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PubMed2001

Distribution and localization of CMP-N-acetylneuraminic acid hydroxylase and N-glycolylneuraminic acid-containing glycoconjugates in porcine lymph node and peripheral blood lymphocytes.

An immunohistochemical analysis was performed on paraplast-embedded sections of porcine lymph node with antibodies specific for CMP-N-acetylneuraminic acid hydroxylase (h-3 antibody) and glycoconjugate-bound N-glycolylneuraminic acid (Neu5Gc), which appears as a result of the hydroxylase reaction (a-Gc antibody). The observed localization of the enzyme in cells of the perifollicular zone, including lymphocytes, was reflected in a similar distribution of glycoconjugate-bound Neu5Gc. This result confirms previous biochemical investigations on the role of the hydroxylase in regulating Neu5Gc biosynthesis in vitro on a histological level. An analysis of lymphocytes isolated from porcine thymus, spleen, lymph node and peripheral blood revealed differences in the amount of Neu5Gc in the various lymphocytes that correlated well with the activity of the hydroxylase determined in these cells. The largest amount of Neu5Gc and highest activity of the enzyme were detected in the peripheral blood lymphocytes (PBL). Immunohistochemical studies with a-Gc and h-3 antibodies on sections of paraplast-embedded PBL showed that these antigens were located at the cell surface and in the cytosol, respectively. Ultrastructural immunocytochemistry with the h-3 antibody and immunogold labelling was used to investigate the subcellular localization of the hydroxylase. The enzyme was detected in the cytosol in the vicinity of the nuclear membrane and the outer membrane of mitochondria, in particular those close to the nucleus. The antigen was also detected on cytoplasmic tubular structures. In addition, a weak labelling of the Golgi apparatus was also observed occasionally. The possibility that this localization may be related to the availability of the substrate CMP-Neu5Ac and the redox partner cytochrome b5 is discussed.

Animals↗
PubMed2004

Mycobacterium tuberculosis and Mycobacterium avium modify the composition of the phagosomal membrane in infected macrophages by selective depletion of cell surface-derived glycoconjugates.

The growth of pathogenic mycobacteria in phagosomes of the host cell correlates with their ability to prevent phagosome maturation. The underlying molecular mechanism remains elusive. In a previous study, we have shown that Mycobacterium avium depletes the phagosome membrane of cell surface-derived glycoconjugates (de Chastellier and Thilo, Eur. J. Cell Biol. 81, 17-25, 2002). We now extended these quantitative observations to the major human pathogen, Mycobacterium tuberculosis (H37Rv). At increasing times after infection of mouse bone marrow-derived macrophages, cell-surface glycoconjugates were labelled enzymatically with [3H]galactose. Subsequent endocytic membrane traffic resulted in a redistribution of this label from the cell surface to endocytic membranes, including phagosomes. The steady-state distribution was measured by quantitative autoradiography at the electron microscope level. Relative to early endosomes, with which phagosomes continued to fuse and rapidly exchange membrane constituents, the phagosome membrane was depleted about 3-fold, starting during infection and in the course of 9 days thereafter. These results were in quantitative agreement with our previous observations for Mycobacterium avium. For the latter case, we now showed by cell fractionation that the depletion was selective, mainly involving glycoproteins in the 110-210 kDa range. Together, these results indicated that pathogenic mycobacteria induced and maintained a bulk change in phagosome membrane composition that could be of special relevance for survival of pathogenic mycobacteria within phagosomes.

Animals↗
PubMed1995

Role of glycoconjugates in adherence of Salmonella pullorum to the intestinal epithelium of chicks.

1. The distribution of glycoconjugates on the surface of Salmonella pullorum and the ileal epithelium of chicks was demonstrated by lectin cytochemistry. The role of glycoconjugates in adherence of S. pullorum to the ileal epithelium was determined by a sugar inhibition assay using the scanning electron microscope. 2. S. pullorum exhibited binding to Concanavalin A (Con A) and wheat germ agglutinin (WGA) but not to soyabean agglutinin (SBA), Ricinus communis agglutinin (RCA) and Ulex europaeus agglutinin (UEA). 3. The ileal epithelium of chicks bound WGA, Con A and SBA. The binding sites for WGA were on the brush border and cytoplasm of columnar enterocytes as well as on goblet cells. The binding of Con A was confined to the cytoplasm of columnar enterocytes, while SBA bound, in a limited way, to the brush border of columnar enterocytes. 4. After an oral dose of S. pullorum, adherence to the ileal epithelium was inhibited by methyl alpha-D-mannopyranoside.

Animals↗
PubMed2005

Aspects of glycoconjugate production and lysozyme- and defensins-expression of the ceruminous glands of the horse (Equus przewalskii f. dom.).

The distribution of complex glycoconjugates and antimicrobial substances in the ceruminous glands of the horse (Equus przewalskii f. dom., type: pony) was studied using carbohydrate histochemical and immunohistochemical methods. The epithelial cells and luminal secretion of these glands exhibited considerable amounts of glycoconjugates with various saccharide residues, such as alpha-D-mannose, alpha-L-fucose, beta-D-galactose, beta-N-acetyl-D-glucosamine and sialic acid, including O-acetylated sialic acid. Several sugars (alpha-D-mannose, alpha-L-fucose, and beta-D-galactose) were also detectable in the secretion of sebaceous glands present. Additionally, lysozyme and the peptide group of beta-defensins are demonstrated as products of the apocrine ceruminous glands and sebaceous glands. The results obtained are discussed with regard to the functional significance of the glandular secretions. It is suggested that the complex carbohydrates, lysozyme and beta-defensins found in the ceruminous gland secretions are involved in the function of cerumen as a general antimicrobial protective agent in the external auditory canal.

Animals↗
PubMed2003

Protective immunity of pneumococcal glycoconjugates.

Pneumococcal polysaccharides (PSs), designated as T-cell independent type 2 (TI-2) antigens, induce poor immune responses in young children. Splenic marginal zone B cells, associated with CD21, CD19 and C3d, play an important role in TI-2 antibody responses, and provide host defense against bacterial pathogens. Antibody response, avidity, and opsonophagocytic activity of antisera were examined in mice immunized with type 9V PS conjugated to inactivated pneulmolysin (Ply) or to autolysin (Aly). Compared to mice given 9V PS alone, serum IgG and IgM concentrations against the 9V PS were higher in mice immunized with conjugates. High concentrations of serum antibodies were maintained for over 12 weeks. The relative avidities of IgG and IgM antibodies and opsonophagocytic activity against 9V pneumococci were high in mice immunized with conjugates. Thus, conjugate vaccines can induce high as well as long duration of antibody response and effective functional activity. In another study, mice received intranasal immunization with type 9V conjugate or 9V PS. These animals produced 9V PS IgG and IgA antibodies in their serum, spleen, intestine, lung, Peyer's patch and fecal extract samples. Mice immunized with these glycoconjugates exhibited opsonophagocytic activity and rapid bacterial clearance from blood and provided homologous and cross-protection against challenge with virulent pneumococci. These results indicate that intranasal immunization with glycoconjugate vaccines may serve as an alternative and convenient approach for prevention of pneumococcal infection.

Animals↗
PubMed1999

Participation of ABH glycoconjugates in the secretory response to Escherichia coli heat-labile toxin in rabbit intestine.

The ability of membrane ABH blood group-active glycoconjugates to act as receptors of the heat-labile enterotoxin of Escherichia coli (LTh) was studied in vitro and in vivo when GM1 was blocked by the cholera toxin B subunit. Rabbits were classified as AB or H based on intestinal ABH-antigenic activities. Brush border membranes from AB rabbits contained 4 times more LTh binding sites than the H ones. LTh interaction could be inhibited by lectins that recognize ABH determinants. LTh induced a similar dose-dependent secretory response in ligated ileal loops of both types of animals. Anti-AB antibodies and Ulex europaeus I lectin could significantly reduce the fluid accumulation in AB and H rabbits, respectively. LTh caused adenylate cyclase activation even when GM1 was blocked, and this effect was abolished by the addition of specific ABH ligands. These results suggest that ABH glycoconjugates are involved in the host secretory response to LTh in rabbit intestine.

ABO Blood-Group System↗
PubMed2001

Characterization of the antibody response to pneumococcal glycoconjugates and the effect of heat-labile enterotoxin on IGg subclasses after intranasal immunization.

The antibody response to pneumococcal glycoconjugate (Pnc) was characterized by analyzing pneumococcal polysaccharide (PPS)-- and protein carrier-specific IgG subclass profiles and their relationship. Mice were immunized intranasally (inl) or subcutaneously (sc) with Pnc with mutants of Escherichia coli heat-labile enterotoxin, LT-R72 and LT-K63, as mucosal adjuvants. Subcutaneous immunization with Pnc alone induced predominantly IgG1, whereas native PPS administered sc induced very low IgG titers that were exclusively of the IgG3 subclass. Compared with sc immunization with Pnc alone, inl immunization with Pnc and LT mutants induced significantly higher systemic IgG2a, IgG3, and IgA antibodies to both PPS and the carrier, whereas the IgG1 titers were comparable. There also was a significant correlation between PPS- and protein carrier--specific antibody responses for all IgG subclasses. This demonstrates that LT mutants can be used to both enhance and modulate the antibody response to the PS moiety of glycoconjugate vaccines.

Adjuvants, Immunologic↗
PubMed1999

Heterogeneous expression of glycoconjugates among individual glomeruli of the hamster main olfactory bulb.

Glomeruli within the main olfactory bulb (MOB) are known as areas of synapse formation between axon terminals of olfactory neurons in the olfactory epithelium and dendrites of the first relay neurons (mitral and tufted cells) in the MOB, so that they serve as functional units in olfaction. We examined expression patterns of glycoconjugates in the glomeruli of the hamster MOB by lectin histochemistry using 21 biotinylated lectins. Thirteen lectins, WGA, s-WGA, DSL, DBA, SBA, WA, SJA, RCA-I, PNA, ECL, UEA-I, PSA and LCA, showed differential binding patterns among the glomeruli. To evaluate these differential binding patterns of lectins, we analysed staining intensity of each of the 13 lectins on the level of individual glomeruli by image analysis, and classified staining intensity into five grades (negative, 1+, 2+, 3+, 4+) on the basis of results obtained. This classification enables us to make detailed comparison among individual glomeruli. We further analysed the grade of staining intensity of each of the 13 lectins in the same glomerulus in adjacent serial sections by image analysis, and found that individual glomeruli varied in combination of grades of staining intensity and kinds of lectins. These results indicate that glycoconjugates are expressed heterogeneously in individual glomeruli, and that heterogeneous expression may contribute to the topographic organization of the primary olfactory pathway.

Animals↗
PubMed2001

Glycoconjugate structures of parasitic protozoa.

Glycoconjugates are abundant and ubiquitious on the surface of many protozoan parasites. Their tremendous diversity has implicated their critical importance in the life cycle of these organisms. This review highlights our current knowledge of the major glycoconjugates, with particular emphasis on their structures, of representative protozoan parasites, including Leishmania, Trypanosoma, Giardia, Plasmodia, and others.

Animals↗
PubMed1995

Galactofuranose-containing glycoconjugates in trypanosomatids.

Galactofuranose has been characterized in glycoinositolphospholipid (GIPL) anchor-like structures having a glycerolipid or a ceramide, as in lipopeptidophosphoglycan (LPPG) of Trypanosoma cruzi, in the oligosaccharide core of lipopeptidophosphoglycan (LPG) of Leishmania species, and also modifying high-mannose chains of trypanosomatid glycoproteins. Galactofuranose is usually present linked beta 1-->3 to Man, either as a terminal non-reducing unit, like in LPPG, or in the middle of the oligosaccharide core, as in LPG. The presence in protozoan parasites of galactose in the furanose configuration is a feature which deserves further attention since the mammalian hosts do not appear to produce glycoconjugates containing this structural unit. For that reason, hosts produce antibodies against galactofuranose, which may turn out to be important in understanding the pathogenesis and in the development of diagnostic methods. The metabolic pathways involved in the attachment to or removal of galactofuranose from glycoconjugates have not yet been elucidated. This is an area of incipient research, but of growing importance, since it will foster the design of inhibitors which may prove to be useful for the treatment of disease.

Animals↗
PubMed2005

Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays.

The microaerophilic bacterium Helicobacter pylori is well established for its role in development of different gastric diseases. Bacterial adhesins and corresponding binding sites on the epithelial surface allow H. pylori to colonize the gastric tissue. In this investigation, the adhesion of H. pylori to dot blot arrays of natural glycoproteins and neoglycoproteins was studied. Adhesion was detected by overlay with fluorescence-labeled bacteria on immobilized (neo)glycoproteins. The results confirmed the interaction between the adhesin BabA and the H-1-, Lewis b-, and related fucose-containing antigens. In addition, H. pylori bound to terminal alpha2-3-linked sialic acids as previously described. The use of a sabA mutant and sialidase treatment of glycoconjugate arrays showed that the adherence of H. pylori to laminin is mediated by the sialic acid-binding adhesin, SabA. The adhesion to salivary mucin MUC5B is mainly associated with the BabA adhesin and to a lesser extent with the SabA adhesin. This agrees with reports, that MUC5B carries both fucosylated blood group antigens and alpha2-3-linked sialic acids. The adhesion of H. pylori to fibronectin and lactoferrin persisted in the babA/sabA double mutant. Because binding to these molecules was abolished by denaturation rather than by deglycosylation, it was suggested to depend on the recognition of unknown receptor moieties by an additional unknown bacterial surface component. The results demonstrate that the bacterial overlay method on glycoconjugate arrays is a useful tool for exploration and the characterization of unknown adhesin specificities of H. pylori and other bacteria.

Adhesins, Bacterial↗
PubMed2006

Structural characterization of N-glycans from the freshwater snail Biomphalaria glabrata cross-reacting with Schistosoma mansoni glycoconjugates.

The human parasitic trematode Schistosoma mansoni has a complex life cycle that includes the freshwater snail Biomphalaria glabrata as intermediate host. Within each stage, the parasite synthesizes a wide array of glycoconjugates, exhibiting, in part, unique carbohydrate structures. In addition, the parasite expresses definitive host-like sugar epitopes, such as Lewis X determinants, supporting the concept of carbohydrate-mediated molecular mimicry as an invasion and survival strategy. In the present study, we investigated whether common carbohydrate determinants occur also at the level of the intermediate host. To this end, a structural characterization of hemolymph glycoprotein-N-glycans of B. glabrata was performed. N-glycans were released from tryptic glycopeptides and labeled with 2-aminopyridine. Sugar chains serologically cross-reacting with S. mansoni glycoconjugates were isolated by immunoaffinity chromatography using a polyclonal antiserum directed against schistosomal egg antigens and fractionated by Aleuria aurantia lectin affinity chromatography and high-performance liquid chromatography. Obtained glycans were analyzed by different mass spectrometric techniques as well as by monosaccharide constituent and linkage analysis. The results revealed a highly heterogeneous oligosaccharide pattern. Cross-reacting species represented about 5% of the total glycans and exhibited a terminal Fuc(alpha1-3)GalNAc unit, a (1-2)-linked xylosyl residue, or both types of structural motifs. In conclusion, our study demonstrates the presence of common carbohydrate epitopes also at the level of S. mansoni and its intermediate host.

Animals↗
PubMed1999

Detection of glycoconjugates by lectin gold labelling, silver enhancement, and scanning electron microscopy.

A method for detecting glycoconjugates on cell surfaces in scanning electron microscopy is described. Terminal saccharides were specifically recognized by a lectin conjugated to biotin, and, after incubation with an anti-biotin antibody conjugated to colloidal gold, silver enhancement was used to produce deposits large enough to be detected in standard scanning electron microscopes. Secondary electron images revealed the ultrastructure of the tissue investigated, while backscattered electron images showed the distribution of lectin binding sites. Using digital recording and processing, the two channels were combined in colour-encoded images. The new method brings together lectin histochemistry and scanning electron microscopy and thus allows the three-dimensional distribution of glycoconjugates to be analysed at an ultrastructural level.

Animals↗
PubMed1999

Up-regulation of the alpha2,6-sialyltransferase messenger ribonucleic acid increases glycoconjugates containing alpha2, 6-linked sialic acid residues in granulosa cells during follicular atresia of porcine ovaries.

The sugar chains in cellular glycoconjugates have many biological functions. Extensive morphological development and remodeling occur in the ovary of female animals. This caused us to study glycobiological characteristics of ovarian cells, particularly granulosa cells that undergo apoptosis during follicular atresia. The lectin Sambucus sieboldiana agglutinin (SSA) specific for Siaalpha2,6Gal/GalNAc showed positive staining for granulosa cells only in atretic follicles of porcine ovaries by lectin histochemistry. Lectin blot analysis for SSA demonstrated specific glycoproteins only in atretic follicles. Furthermore, we performed analysis of backbone structures of SSA-positive glycans carried by granulosa cell glycoproteins increased during atresia by glycosidase treatment. Most of these structures were Siaalpha2,6Galbeta1,4GlcNAc on complex-type N-glycans, suggesting that only ST6Gal I of four distinct alpha2,6-sialyltransferases catalyzes alpha2,6-sialic acid transfer in most of the increased glycoproteins of granulosa cells during follicular atresia. Reverse transcription-polymerase chain reaction analysis demonstrated that the expression of ST6Gal I mRNA was up-regulated in granulosa cells during atresia. These results suggested that the alteration of glycoconjugates by ST6Gal I in granulosa cells during atresia is involved in some processes of ovarian follicular atresia and granulosa cell apoptosis.

Animals↗
PubMed1989

Effect of sodium butyrate, a differentiating agent, on cell surface glycoconjugates of a human pancreatic cell line.

The effects of sodium butyrate, a differentiating agent, on growth properties and glycoconjugates of a human pancreatic carcinoma cell line (CAPAN-1) were studied. Butyrate caused marked changes of in vitro growth properties including prolongation of doubling time and greatly reduced colony forming efficiency in soft agar. Cell surface labeling revealed significant alterations in proteins and glycoproteins after treatment with sodium butyrate (appearance of glycoproteins of molecular weight 250,000, 220,000, and 70,000; reduction of glycoproteins of 164,000, 148,000, 110,000, and 66,800 sizes; increases in proteins/glycoproteins of 85,000 and 78,000). Metabolic labeling of the cells with [3H]fucose or [3H]galactose revealed that sodium butyrate treatment caused a marked reduction in the fucose-containing neutral glycolipids with six or more carbohydrate side chains and an increase in [3H]galactose-labeled neutral glycolipids, particularly GL-3a, GL-4a, and GL-5a. There was marked reduction in the labeling of a ganglioside with mobility similar to that of GM4 and of sulfogalactosylceramide. An increase in a ganglioside with mobility above GM1 was also caused by butyrate. These data indicate that sodium butyrate may be useful in the identification of differentiation or malignancy-associated glycoconjugate markers of human pancreatic cells.

Butyrates↗
PubMedDate not supplied

Mapping of receptors for carbohydrate constituents of glycoconjugates in well-differentiated and malignant ependymomas: a glycohistochemical study.

Recognitive interactions between the carbohydrate part of cellular glycoconjugates and endogenous receptors supposedly govern important biological processes. Consequently, their elucidation can be of considerable value in tumour diagnosis. The histochemical patterns of expression of endogenous sugar receptors (e.g. endogenous lectin-like proteins) of 10 cases of well-differentiated ependymoma and 10 cases of malignant ependymoma were analysed, using a panel of 18 biotinylated (neo)glycoproteins and a standardized staining protocol. Within this panel, differences in the extent of staining for intracellular sugar receptors in well-differentiated and malignant ependymomas were histochemically detectable. In comparison to the well-differentiated ependymomas, the anaplastic form of the tumour exhibited a generally higher capacity to specifically bind labelled (neo)glycoproteins, containing alpha- or beta-glucosides and a disaccharide, characteristic for one type of beta-galactoside-terminated chain structure of glycoproteins. A significantly reduced binding was seen for tumours of the anaplastic type with labelled markers, carrying histochemically indispensable glucuronic acid residues. These findings suggest that labelled neoglycoproteins are a valuable tool for assessing the endogenous sugar-binding capacity in diagnostic histopathology. Our descriptive analysis of endogenous sugar receptors may also be a rational basis for studies on the functional significance of changes in the expression of their endogenous ligands and the cellular glycoconjugates. Further investigations are also possible on the correlation between the degree of differentiation and expression of both parts of a recognitive system, based on protein (receptor)-carbohydrate (ligand) interactions, in tumours of the central nervous system, especially ependymomas.

Brain Neoplasms↗
PubMed1993

Lectin histochemistry of glycoconjugates in horse salivary glands.

The glycoconjugate content of major horse salivary glands was investigated by means of horseradish peroxidase-conjugated lectins. Qualitative differences were observed in the terminal sugar residues of secretory glycoproteins and glycoconjugates linked to the apical surface of excretory duct epithelial cells. Mucous acinar cells in mandibular and sublingual glands contained oligosaccharides with D-galactose, alpha- and beta-N-acetylgalactosamine, N-acetylglucosamine and fucose residues, whereas mandibular, sublingual and parotid serous cells contained only oligosaccharides with terminal alpha- and beta-N-acetylgalactosamine residues. The apical portion of striated and interlobular duct lining cells of mandibular and sublingual glands stained for alpha- and beta-N-acetylgalactosamine and for N-acetylglucosamine. In parotid gland the cytoplasm of intercalated duct cells and the apical surface of striated duct epithelial cells stained for alpha-N-acetylgalactosamine.

Animals↗
PubMed2006

Cell surface lectin-binding glycoconjugates on marine planktonic protists.

Carbohydrate-protein interactions appear to play an important role in the phagocytosis of microbial prey by free-living protozoa. The present study utilizes FITC-labelled plant lectins to investigate the presence and localization of cell surface glycoconjugates on live and fixed planktonic protists (Dunaliella primolecta, Oxyrrhis marina, Goniomonas amphinema, Paraphysomonas vestita and Euplotes vannus). With live flagellate preparations, lectins primarily bound to external cell surfaces, with minimal internal staining observed. In contrast, cell fixation permeabilized cell membranes, allowing lectins to bind to internal structures, such as nuclear membranes and food vacuoles, interfering with the characterization of cell surface glycoconjugates. The method developed to label cell surface sugar moieties of live planktonic protists successfully overcomes the problems associated with fixation, and thus provides a useful protocol for future studies on protistan cell surface carbohydrate characterization.

Animals↗