Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin

1991 ◽  
Vol 213 ◽  
pp. 69-77 ◽  
Author(s):  
M. Islam Khan ◽  
Dipak K. Mandal ◽  
C.Fred Brewer
Keyword(s):  
Concanavalin A ◽  
Soybean Agglutinin

Changing surface antigen and carbohydrate patterns during the development of Oesophagostomum dentatum

Parasitology ◽  
1999 ◽  
Vol 119 (5) ◽  
pp. 491-501 ◽  
Author(s):  
A. JOACHIM ◽  
B. RUTTKOWSKI ◽  
A. DAUGSCHIES
Keyword(s):  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Soybean Agglutinin ◽  
Peanut Agglutinin ◽  
Oesophagostomum Dentatum ◽  
Periodate Treatment

Living and fixed specimen of Oesophagostomum dentatum were labelled in situ with serum antibodies or a panel of biotin- labelled lectins. Specific binding of antibodies was observed in all parasitic stages – freshly exsheathed 3rd-stage larvae (L3), 3rd- and 4th-stage (L4) larvae cultured in vitro and L3 and L4 and adults isolated from pig intestines. The shedding of the stained layer by motile larvae was inhibited by levamisole-induced paralysis. Larvae cultured in vitro exposed serum-derived proteins on their surface which could be labelled with secondary antibody directed against the respective serum donor species. While freshly exsheathed larvae were recognized by O. dentatum-positive serum only, older larvae and adults cross-reacted with serum from pigs infected with O. quadrispinulatum, a closely related species. Lectin binding varied considerably between stages. While binding was not observed in pre-parasitic stages, Concanavalin A, Soybean Agglutinin, Wheat Germ Agglutinin, Ricinus communis Agglutinin and Peanut Agglutinin bound to developing larvae in varying degrees. Dolichos biflorus Agglutinin only bound to advanced (luminal) larval stages, while adults generally displayed only weak or partial lectin binding (except with Concanavalin A and Wheat Germ Agglutinin). Ulex europaeus Agglutinin only labelled larvae derived from cultures containing 10% pig serum. Cleavage of the carbohydrate residues by sodium periodate treatment resulted in reduction of antibody binding to cultured larvae, but not to freshly exsheathed L3. Concanavalin A, Soybean Agglutinin, and Peanut Agglutinin binding was also reduced by periodate treatment, while binding of Wheat Germ Agglutinin and Ricinus communis Agglutinin was inhibited only in early L3, but not in older stages. The different lectin labelling patterns are related to the different stages of the nematode – infective, invasive, histotropic, and luminal – and may serve as a mode of adaptation for the parasite against the host's immune attack by surface glycoprotein variation, together with antigen shedding (as demonstrated by labelling of motile larvae) and a possible acquisition of host molecules at the parasite's surface. Furthermore, a possible role of this developmental variation in surface carbohydrates in parasite–parasite interactions is discussed.

scholarly journals Unfolding Studies on Soybean Agglutinin and Concanavalin A Tetramers: A Comparative Account

2005 ◽  
Vol 88 (2) ◽  
pp. 1300-1310 ◽  
Author(s):  
Sharmistha Sinha ◽  
Nivedita Mitra ◽  
Gyanendra Kumar ◽  
Kanika Bajaj ◽  
Avadhesha Surolia
Keyword(s):  
Concanavalin A ◽  
Soybean Agglutinin

Differential redistribution of lectin receptor classes on clonal rat myotubes and myoblasts

1986 ◽  
Vol 83 (1) ◽  
pp. 181-196
Author(s):  
J.T. Sawyer ◽  
R.A. Akeson
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Lens Culinaris ◽  
Qualitative Change ◽  
Soybean Agglutinin ◽  
Plant Lectins ◽  
Lectin Receptor ◽  
Lens Culinaris Agglutinin ◽  
Cell Surface Glycoconjugates

To evaluate the relative mobilities of cell surface glycoconjugates during myogenesis we have studied the redistribution of fluorescein-conjugated plant lectins on L6 rat myogenic cells. Previous experiments had demonstrated that the receptors for the lectins soybean agglutinin (SBA), wheat germ agglutinin, concanavalin A and Lens culinaris agglutinin all were relatively uniformly distributed on both myoblasts and myotubes, and that SBA receptors were capable of rapid redistribution on myotubes but not myoblasts at 4 degrees C (Sawyer & Akeson, 1983). Here we show that when SBA-labelled myoblasts are incubated at 37 degrees C, or for extended times at 4 degrees C, the lectin aggregates as on myotubes. So it appears that SBA-binding components show a quantitative rather than qualitative change in their mobility during L6 differentiation. In addition, the redistribution of the three other lectins on myoblasts and myotubes was either less prominent (i.e. showing fewer apparent surface clusters) or occurred less rapidly than with SBA. None of these three lectins showed striking differences in mobility between myoblasts and myotubes. Thus, it appears that SBA binds to a subset of surface glycoconjugates that is relatively highly mobile, and that this mobility is specifically enhanced with differentiation.

Localization of glycopeptides and race-variable polypeptides in urediosporelings and urediosporeling walls of Puccinia graminis tritici; affinity to concanavalin A, soybean agglutinin, and Lotus lectin

1987 ◽  
Vol 65 (9) ◽  
pp. 1785-1791 ◽  
Author(s):  
W. K. Kim ◽  
N. K. Howes
Keyword(s):  
Concanavalin A ◽  
Brilliant Blue ◽  
Blue Staining ◽  
Puccinia Graminis ◽  
Two Dimensional ◽  
Soybean Agglutinin ◽  
Wheat Stem Rust ◽  
Coomassie Brilliant Blue ◽  
India Ink ◽  
Coomassie Brilliant

Detergent-soluble polypeptides from urediosporelings and purified germ-tube walls of urediosporelings of wheat stem rust, Puccinia graminis f.sp. tritici, races C1(17), C17(56), and C36(48) were separated by two-dimensional isoelectric focusing – polyacrylamide gel electrophoresis. More than 280 polypeptides were distinguished by Coomassie brilliant blue staining in each race, and there were 18 polypeptides that varied among the three races, 7 of which were coincident with urediosporeling wall polypeptides. Polypeptides transferred from two-dimensional gels onto nitrocellulose membrane were either stained with India ink or probed with concanavalin A – peroxidase for the location of concanavalin A binding glycoproteins. Of 97 concanavalin A binding glycoproteins in urediosporelings, 41 were coincident with polypeptides that stained with Indian ink and 3 were coincident with race-variable polypeptides. The walls of urediosporelings contained few polypeptides that stained with Coomassie brilliant blue or India ink, but most were concanavalin A binding. None of the polypeptides had affinity to soybean agglutinin or Lotus lectin, suggesting that galactose or fucose is not a terminal sugar moiety in these polypeptides. We conclude that race-variable polypeptides are located both within the cytoplasm and in the walls of urediosporelings, but most are not glycosylated.

scholarly journals Studies on the cell surface of zoospores and cysts of the fungus Phytophthora cinnamomi: nature of the surface saccharides as determined by quantitative lectin binding studies.

1985 ◽  
Vol 33 (5) ◽  
pp. 384-388 ◽  
Author(s):  
A Bacic ◽  
M L Williams ◽  
A E Clarke
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Phytophthora Cinnamomi ◽  
Lectin Binding ◽  
Soybean Agglutinin ◽  
Binding Studies ◽  
Con A

The nature of the surface saccharides of zoospores, "partially encysted zoospores" and cysts of the root-rotting fungus Phytophthora cinnamomi, has been examined by quantitative lectin binding studies. Zoospores bound concanavalin A (Con A), but did not bind any of a variety of other lectins tested. In contrast, both cysts and "partially encysted zoospores" bound soybean agglutinin (SBA) as well as Con A. This indicates that accessible alpha-D-glucosyl/alpha-D-mannosyl-containing glycoconjugates predominate at the zoospore surface, whereas both alpha-D-glucosyl/alpha-D-mannosyl and galactosyl and/or N-acetyl-D-galactosaminosyl residues are accessible at the surface of cysts and "partially encysted zoospores." Neither Ulex europeus lectin nor wheat germ agglutinin (WGA) bound to any of the three cell preparations, indicating the absence of accessible alpha-L-fucosyl and N-acetyl-D-glucosaminosyl residues.

Effects of some plant lectins on hydrogen peroxide release from macrophages induced with streptococcal preparation OK-432

1980 ◽  
Vol 28 (2) ◽  
pp. 336-343
Author(s):  
H Tomioka ◽  
H Saito
Keyword(s):  
Concanavalin A ◽  
Inhibitory Action ◽  
Wheat Germ ◽  
Specific Binding ◽  
Inhibitory Effect ◽  
Soybean Agglutinin ◽  
Peanut Agglutinin ◽  
Macrophage Phagocytosis ◽  
Receptor Sites ◽  
Wheat Germ Lectin

Concanavalin A and phytohemagglutinin were found to cause marked inhibition of H2O2 release from macrophages induced with killed streptococci (preparation OK-432). The inhibitory effect of these two lectins on the H2O2 release from macrophages was observed with spontaneous and wheat germ lectin-triggered H2O2 release. This suggests that the lectins act directly on the macrophage H2O2-releasing function, per se, but not on the wheat germ lectin-H2O2 release-enhancing process. Concanavalin A exhibited its inhibitory action on macrophage H2O2 release by specific binding to D-mannopyranoside receptor sites on the macrophage cell surface. Galactose-binding lectins, peanut agglutinin, and soybean agglutinin failed to inhibit, but, on the other hand, slightly enhanced macrophage H2O2 release. The effect of these five lectins on the phagocytosis of latex particles by macrophages was tested. Wheat germ lectin, concanavalin A, and phytohemagglutinin significantly depressed the macrophage phagocytosis, whereas peanut agglutinin and soybean agglutinin failed to show any inhibitory action.

scholarly journals Conjugation in Tetrahymena pyriformis. The effect of polylysine, concanavalin A, and bivalent metals on the conjugation process.

1976 ◽  
Vol 70 (2) ◽  
pp. 287-293 ◽  
Author(s):  
L Ofer ◽  
H Levkovitz ◽  
A Loyter
Keyword(s):  
Molecular Weight ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Tetrahymena Pyriformis ◽  
Degree Of Polymerization ◽  
Soybean Agglutinin ◽  
Polyaspartic Acid ◽  
Marked Inhibition ◽  
Bivalent Metals ◽  
Conjugation Process

The polycation polylysine, at different degrees of polymerization, was found to cause a marked inhibition of the conjugation process. Inhibition of conjugation by polylysine was highly dependent on the molecular weight of the polymer. When polylysine of a mol wt of 1,250 (degree of polymerization=6) was used, a concentration of 1.6 X 10(-5) M was required for a complete inhibition of conjugation, while only 2 X 10(-7) M of polylysine of a mol wt of 71,000 (degree of polymerization=340) was needed for the same effect. Polyaspartic acid prevented the inhibition of conjugation by polylysein. Chelators of bivalent metals such as O-phenanthroline (10(-3) M), EDTA (10(-3) M), and EGTA (5 X 10(-3) M) strongly inhibit the conjugation process in Tetrahymena pyriformis. The inhibition was partially prevented when bivalent metals such as Zn++, Fe++, and Ca++ were added together with the chelators. The lectin concanavalin A (25 mug/ml) completely prevented the conjugation process, while other lectins, such as phytohemagglutinin (500 mug/ml), soybean agglutinin (75 mug/ml) and wheat germ agglutinin (250 mug/ml) had no effect. Inhibition of conjugation by concanavalin A is completely reversible by 40 mM of alpha-methyl-D-mannoside.

Evidence for binding between host proteins and pathogen wall components in the wheat stem rust system from affinity protein blotting technique

1988 ◽  
Vol 66 (9) ◽  
pp. 1702-1706
Author(s):  
W. K. Kim ◽  
H. J. Reisener
Keyword(s):  
Concanavalin A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Soybean Agglutinin ◽  
Nitrocellulose Membrane ◽  
Host Proteins ◽  
Wheat Stem Rust ◽  
Wheat Leaf ◽  
Blotting Technique ◽  
Coomassie Brilliant ◽  
Wall Components

Polypeptides extracted from the urediosporeling walls of Puccinia graminis tritici were separated by two-dimensional isoelectric focusing – polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue or silver or electrophoretically transferred onto nitrocellulose membrane and probed for glycosylation using concanavalin A – horseradish peroxidase, soybean agglutinin-biotin – avidin peroxidase labeled, and Lotus lectin-biotin – avidin peroxidase labeled. More than 40 proteins were distributed in the gel by silver staining. Forty concanavalin A binding glycopeptides were identified in the blot, but none of them had affinity to soybean agglutinin or Lotus lectin. When fungal polypeptides were electrophoretically transferred through a nitrocellulose membrane that was pretreated with wheat leaf proteins, several fungal glycoproteins bound to the plant protein, suggesting that these pathogen wall components bound selectively to host proteins.

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