS structures. In contrast to the previously reported structure of N. meningitidis lipid-A [V. A. Kulshin, U. Zähringer, B. Linder, C.E. Frasch, C-M. Tsai, B.A. Dmitriev, and E.T Rietschel, J. Bacteriol., 174, (1992)1793-1800], only 30% of the lipid-A from NMB LOS possesses 4'-phosphate. Comparison with the lipid-A of LOS purified from an isogenic acapsulate mutant, M7, revealed that the 4'-position was almost completely occupied with phosphate. These data emphasize the structural heterogeneity of the OS and phosphate substituents of Hep II, and 4'-phosphorylation of lipid-A of meningococcal LOS.

Carbohydrate Sequence↗
PubMed1998

Conformational differences among mono- and oligosaccharide fragments of O-specific polysaccharides of Vibrio cholerae O1 revealed by circular dichroism.

The circular dichroism (CD) of synthetic mono- and oligosaccharides that represent the terminal, non-reducing group of O-antigens of Vibrio cholerae O1 from the subtypes Ogawa and Inaba was measured in various solvents. We found differences in the CD of the monosaccharides of these subtypes that decrease with increasing chain lengths of the oligosaccharides. The differences can be explained by different orientations of the N-acyl side chain of the terminal monosaccharides. The linear relationship of ellipticity versus the number of residues in an oligosaccharide chain follows the principle of optical superposition. This, together with a similar contribution by internal units to the overall ellipticity, suggests an identical, regular conformation of oligosaccharide fragments of both Ogawa and Inaba series.

Carbohydrate Conformation↗
PubMed1998

Structural heterogeneity of the sialic-acid-containing oligosaccharides from the lipopolysaccharide of Hafnia alvei strain 2 as detected by FABMS studies.

The structure of four oligosaccharide fractions from the Hafnia alvei strain 2 lipopolysaccharide (LPS) have been assigned by FABMS. This approach corroborates data previously established by NMR spectroscopy for the major oligosaccharides in these fractions [A. Gamian, E. Romanowska, U. Dabrowski, J. Dabrowski, Biochemistry 30 (1991) 5032-5038; E. Katzenellenbogen, A. Gamian, E. Romanowska, U. Dabrowski, J. Dabrowski, Biochem. Biophys. Res. Commun. 194 (1993) 1058-1064; N. Ravenscroft, A. Gamian, E. Romanowska, Eur. J. Biochem. 227 (1995) 889-896]. In addition, the MS/MS with B/E linked scan technique allowed the detection of an additional oligosaccharide with the structure: [formula: see text] lacking the branched O-6 linked glucopyranose residue at the 3-linked Gal unit, which indicates a structural heterogeneity for the major oligosaccharide fraction.

Carbohydrate Sequence↗
PubMed1999

Enzymatic glycosylation of reducing oligosaccharides linked to a solid phase or a lipid via a cleavable squarate linker.

Reducing oligosaccharides were converted into their corresponding glycosylamines, and these were reacted with 3,4-diethoxy-3-cyclobuten-1,2-dione (squaric acid diethyl ester). The resulting derivatives could be linked to amino-functionalized lipids, solids, or proteins. Treatment of the obtained lipid or solid conjugates with aqueous bromine or, alternatively, with ammonia-ammonium borate cleaved the linkage and regenerated the oligosaccharide glycosylamines, which were in turn rapidly hydrolyzed to the reducing oligosaccharides. To demonstrate the usefulness of this linkage in enzymatic oligosaccharide synthesis, lactose was linked to a lipid or a solid phase, the obtained conjugates were then subjected to two enzymatic glycosylations (either consecutively or 'one-pot'). The resulting materials were then cleaved to give, in both cases, the expected reducing tetrasaccharide (lacto-N-neotetraose) in good yield.

Bacterial Proteins↗
PubMed1999

Oligosaccharides released by hydrazinolysis from Tamm-Horsfall protein of various human donors contain similar high-mannose glycans.

As pathophysiological functions claimed for Tamm-Horsfall protein (THP) are related to its sugar moiety, we examined influence of pregnancy and various diseases on high-mannose chains. Hydrazinolysis was used to liberate oligosaccharides from THP polypeptide backbone. After HPLC separation of fluorescently labelled glycans similar profiles of neutral oligosaccharides were observed in THP of healthy subjects, pregnant women, patients with Bartter's syndrome, patients with acute lymphoblastic leukemia and a patient with carbohydrate deficient glycoprotein syndrome. THP contains Man-5, Man-6 and Man-7 glycans, with the preponderant amount of Man-6 glycan (about 7% of total THP oligosaccharides). No statistically significant differences were found in THP high-mannose glycans profiles between control subjects and pregnant women or patients. It is likely that neither pregnancy nor the pathological conditions examined affect high-mannose chains. In our opinion hydrazinolysis as a method of oligosaccharides liberation, in contrast to enzymatic deglycosylation, is more appropriate for analysis of the sugar moiety of THP.

Adolescent↗
PubMed1997

Stimulation of human keratinocyte growth by alginate oligosaccharides, a possible co-factor for epidermal growth factor in cell culture.

Oligosaccharides, involved in regulation of plant developmental and defensive processes, were tested to determine their ability to enhance proliferation of human keratinocytes. A mixture of alginate oligosaccharides remarkably stimulated keratinocyte growth and [3H]thymidine uptake in the presence of epidermal growth factor (EGF). The activity was comparable to bovine pituitary extract, a common complement in keratinocyte culture, and additive on BPE-induced stimulation. The most effective oligosaccharide in the mixture was identified and its chemical structure was determined. These findings demonstrate a novel activity of alginate oligosaccharide(s) in keratinocyte growth and suggest a possible co-factor for EGF-dependent stimulation in medium for keratinocytes.

Alginates↗
PubMed1998

Jacalin interacts with Asn-linked glycopeptides containing multi-antennary oligosaccharide structure with terminal alpha-linked galactose.

The carbohydrate binding properties of jacalin lectin were examined using RAF9 cell-derived D-[6-3H]glucosamine-radiolabeled total glycopeptides containing N-linked and O-linked oligosaccharides. The binding of N-linked glycopeptides to jacalin was abolished by treatment of alpha-galactosidase whereas O-linked glycopeptides were still bound lectin after this treatment. The removal of O-linked oligosaccharides by mild alkaline/borohydride treatment completely eliminated the lectin binding of alpha-galactosidase treated glycopeptides. These results demonstrate that jacalin interacts with cellular glycopeptides containing N-linked oligosaccharides with terminal alpha-galactose residues as well as glycopeptides containing O-linked oligosaccharides.

Animals↗
PubMed2001

Role of oligosaccharides in the immune response of sheep vaccinated with Lucilia cuprina larval glycoprotein, peritrophin-95.

The larvae of the fly Lucilia cuprina cause a cutaneous myiasis in mammalian hosts, particularly sheep. The glycoprotein, peritrophin-95, isolated from Lucilia cuprina larval peritrophic matrix, is a candidate vaccine antigen. This protein induced an immune response in vaccinated sheep that inhibited larval growth. Recombinant forms of peritrophin-95 were produced in bacteria and baculovirus-infected insect cells. The bacterial protein was not glycosylated and incorrectly folded whereas the insect cell-expressed protein was glycosylated and probably correctly folded. Sheep immunised with purified native peritrophin-95 generated strong larval growth inhibitory activity in their sera, whereas sheep immunised with either recombinant form of peritrophin-95 generated only relatively weak inhibitory activity. Ingested ovine antibodies to native peritrophin-95 mediated the anti-larval growth activity and this was independent of the presence of ovine complement. The activity was associated with IgG(1) and IgG(2) but not IgM. There were strong antibody responses to both the correctly folded native peritrophin-95 polypeptide and the oligosaccharides present on this glycoprotein. Immuno-affinity isolation of antibody to the peritrophin-95 polypeptide and antibody to peritrophin-95 oligosaccharides demonstrated that the larval growth inhibitory activity resided with both antibodies. Lectin blots and ELISA data showed substantial differences between the oligosaccharides attached to native peritrophin-95 and insect cell-expressed recombinant peritrophin-95. It was concluded that the oligosaccharides attached to native peritrophin-95 and its unique polypeptide structure are essential for the induction of larval growth inhibitory activity in the sera of sheep vaccinated with this antigen.

Animals↗
PubMed2001

Resolution of structural isomers of sialylated oligosaccharides by capillary electrophoresis.

The resolution of structural isomers in mixtures of oligosaccharides is often challenging. Capillary electrophoresis was employed to separate three sets of structural isomers of sialylated oligosaccharides found in human milk and bovine colostrum. Different running buffers were necessary to achieve optimal baseline resolution. To resolve 3'- and 6'-sialyllactoses, 0.2 M aqueous sodium phosphate containing 40% methanol as an organic modifier was used as a running buffer. To resolve 3'- and 6'-sialyllactosamines, 0.4 M aqueous sodium phosphate without organic modifier was used. Baseline resolution of sialyllacto-N-tetraose-a and -b and sialyllacto-N-neotetraose-c was achieved with a 0.4 M Tris-HCl buffer containing 250 mM sodium dodecyl sulfate and 10% methanol as the organic modifier. Thus, each of these sets of structural isomers of sialylated oligosaccharides required a unique running buffer with respect to buffer type, concentration, pH, presence of organic modifiers, and surfactants. Similar electrophoresis conditions may be useful for resolving and analyzing other structural isomers of acidic oligosaccharides by capillary electrophoresis.

Carbohydrate Conformation↗