Structure and cytochemistry of the walls of urediospores, germ tubes, and appressoria of Puccinia graminis tritici

1986 ◽  
Vol 64 (3) ◽  
pp. 476-485 ◽  
Author(s):  
D. E. Harder ◽  
J. Chong ◽  
R. Rohringer ◽  
W. K. Kim
Keyword(s):  
Concanavalin A ◽  
Outer Layer ◽  
Wheat Germ ◽  
Germ Tube ◽  
Lectin Binding ◽  
Periodic Acid ◽  
Puccinia Graminis ◽  
Spore Walls ◽  
Germ Tubes ◽  
Wheat Germ Lectin

Several cytochemical methods demonstrated that urediospore walls of Puccinia graminis f. sp. tritici were probably composed of five layers, including the pellicle as the outermost layer. Two previously undescribed layers were located around the inner periphery of the spore walls. Staining for periodate-sensitive glycosubstances occurred uniformly and heavily throughout the wall except that the pellicle was unstained, and the innermost layer (3c) was more lightly stained by periodic acid – thiocarbohydrazide – silver proteinate. There was little wheat germ lectin or concanavalin A binding to the urediospore wall except in the hilar region, where wheat germ lectin bound heavily, and in the germ pore region, where binding of concanavalin A occurred. The walls of about one-half of the urediospores that were examined contained silicon deposits. Germ tube walls were composed of two layers: a broad outer layer and a narrower inner layer. The inner layer stained more heavily for periodate-sensitive glycosubstances than did the outer layer. Germ tube walls bound wheat germ lectin, but not concanavalin A. Appressorial walls were also composed of two layers, but the inner layer was much broader than that of germ tube walls, and the outer layer stained more heavily for periodate-sensitive glycosubstances. There was strong wheat germ lectin binding to the appressorial walls, but concanavalin A binding was sparse. Both germ tubes and appressoria were coated with a mucilagenouslike substance.

Lectins as Cytochemical Probes of the Developing Wheat Grain. V. Demonstration of Separate Polysaccharides Containing N-Acetyl-D-Glucosamine and D-Galactose in Nuclear Epidermal Cell Walls

1984 ◽  
Vol 11 (3) ◽  
pp. 179 ◽  
Author(s):  
BA Baldo ◽  
D Barnett ◽  
JW Lee
Keyword(s):  
Epidermal Cell ◽  
Cell Walls ◽  
Wheat Germ ◽  
Periodic Acid ◽  
Fluorescein Isothiocyanate ◽  
Wheat Grain ◽  
Periodic Acid Schiff ◽  
Thin Sections ◽  
Lectin Staining ◽  
Wheat Germ Lectin

Fluorescein isothiocyanate-labelled lectin from wheat-gem, which binds N-acetyl-D-glucosamine, and Griffonia simplicifolia, Arachis hypogaea and Glycine max lectins, each of which binds D-galactose, react with nucellar epidermal cell walls in thin sections of plastic-embedded developing wheat grain. Reactivity of these cell walls with periodic acid-Schiff reagent, the absence of staining with protein stains and the failure of a number of proteases and the endoglycosidases D and H to prevent the binding suggested that the lectin-reactive wall components are neither proteins nor N-glycosidically linked glycoproteins. Morphological differences in lectin staining patterns and treatment of sections with chitinase and α-galactosidase, prior to the reaction with the lectins, indicated that two separate polysaccharides are probably involved in the binding. Chitinase removed the reactivity of the nucellar epidermal cell walls for wheat-germ lectin but the binding of D-galactose-specific lectins was unimpaired. Conversely, α-galactosidase did not affect the binding of wheat-germ lectin but reactivity with the galactose-specific lectins was abolished. From the available evidence we conclude that one polysaccharide in the nucellar epidermal cell wall reacts with wheat-germ lectin and contains N-acetyl-D-glucosamine in a chitin-like structure. The other polysaccharide reacts with D-galactose- specific lectins by virtue of terminal α-D-galactose residues. Hydrolysis and subsequent chromatographic analysis of nucellar epidermal cell walls peeled from immature grains revealed the presence of D-glucosamine, D-glucose, D-galactose, D-xylose, L-arabinose and a trace of D-mannose.

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 Immunogenetics of a macroglobulin allotype in cattle

1978 ◽  
Vol 31 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Domenico Iannelli ◽  
Piero Masina
Keyword(s):  
Isoelectric Point ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Serum Antigen ◽  
Cattle Serum ◽  
The One ◽  
Wheat Germ Lectin

SUMMARYThe paper describes a cattle serum antigen (McA2) located on a macroglobulin molecule which has its isoelectric point at pH 5 and is capable of interacting with the wheat germ lectin and concanavalin A.The specificity is inherited in a simple Mendelian manner and the gene controlling its synthesis is allelic to the one controlling the synthesis of the McAl antigen.

scholarly journals Regional distribution of N-acetyl-D-galactosamine residues in the glycocalyx of glomerular podocytes.

1983 ◽  
Vol 96 (5) ◽  
pp. 1189-1196 ◽  
Author(s):  
J Roth ◽  
D Brown ◽  
L Orci
Keyword(s):  
Basement Membrane ◽  
Cell Surface ◽  
Binding Sites ◽  
Wheat Germ ◽  
Lectin Binding ◽  
Glomerular Cell ◽  
Thin Sections ◽  
Foot Process ◽  
Wheat Germ Lectin ◽  
Lectin Binding Sites

Helix pomatia lectin (HPL) bound to colloidal gold was used as a specific cytochemical probe for the localization of terminal nonreducing N-acetyl-D-galactosamine residues in thin sections of rat kidney. In the glomerulus, lectin-binding sites were associated only with the podocyte foot process bases and were not found on the free cell surface of podocytes or on any other glomerular components. Gold-particle label was often arranged in the form of clusters which extended from the foot process base to the lamina rare externa and lamina densa of the basement membrane. In contrast, wheat germ lectin (WGL)-binding sites (beta-[1 leads to 4] linked N-acetyl-D-glucosamine residues and N-acetylneuraminic acid residues) were found in all regions of the podocyte plasma membrane and on the cell surface of all other glomerular cell types. In addition, WGL-binding sites were present in all three layers of the glomerular basement membrane (GBM) as well as in the mesangial matrix. A quantitative evaluation of the pattern of labeling for HPL-binding sites together with the sugar specificity of this lectin suggest that a component of the glycocalyx is being detected rather than a basement membrane component. This was confirmed by the absence of H. pomatia lectin-binding sites in preparations of isolated GBM which retained, however, wheat germ lectin-binding sites. These data show that the glycocalyx of the foot process base is a highly specialized cell surface domain with respect to its carbohydrate composition.

Hydrogen Peroxide-Releasing Function of Chemically Elicited and Immunologically Activated Macrophages: Differential Response to Wheat Germ Lectin and Concanavalin A

1980 ◽  
Vol 29 (2) ◽  
pp. 469-476
Author(s):  
Haruaki Tomioka ◽  
Hajime Saito
Keyword(s):  
Phorbol Myristate Acetate ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Peritoneal Macrophages ◽  
Prostaglandin E ◽  
Activated Macrophages ◽  
Myristate Acetate ◽  
Zymosan A ◽  
Streptococcal Preparation ◽  
Wheat Germ Lectin

Various types of mouse peritoneal macrophages were studied for H 2 O 2 release in the presence of wheat germ lectin or phorbol myristate acetate. Macrophages elicited 3 days before harvest by a single injection of thioglycolate, zymosan A, or a streptococcal preparation (OK-432) were highly responsive to wheat germ lectin, resulting in a marked increase in H 2 O 2 release. However, immunologically activated macrophages induced by double injections of live and heat-killed BCG at 15 and 3 days before harvest or by double injections of zymosan A or OK-432 at 20 and 3 days before harvest did not show any significant response to wheat germ lectin. On the other hand, all macrophages tested responded well to phorbol myristate acetate by augmentation of H 2 O 2 release. Concanavalin A inhibited wheat germ lectin- and phorbol myristate acetate-triggered H 2 O 2 release from all types of macrophages, but inhibition was much more marked in the case of wheat germ lectin-stimulated H 2 O 2 release. Succinylated concanavalin A (divalent concanavalin A) showed only slight suppressive action against macrophage H 2 O 2 release, and prostaglandin E 1 and dibutyryl cyclic adenosine 3′, 5′-monophosphate caused depression of H 2 O 2 release from OK-432-induced macrophages.

Lectins used to prepare serum free of glycoprotein hormones for use as a matrix in radioimmunoassay.

1981 ◽  
Vol 27 (1) ◽  
pp. 52-56 ◽  
Author(s):  
M C Stuart ◽  
S Ellis ◽  
L Gowlland ◽  
S Tuff
Keyword(s):  
Human Serum ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Specific Binding ◽  
Beta Subunit ◽  
Glycoprotein Hormones ◽  
Serum Free ◽  
Free Serum ◽  
Wheat Germ Lectin

Abstract Hormone-free serum is required for use as a matrix for standards in the radioimmunoassay of hormones. The glycoprotein hormones are difficult to remove from serum by conventional techniques. We exploited the specific binding of carbohydrates by lectins to extract glycoprotein hormones from human serum. Passing serum over Concanavalin A Sepharose efficiently removed lutropin and the beta subunit of choriogonadotropin. Wheat-Germ Lectin Sepharose completely removed these, and also follitropin and thyrotropin. The latter treatment is shown to provide a suitable matrix for standards in radioimmunoassays of the four hormones.

Lack of binding of serum glycoprotein hormone α subunit to Concanavalin A–Sepharose reflects increased branching of the oligosaccharide chains

1984 ◽  
Vol 103 (1) ◽  
pp. 111-116 ◽  
Author(s):  
A. J. Chapman ◽  
J. T. Gallagher ◽  
C. G. Beardwell ◽  
S. M. Shalet
Keyword(s):  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Pituitary Tumours ◽  
Con A ◽  
Glycoprotein Hormone ◽  
Α Subunit ◽  
Binding Forms

ABSTRACT The lectin-binding properties of serum α subunit were studied by lectin affinity chromatography. Normal individuals and most patients with pituitary tumours produced α subunit which bound specifically to Concanavalin A–Sepharose (Con A). Some patients with pituitary tumours produced both Con A-reactive α subunit and α subunit which did not bind to Con A. Concanavalin A–Sepharose-binding α subunit from all sources bound strongly to Ricinus communis agglutinin–Sepharose after treatment with neuraminidase. Serum α subunit from those patients with pituitary tumours, which did not bind to Con A, bound to wheat germ agglutinin–Sepharose, exhibiting both weakly binding and strongly binding forms. Serum α subunit from both patients and controls, which did bind to Con A, showed only weak affinity for wheat germ agglutinin–Sepharose. Neither the low affinity nor the high affinity of serum α subunit from any source for wheat germ agglutinin–Sepharose was affected by neuraminidase. These findings show that (a) the predominant pattern of glycosylation of serum α subunit from normal controls is a Con A-reactive, biantennate complex oligosaccharide and (b) that the structural alteration which results in serum α subunit which does not bind to Con A in some patients with pituitary tumours is not an absence of carbohydrate, rather the α subunit contains highly branched, either complex or hybrid oligosaccharides. J. Endocr. (1984) 103, 111–116

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