scholarly journals Application of two new methods for cleavage of polysaccharides into specific oligosaccharide fragments. Structure of the capsular and extracellular polysaccharides of Rhizobium japonicum that bind soybean lectin.

1982 ◽  
Vol 257 (4) ◽  
pp. 1870-1875
Author(s):  
A.J. Mort ◽  
W.D. Bauer
Keyword(s):  
Rhizobium Japonicum ◽  
Extracellular Polysaccharides ◽  
New Methods ◽  
Soybean Lectin

Fractionation and characterization of two morphologically distinct types of cells in Rhizobium japonicum broth culture

1980 ◽  
Vol 26 (2) ◽  
pp. 107-114 ◽  
Author(s):  
S. Shantharam ◽  
J. A. Gow ◽  
A. K. Bal
Keyword(s):  
Star Formation ◽  
Binding Sites ◽  
Broth Culture ◽  
Rhizobium Japonicum ◽  
Nodule Formation ◽  
Bacterial Cells ◽  
Differential Centrifugation ◽  
Capsular Material ◽  
Soybean Lectin

Differential centrifugation of stationary phase broth culture of Rhizobium japonicum yielded two distinct morphological types of bacterial cells, rods, and small coccoid forms with capsulated and non-capsulated cells in each group. The rods usually had polar capsules which resulted in "star" formation. The coccoid bacteria were either free with thick capsular material surrounding the cells or held together in a common capsular sheath forming clusters and chains. 125I soybean lectin bound to the two types of cells. The binding sites were localized in the capsular material as revealed by colloidal gold- and ferritin-labelled lectin. Both fractions were capable of nodule formation in the soybean.

Interaction of lectins from soybean and peanut with rhizobia that nodulate soybean, peanut, or both plants

1980 ◽  
Vol 26 (12) ◽  
pp. 1489-1497 ◽  
Author(s):  
Steven G. Pueppke ◽  
Tom G. Freund ◽  
Brent C. Schulz ◽  
Harvey P. Friedman
Keyword(s):  
Lectin Binding ◽  
Rhizobium Japonicum ◽  
Lectin Receptors ◽  
Affinity Constants ◽  
Arachis Hypogaea L ◽  
Soybean Rhizobia ◽  
Glycine Max L ◽  
Soybean Lectin ◽  
Rhizobium Sp ◽  
Lectin Binding Sites

Four of 14 strains of Rhizobium japonicum from soybean nodulated peanut (Arachis hypogaea L. cultivar Jumbo Virginia), and 3 of 8 Rhizobium sp. strains from peanut nodulated soybean (Glycine max (L.) Merr. cultivar Harosoy 63). Cells of three peanut rhizobia bound fluorescent-and radioisotope-labeled soybean lectin. Two of these strains failed to nodulate soybean, and conversely, two peanut strains that nodulated soybean did not bind to soybean lectin. Both culture medium and age had pronounced effects of the number of peanut rhizobia cells that bound fluorescent-labeled soybean lectin. Harosoy 63 soybean root exudates stimulated the growth of peanut rhizobia, but had no consistent influence on the number of cells that bound soybean lectin. Although extracellular soybean lectin receptors were present in culture fluids from each of the peanut rhizobia whose cells bound the lectin, the titer of receptors was greatest for strain 3G4b5. The affinity constants for the adherence of soybean lectin to Rhizobium sp. 3G4b5 cells from cultures of various ages ranged from 4.2 × 106 to 4.9 × 106M−1 and the number of lectin binding sites per cell decreased as cells aged. Cells of the soybean and peanut rhizobia did not bind fluorescent- or radioisotope-labeled peanut lectin. The results indicate that there is no relation ship between the ability of peanut and soybean rhizobia to nodulate the reciprocal host plant and their ability to bind to the lectin of that plant.

Polarity in the exponential-phase Rhizobium japonicum cell

1977 ◽  
Vol 23 (9) ◽  
pp. 1274-1284 ◽  
Author(s):  
H. C. Tsien ◽  
E. L. Schmidt
Keyword(s):  
Cell Attachment ◽  
Lectin Binding ◽  
Polar Body ◽  
Ruthenium Red ◽  
Exponential Phase ◽  
Rhizobium Japonicum ◽  
Extracellular Polysaccharides ◽  
Thin Sections ◽  
Polar Bodies ◽  
Polymer Distribution

Highly distinctive aspects of the exponential-phase Rhizobium japonicum cell were disclosed by means of thin sections, freeze etching, fluorescent antibodies, and ruthenium red staining. Polarity was expressed in the form of reserve polymer distribution near one end of the cell and as cytoplasmic localization near the opposite end. In addition, exocellular polysaccharide (EPS) accumulated preferentially around the cytoplasmic end, and the feature described previously as an "immunofluorescent polar tip" was seen clearly as an extracellular polar body (EPB) on the tip of the cell at the reserve polymer end. Compartmentalization of cytoplasm and reserves were consistent features of nearly all exponential cells of the two strains studied; strain 31, however, formed little EPS and had a high incidence of a large, tightly bound EPB, while strain 138 formed EPS extensively and had a low incidence of EPB. Extracellular polysaccharides of strain 138 reacted with soybean lectin in gel diffusion tests, so that the EPS seen in electron micrographs is tentatively considered to include the lectin-binding material. Extracellular polar bodies were accumulations of granular and fibrillar material with properties consistent with the presence of polysaccharide and lipopolysaccharide. The role of EPB in cell to cell attachment was confirmed by electron microscopy.

Role of lectins in plant–microorganism interactions. IV. Ultrastructural localization of soybean lectin binding sites on Rhizobium japonicum

1978 ◽  
Vol 24 (7) ◽  
pp. 785-793 ◽  
Author(s):  
H. E. Calvert ◽  
M. Lalonde ◽  
T. V. Bhuvaneswari ◽  
W. D. Bauer
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Soybean Seed ◽  
Ultrastructural Localization ◽  
Rhizobium Japonicum ◽  
Outer Membranes ◽  
Capsular Material ◽  
Soybean Lectin ◽  
Lectin Binding Sites

The binding of purified, ferritin-labeled soybean seed lectin to the cell surfaces of Rhizobium japonicum 311b 138 has been examined by whole mount, thin section, and freeze-etch electron microscopy. The ferritin-labeled lectin binds in a biochemically specific manner to the capsular material of this bacterium. The lectin does not bind to the outer membranes of the cells or to flagella. Labeled lectin binds to sites throughout the capsular structure, although the density of labeling is somewhat greater on the outer surface of the capsule. Some cells appear to be partially encapsulated. Preservation of the capsular material proved difficult, and methods for retaining most of the capsular material were developed.

Differentiation of Rhizobium japonicum strain derivatives by antibiotic sensitivity patterns, lectin binding, and utilization of biochemicals

1980 ◽  
Vol 26 (5) ◽  
pp. 606-612 ◽  
Author(s):  
Michael C. Meyer ◽  
Steven G. Pueppke
Keyword(s):  
Parental Strain ◽  
Lectin Binding ◽  
Antibiotic Sensitivity ◽  
Colony Morphology ◽  
Rhizobium Japonicum ◽  
Large Colony ◽  
Utilization Patterns ◽  
Small Colony ◽  
Derivatives Of ◽  
Soybean Lectin

Several strains of Rhizobium japonicum have been reported to consist of mixtures of stable derivatives having distinct colony morphologies and physiological characteristics. We isolated derivatives from strains of R. japonicum and systematically compared them with previously isolated derivatives with respect to the utilization of biochemicals, antibiotic sensitivity, and soybean lectin binding. With the exception of a pair of derivatives from 3I1b 110, one of which utilized pyruvate and one of which did not, sibling derivatives had essentially identical biochemical utilization patterns. The sibling derivatives of parental strains 3I1b 110 and 3I1b 140 exhibited marked variation in their sensitivities to several antibiotics, including gentamicin, sulfamethoxazole, and tetracycline. Compared with the derivatives with small colony morphology, derivatives with large colony morphology were in general more sensitive to these antibiotics. With one exception, the binding of soybean lectin to the derivatives was quantitatively the same as that to the parental strain. The anomaly was 110-Y which, in contrast to its parental strain and sibling derivatives, failed to bind detectable amounts of the lectin. 110-Y, as well as all the other derivatives and parental strains, nodulated Disoy soybean.

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