scholarly journals Studies on the relationship between lectin binding carbohydrates and different strains of Leishmania from the New World

1982 ◽  
Vol 77 (1) ◽  
pp. 19-27 ◽  
Author(s):  
J. Schottelius ◽  
S. C. Gonçalves da Costa
Keyword(s):  
Phaseolus Vulgaris ◽  
Arachis Hypogaea ◽  
New World ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Dolichos Biflorus ◽  
Canavalia Ensiformis ◽  
Ulex Europaeus ◽  
Different Strains ◽  
The Relationship

The culture forms of L. mexicana pifanoi (LRC L-90), L. mexicana mexicana (LRC L-94, M-379); L. braziliensis braziliensis (LRC L-77, L-1, M-2903, H-LSS) and L. mexicana amazonensis (H-JMMO, M-JOF, H-21, H-PLL,M-1696) were tested with the following lectins: Canavalia ensiformis, Ricinus communis-120, Axinella polypoides, Phaseolus vulgaris, Evonymus europaeus, lotus tetragonolobus, Dolichos biflorus, Aaptos papillata II, Laburnum alpinum, Ulex europaeus, Arachis hypogaea and Soja hispida. All examined strains of Leishmania were agglutinated by C. ensiformis, R. communis-120 and A. popypoides. No agglutination reactions were observed with P. vulgaris, D.biflorus, A. papillata II, E. europaeus and L. tetragonolobus. Only L. m. pifanoi and the L. m. amazonensis strains H-JMMO and MJOF showed agglutination reactions with S. hispida, U. europaeus, L. alpinum and A. hypogaea, while L. m. mexicana (LRC L-94; M-379) strains, L. b. braziliensis H. LSS, LRC L-77; L-1; M-2903 and the L. m. amazonensis strains, H-PLL, H-21, M-1696 showed no agglutination reactions with these four lectins.

Echinostoma caproni and E. trivolvis alter the binding of glycoconjugates in the intestinal mucosa of C3H mice as determined by lectin histochemistry

1993 ◽  
Vol 67 (3) ◽  
pp. 179-188 ◽  
Author(s):  
T. Fujino ◽  
B. Fried
Keyword(s):  
Ricinus Communis ◽  
Villous Atrophy ◽  
Lectin Binding ◽  
Goblet Cells ◽  
Lectin Histochemistry ◽  
Dolichos Biflorus ◽  
Echinostoma Caproni ◽  
Ulex Europaeus ◽  
C3h Mice ◽  
Small Intestines

AbstractMouse (C3H) mucosal glycoconjugates were examined in normal small intestines and intestines infected with Echinostoma caproni, or E. trivolvis using six different fluorescein-conjugated lectins: Triticum, vulgaris agglutinin (WGA), Ulex europaeus agglutinin I (UEA-I), Ricinus communis agglutinin I (RCA-I). Glycine max soybean agglutinin (SBA), Dolichos biflorus agglutinin (DBA), and Arachis hypogaeu peanut agglutinin (PNA). The expression of lectin-binding sites and the intensity of the binding of lectins in the mouse small intestines were changed by infection with the echinostomes. Specific differences in the reaction to glycoproteins were clearly observed between the mouse intestines infected with E. caproni and those infected with E. trivolvis. In E. caproni infection, binding of most of the lectins to the villi was remarkably reduced in accord with the villous atrophy and loss of goblet cells. In contrast, in E. trivolvis infection, the binding of WGA, RCA-I and DBA was reduced in the microvillar surfaces, but binding of UEA-I and SBA were unchanged compared to the control intestines. The lectin binding to goblet cells in E. trivolvis-infected mice mostly increased. These observations may reflect the marked increase in goblet cells and the less severe damage in the villi of E. trivolvis infection compared to E. caproni infection. Most of the glycoconjugates were slightly reduced in the hyperplastic crypts except for N-acetyl glucosamine. It is possible that glucose metabolism in the host intestines infected with E. trivolvis was activated. resulting in an increase in the rate of mucin synthesis as well as qualitative changes in mucus, thereby mediating the expulsion of the worms.

scholarly journals A comparison of lectin binding in rat and human peripheral nerve.

1986 ◽  
Vol 34 (11) ◽  
pp. 1487-1493 ◽  
Author(s):  
A K Gulati ◽  
A A Zalewski ◽  
K B Sharma ◽  
D Ogrowsky ◽  
G S Sohal
Keyword(s):  
Peripheral Nerves ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Nerve Degeneration ◽  
Binding Affinities ◽  
Light Microscopic Level ◽  
Dolichos Biflorus ◽  
Ulex Europaeus ◽  
Maclura Pomifera ◽  
Subsequent Regeneration

Eleven different fluorescein- or peroxidase-conjugated lectins with different sugar-binding affinities were employed to analyze and compare glycoconjugates of rat and human peripheral nerves at the light microscopic level. A majority of lectins showed a distinct binding pattern in different structures of the nerve. Lectin binding was similar but not identical in rat and human nerves. Limulus polyhemus agglutinin did not stain any structures in rat or human nerves. In both species, all other lectins bound to the perineurium. Perineurial staining was intense with Canavalia ensiformis (Con A), Triticum vulgaris (WGA), Maclura pomifera (MPA); moderate with Glycine max (SBA), Griffonia simplicifolia-I (GS-I) and GS-II; weak with Ulex europaeus (UEA), Dolichos biflorus (DBA), and Ricinus communis (RCA). In the endoneurium of both species, ConA staining was intense, MPA and WGA moderate, SBA, GS-II, PNA, and RCA weak, and UEA and DBA absent. Interestingly, GS-I stained rat but not human endoneurium. Most lectins bound to blood vessels. GS-I bound to rat but not human, whereas UEA bound to human but not rat vessels. The results show that lectins can be used to reveal heterogeneity in sugar residues of glycoconjugates within neural and vascular components of nerves. They may therefore be potentially useful in detecting changes in glycoconjugates during nerve degeneration and subsequent regeneration after trauma or in pathological states.

scholarly journals A cytochemical study of lectin receptors on isolated chick neural retina neurons in vitro

1982 ◽  
Vol 53 (1) ◽  
pp. 1-20
Author(s):  
J.A. Bee
Keyword(s):  
Sialic Acid ◽  
Cell Body ◽  
Growth Cone ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Neuronal Cell ◽  
Cytochemical Study ◽  
Lectin Receptors ◽  
Dolichos Biflorus ◽  
Dolichos Biflorus Agglutinin

The cell body, neurite and growth cone of isolated retinal neurons have been compared on the basis of their ability to bind a number of fluorescently labelled lectins, each possessing a unique carbohydrate specificity. The susceptibility of the respective binding patterns following pretreatment of these fixed cells with either neuraminidase or trypsin was also investigated. Neuronal cell bodies displayed the most intense binding of each lectin, with localization of limulin binding (specific for sialic acid) predominantly to the neurite hillock, the point on the cell body from which the neurite projects. Limulin binding was almost totally abolished by pretreatment with either neuraminidase or trypsin. In contrast to the cell body, limulin binding to the neurite or growth cone was not detected. These regions of the cell apparently possessed sialic acid, however, since pretreatment with neuraminidase reduced wheat germ agglutinin binding (to N-acetylglucosamine) and markedly enhanced Dolichos biflorus agglutinin binding (to N-acetylgalactosamine) to both the neurite and growth cone. The initially low binding of Dolichos biflorus agglutinin to the neurite and growth cone was slightly enhanced by pretreatment with trypsin. Uniformly low levels of binding of either Ricinus communis agglutinin 60 (galactose, N-acetylgalactosamine) or R. communis agglutinin 120 (galactose) was observed over the entire neuron. R. communis agglutinin 120 binding was not enhanced by pretreatment with neuraminidase. Receptors for either concanavalin A (mannose, glucose) or Ulex europaeus agglutinin I (fucose) were abundant over the entire nerve cell with the former exhibiting more marked trypsin sensitivity. From these data, it is apparent that the repertoire of lectin binding sites of the neurite and growth cone of these differentiating nerve cells differs markedly from that of the cell body, which itself demonstrates some degree of regionalization.

scholarly journals Localization of carbohydrate components in rat colon with fluoresceinated lectins.

1978 ◽  
Vol 26 (6) ◽  
pp. 452-458 ◽  
Author(s):  
E Essner ◽  
J Schreiber ◽  
R A Griewski
Keyword(s):  
Epithelial Cells ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Ricinus Communis ◽  
Rat Colon ◽  
Dolichos Biflorus ◽  
Ulex Europaeus ◽  
Descending Colon ◽  
Carbohydrate Components ◽  
Cryostat Sections

Cryostat sections of rat descending colon were studied by fluorescence microscopy after exposure to conjugates of fluorescein isothicoyanate with lectins from Glycine max (soybean), Triticum vulgaris (wheat germ), Ricinus communis (castor bean), Ulex europaeus, (gorse), Dolichos biflorus (horse gram) and Canavalia ensiformis (concanavalin A) (Jack bean). No two lectins showed identical patterns of fluorescence. FITC-conjugates of soybean and D. biflorus lectins reacted strongly with the mucus present in the crypt lumens and with the surface (as well as cytoplasm) of the epithelial cells suggesting that these sites are rich in terminal, non-reducing, N-acetylgalactosamine residues. Wheat germ, R. communis, U. europaeus and concanavalin A-FITC conjugates did not stain mucus but showed fluorescence in the cytoplasm of absorptive cells as well as in the lamina propria and submucosa. The FITC-R. communis conjugate also reacted with structures in the apical portion of epithelial cells that may correspond to the Golgi apparatus.

scholarly journals A lectin-binding glycoprotein of Mr 135,000 associated with basal keratinocytes in pig epidermis

1986 ◽  
Vol 237 (2) ◽  
pp. 405-414 ◽  
Author(s):  
I A King ◽  
A Tabiowo ◽  
F M Pope
Keyword(s):  
Basal Cell ◽  
Concanavalin A ◽  
High Speed ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Polyacrylamide Gel Electrophoresis ◽  
Basal Layer ◽  
Particulate Fraction ◽  
Ulex Europaeus ◽  
Stratified Epithelia

Pig epidermis separated by 1 M-CaCl2 treatment was homogenized and separated into three fractions by filtration through nylon mesh and high-speed centrifugation. Lectin-binding glycoproteins were isolated from urea/deoxycholate/mercaptoethanol extracts of the residue fraction that resisted filtration, from deoxycholate extracts of the particulate material in the filtrate and from the soluble fraction. Concanavalin A, Ricinus communis (castor bean) agglutinin 1, peanut (Arachis hypogaea) agglutinin and Ulex europaeus (gorse) agglutinin-binding glycoproteins in the three epidermal fractions were analysed by SDS/polyacrylamide-gel electrophoresis. A major neuraminidase-sensitive glycoprotein component of the particulate fraction of Mr 135,000 was strongly bound by concanavalin A and Ricinus communis agglutinin 1, but only weakly by peanut and Ulex europaeus agglutinins. This glycoprotein was not detected in the residue or soluble fractions of the epidermis, indicating that it had only a limited distribution within the tissue. The 135,000-Mr glycoprotein was one of two major glycoprotein antigens in the particulate fraction. Rabbits immunized with total particulate glycoproteins produced antibodies directed mainly against 135,000- and 110,000-Mr components. Monospecific antibodies were obtained from guinea pigs immunized with the 135,000-Mr glycoprotein band excised from polyacrylamide gels. Indirect immunofluorescence with the use of affinity-purified antibodies showed that the 135,000-Mr glycoprotein was present at the surface of cells in the basal layer of the epidermis as well as at that of other stratified epithelia. It was not present on differentiating cells in the suprabasal layers of the epithelium, suggesting an important role in the attachment or proliferative functions of basal cells in stratified epithelia. Metabolic labelling studies with skin explants cultured in the presence of D-[3H]glucosamine showed that this basal-cell glycoprotein was synthesized by cultured tissue. The major D-[3H]glucosamine-labelled glycoprotein component in the residue and particulate fractions of cultured epidermis had an Mr of 135,000, was immunoprecipitated by rabbit antisera raised against particulate epidermal glycoproteins and was bound by concanavalin A. The labelling of this glycoprotein with D-[3H]glucosamine was sensitive to tunicamycin, indicating that the basal-cell glycoprotein contained N-glycosidically linked oligosaccharides.

Swainsonine Toxicosis Mimics Lectin Histochemistry of Mannosidosis

1985 ◽  
Vol 22 (4) ◽  
pp. 311-316 ◽  
Author(s):  
J. Alroy ◽  
U. Orgad ◽  
A. A. Ucci ◽  
V. E. Gavris
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Ricinus Communis ◽  
Lectin Histochemistry ◽  
Dolichos Biflorus ◽  
Ulex Europaeus ◽  
Lectin Staining ◽  
Astragalus Lentiginosus ◽  
Cytoplasmic Vacuoles ◽  
Ulex Europaeus Agglutinin I

Cells affected by locoweed (Astragalus lentiginosus) and Swainsona galegifolia toxicosis or mannosidosis exhibit similarities in their catabolism of N-linked glycoproteins and accumulation of cytoplasmic vacuoles. We used nine different biotinylated lectins as histochemical markers for specific sugars and avidin-biotin-peroxidase complex as a visualant to study the cells affected with these conditions. Since locoweed and Swainsona spp block mannosidase activity, we expected a similar lectin staining pattern in cells under these conditions as that seen in mannosidosis. Concanavalia ensiformis agglutinin, wheat germ agglutinin and succinyl wheat germ agglutinin stained the undegraded glycoproteins and oligosaccharides stored in the lysosomes of affected cells in all three conditions. Bandeirea simplicifolia-I, Dolichos biflorus agglutinin, peanut agglutinin, Ricinus communis agglutinin-I, soybean agglutinin and Ulex europaeus agglutinin-I did not stain any of these cells. These results indicate that in all three conditions there is an accumulation of undegraded oligosaccharides that contain α-mannosyl and β-N-acetyl glucosamine residues which are revealed by lectin staining in the vacuoles of all affected cells.

Modification of the outer surface of Erwinia carotovora ssp. atroseptica by the phytoalexin rishitin

1985 ◽  
Vol 31 (12) ◽  
pp. 1108-1112 ◽  
Author(s):  
W. M. Robertson ◽  
G. D. Lyon ◽  
C. E. Henry
Keyword(s):  
Outer Surface ◽  
Ricinus Communis ◽  
Periodic Acid ◽  
Membrane Integrity ◽  
Fluorescein Isothiocyanate ◽  
Erwinia Carotovora ◽  
Limulus Polyphemus ◽  
Dolichos Biflorus ◽  
Ulex Europaeus

The phytoalexin rishitin (500 μg/mL) modified the wall of Erwinia carotovora ssp. atroseptica by removing an outer layer and causing holes to appear through which the cell contents were extruded. A lower concentration of rishitin (300 μg/mL) produced effects on the cytoplasm visible by electron microscopy but no obvious differences in membrane integrity, although sections stained with the periodic acid – thiosemicarbazide – silver proteinate reaction showed a reduction in the intensity with which the carbohydrate layer in the outer membrane was stained which was similar to that found at the higher concentration (500 μg/mL). Labelling rishitin-treated cells with cationized ferritin showed the presence of negative charges on the outer surface of all cells treated with 500 μg rishitin/mL which were absent on nontreated cells and present in only a few cells treated with 300 μg/mL. After incubation of E. carotovora ssp. atroseptica with rishitin, cells bound to fluorescein isothiocyanate labelled lectins from Ricinus communis, Solanum tuberosum, and Triticum vulgaris and rhodamine-labelled avidin; cells of E. carotovora spp. atroseptica treated with ethanol were not labelled. Rishitin-treated cells did not bind to lectins from Arachis hypogaea, Dolichos biflorus, Glycine max, Limulus polyphemus, or Ulex europaeus. These results suggest that the phytoalexin rishitin can modify existing sites or expose previously blocked sites which may be involved in host–pathogen recognition, and may therefore indicate a reinforcement of other recognition processes in vivo.

scholarly journals Changes in the glycosylation pattern during embryonic development of mouse kidney as revealed with lectin conjugates.

1987 ◽  
Vol 35 (1) ◽  
pp. 55-65 ◽  
Author(s):  
L Laitinen ◽  
I Virtanen ◽  
L Saxén
Keyword(s):  
Binding Sites ◽  
Ricinus Communis ◽  
Collecting Duct ◽  
Lectin Binding ◽  
Mouse Kidney ◽  
Kidney Cortex ◽  
Glycosylation Pattern ◽  
Dolichos Biflorus ◽  
Functional Maturation ◽  
Adult Kidney

Distribution of lectin-binding sites in adult and developing mouse kidney was studied with fluorochrome- and peroxidase-coupled lectins. Effects of fixation methods on lectin-binding patterns were also compared. Un-induced mesenchymal cells and ureter bud of the early metanephros reacted with Concanavalin A, Lens culinaris, Ricinus communis I, and wheat germ agglutinins, whereas binding sites for both soybean and peanut (PNA) agglutinins were seen only in ureter bud tissue. On induction, PNA positivity rapidly appeared in the induced, condensed areas of the metanephrogenic mesenchyme. Early glomeruli expressed heterogeneously terminal galactosyl and N-acetylgalactosaminyl moieties in the podocytes. Later, these sites disappeared and were apparently covered by sialic acids. Endothelia also displayed a comparable sialylation of terminal saccharide moieties during maturation. Binding sites for many of the above lectins were also found in the developing proximal and distal tubules. Terminal fucosyl residues, characteristic of mature proximal tubules, appeared during day 13 of development. Dolichos biflorus agglutinin reactivity, typically seen in the collecting ducts, appeared by day 13. Griffonia simplicifolia-I-B4 isolectin reactivity was exclusively localized to endothelial in adult kidney cortex, but in embryonic kidneys reactivity with collecting duct and podocytes was also seen. These results suggest that the compartmentalized expression of cell glycoconjugates in adult mouse kidney is acquired in a sequential manner during development. Such sequential appearance of the mature glycosylation pattern probably reflects functional maturation of the nephron.

Opisthorchis viverrini: ultrastructure and cytochemistry of the glycocalyx of the tegument

2000 ◽  
Vol 74 (1) ◽  
pp. 23-29 ◽  
Author(s):  
W. Apinhasmit ◽  
P. Sobhon ◽  
C. Tarasub ◽  
W. Mothong ◽  
P. Saitongdee ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Binding Sites ◽  
Ricinus Communis ◽  
Ruthenium Red ◽  
Opisthorchis Viverrini ◽  
Binding Studies ◽  
Con A ◽  
Colloidal Iron ◽  
Dolichos Biflorus ◽  
Ulex Europaeus

AbstractThe ultrastructure and cytochemistry of the glycocalyx of the tegument of Opisthorchis viverrini during maturation from newly excysted juvenile to adult stages were investigated using colloidal iron, ruthenium red and lectin stainings. The results showed that the glycocalyx was intensely stained by the first two dyes, thus indicating the presence of relatively high amounts of negative charges. However, the thickness and intensity of the staining decreased during the fluke's maturation. Binding studies using lectin probes on the surface of adult parasites showed that binding sites for Canavaliaensiformis (Con A), Triticum vulgaris (WGA) and Ricinus communis I(RCA I) were present in relative large amounts on the glycocalyx of the adult tegument, whereas those for Dolichos biflorus (DBA) were relatively fewer in number, and those for Ulex europaeus I (UEA I) were absent. The binding patterns of Con A, WGA, RCA I and DBA were generally similar, and the reaction product was uniformly distributed over the dorsal and ventral surfaces of the parasite's body. These bindings, therefore, indicate the presence of D-mannose/D-glucose, N-acetyl-D-glucosamine/sialic acid, D-galactose and N-acetyl-D-galactosamine residues on the glycocalyx of the adult tegument.

Lectin Binding to Human Breast Tumor Cells

1976 ◽  
Vol 34 ◽  
pp. 34-35
Author(s):  
Robert E. Nordquist ◽  
J. Hill Anglin ◽  
Michael P. Lerner
Keyword(s):  
Carcinoma Cell ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Low Frequency ◽  
Breast Carcinoma Cell Line ◽  
Human Breast ◽  
Human Breast Tumor ◽  
Duct Carcinoma ◽  
Specific Antigens ◽  
Ricin Agglutinin

A human breast carcinoma cell line (BOT-2) was derived from an infiltrating duct carcinoma (1). These cells were shown to have antigens that selectively bound antibodies from breast cancer patient sera (2). Furthermore, these tumor specific antigens could be removed from the living cells by low frequency sonication and have been partially characterized (3). These proteins have been shown to be around 100,000 MW and contain approximately 6% hexose and hexosamines. However, only the hexosamines appear to be available for lectin binding. This study was designed to use Concanavalin A (Con A) and Ricinus Communis (Ricin) agglutinin for the topagraphical localization of D-mannopyranosyl or glucopyranosyl and D-galactopyranosyl or DN- acetyl glactopyranosyl configurations on BOT-2 cell surfaces.

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