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At least 19 recordsLinked to original sources
PubMed1980

Role of lipopolysaccharide in wheat germ agglutinin-mediated agglutination of Neisseria meningitidis and Neisseria gonorrhoeae.

Wheat germ agglutinin, having specificity for N-acetyl glucosamine, agglutinated known nonencapsulated Neisseria meningtidis strains, but failed to agglutinate encapsulated strains of all serogroups tested Presence of a capsule, therefore, blocked wheat germ agglutinin agglutination of N. meningitidis strains. In contrast, Neisseria gonorrhoeae strains were strongly agglutinated, providing additional evidence for nonencapsulation of N. meningitidis strains. In contrast, Neisseria gonorrhoeae strains were strongly agglutinated, providing additional evidence for nonencapsulation of N. gonorrhoeae. Purified lipopolysaccharide from a single N. meningitidis and N. gonorrhoeae strains tested. Thus, in absence of capsular polysaccharide wheat germ agglutinin agglutinates Niesseria strains through interaction with lipoplysaccharide in the outer membrane. Of 34 nongroupable throat N. meningitidis isolates, 10 failed to agglutinate in wheat germ agglutinin, suggesing that at least some nongroupable. N. meningitidis strains may possess capsule-like materials.

Agglutination↗
PubMed1978

Similarities in the membrane fluidity of 3T3 and SV101-3T3 cells and its relation to concanavalin A- and wheat germ agglutinin-induced agglutination.

Intact, viable ultransformed 3T3 and transformed SV101-3T3 cells were labeled with fatty acid spin labels and with 2,2,6,6-tetramethylpiperidine-1-oxyl in order to measure the fluidity properties of membrane lipids. Both cell types were grown in regular calf serum and in a lipid-depleted serum supplemented with either oleate or elaidate. The temperature dependence of the spectra obtained revealed inflections that correlate with the temperature below which agglutination with concanavalin A is inhibited, and another inflection that correlates with the temperature below which agglutination with wheat germ agglutinin is inhibited, suggesting that (a) the lipid phase(s) in the vicinity of the receptor(s) for these two lectins differ, and (b) a fluid membrane in the vicinity of the lectin receptor(s) is necessary for agglutination with either concanavalin A or wheat germ agglutinin. Studies with a partially characterized plasma membrane fraction suggest that the plasma membrane fluidity parameters closely resemble those of the intact cell. 3T3 and SV101-3T3 cells show virtually identical fluidity profiles by all of the tests we have applied.

Agglutination↗
PubMed1975

A quantitative assay for concanavalin A- and Ricinus communis agglutinin-mediated agglutinations of rat ascites hepatoma cells. Relationship between concanavalin A binding and cell agglutination.

A simple quantitative assay method was developed for the agglutination of rat ascites hepatoma cells mediated by Concanavalin A or Ricinus communis agglutinin. This method was based on the principle that the turbidity of a cell suspension is proportional to the sum of the cross-sectional area of cells and aggregatesmas predicted by the theoretical consideration, the turbidity decreased when cells were aggregated and the decrease was a function of the average number of the cells in aggregates. The agglutinability of the cells, judged by this method, showed a maximum value at a certain concentration of the agglutinin. By further addition of the agglutinin, the agglutinability slightly decreased from the maximum. These phenomena were observed both for Concanavalin A and Ricinus communis agglutinin. The binding and the agglutination experiments using [3-H]concanavalin A revealed that the binding to approx;0% of the total receptors caused a maximal agglutination. This suggested that the receptors responsible for the agglutination constitute only a small part of the total receptors on the surface.

Agglutination Tests↗
PubMed1979

Relationship of Treponema pallidum to acidic mucopolysaccharides.

Attempts were made to relate Treponema pallidum to the acidic mucopolysaccharides that occur in vivo within host ground substance and in vitro on the surface of cultured testicular cells. Infected testicular tissue was fixed and processed for transmission electron microscopy in the presence of ruthenium red. The use of this inorganic dye demonstrated the large quantity of mucopolysaccharide within testicular tissue and the intimate association of treponemes with this material. Wheat germ agglutinin and soybean agglutinin agglutinated freshly harvested trypsinized testicular cells and trypsinized cultured cells derived from normal rabbit testes (NRT). When stained with toluidine blue, both cell preparations were metachromatic. Prior treatment of cultured NRT cells with hyaluronidase slightly decreased their sensitivity to agglutination by wheat germ agglutinin and soybean agglutinin. Lectin agglutination, metachromasia, and hyaluronidase susceptibility indicated that freshly harvested testicular cells and NRT cells have surface-associated acidic mucopolysaccharides that are probably hyaluronic acid and chondroitin sulfate. A rabbit erythrocyte "sandwich" technique was devised to show that hyaluronidase removed wheat germ agglutinin receptors from the cultured NRT cells. Prior incubation of NRT cells with hyaluronidase, followed by the addition of T. pallidum, resulted in a reduction in numbers of treponemes attached to the NRT cells. The attachment of T. pallidum appears to be mediated through the acidic mucopolysaccharides on the surface of NRT cells. The findings are discussed in terms of the importance of host ground substance mucopolysaccharide to the syphilitic infective process.

Animals↗
PubMed1979

Comparison of some Shigella flexneri (Escherichia coli) hybrids in cross agglutination and agglutinin absorption tests.

Antigenic structure of Lac+ hybrids selected from Escherichia coli x Shigella flexneri crosses was compared in the cross agglutination and absorption tests. Identity of the hybrids from the recipients of serotype 2a and variant Y was proved, as well as from serotypes 1b and 4b. The latter hybrids were coupled with Shigella flexneri strains 3a, 3b and 3c. The hybrids appeared almost identical with serotype 3c.

Absorption↗
PubMed1986

Ricinus communis agglutinin-mediated agglutination and fusion of glycolipid-containing phospholipid vesicles: effect of carbohydrate head group size, calcium ions, and spermine.

The glycolipids galactosylcerebroside (GalCer), lactosylceramide (LacCer), and trihexosylceramide (Gb3) were inserted into phospholipid vesicles, consisting of phosphatidylethanolamine and phosphatidic acid. The extent to which their carbohydrate head groups protruded beyond the vesicle surface and their interference with membrane approach were examined by determining vesicle susceptibility toward type I Ricinus communis agglutinin (RCA1) induced agglutination and Ca2+- and spermine-induced aggregation and fusion either in the presence or in the absence of the lectin. The initial agglutination rates increased in the order GalCer much less than LacCer less than Gb3, while a reversed order was obtained for Ca2+- and spermine-induced aggregation and fusion, indicating an enhanced steric interference on close approach of bilayers with increasing head group size. The lectin-mediated agglutination rates for LacCer- and Gb3-containing vesicles increased by an order of magnitude when Ca2+ was also included in the medium, at a concentration that did not induce aggregation per se. Charge neutralization could not account for this observation as the polyvalent cation spermine did not display this synergistic effect with RCA1. Addition of Ca2+ to preagglutinated vesicles substantially reduced the threshold cation concentration for fusion (micromolar vs. millimolar). Quantitatively, this concentration decreased with decreasing carbohydrate head group size, indicating that the head group protrusion determined the interbilayer distance within the vesicle aggregate. The distinct behavior of Ca2+ vs. spermine on RCA1-induced agglutination on the one hand and fusion on the other indicated that Ca2+ regulates the steric orientation of the carbohydrate head group, which appears to be related to its ability to dehydrate the bilayer. As a result, lectin agglutinability becomes enhanced while fusion will be interrupted as the interbilayer distance increases, the threshold head group size being three carbohydrate residues (Gb3). Finally, GalCer-containing vesicles were not agglutinated by RCA1 at ambient temperature, irrespective of the presence of Ca2+. Above 25 degrees C, RCA1 facilitated Ca2+-induced fusion of the vesicles, which was abolished by the haptenic sugar lactose. Since Gb3- and LacCer-containing vesicles displayed a similar behavior, a temperature-induced alteration in the supporting lipid matrix is suggested, which apparently affects lectin/glycolipid interaction.

Agglutination↗
PubMed1993

Agglutinins from aquatic insects--tumor cell agglutination activity.

Agglutinins were identified in whole body extracts of aquatic insects by means of murine tumor cell agglutination, using sarcoma 180 ascites, Ehrlich, and MM-46 cells. Screening revealed agglutinins in 5 of 10 of the larvae tested, and in 2 of 6 of the water-dwelling adult insects; Gerris paludum insularis and Gyrinus japonicus. Only the agglutinin from adult G. paludum also agglutinated human erythrocytes. An ascites tumor was converted into a solid form in vivo after administration of G. paludum agglutinin. The observation that these aquatic insect agglutinins preferentially agglutinate tumor cells has considerable implications in terms of anti-tumor effects such as inhibition of cell proliferation and metastasis.

Agglutination↗
PubMed1976

The chromaffin granule surface. Localization of carbohydrate on the cytoplasmic surface of an intracellular organelle.

Intact chromaffin granules from bovine adrenal medulla are shown to have complex carbohydrates on their external (cytoplasmic) surface. This is demonstrated by the facts (1) that granules can be agglutinated by wheat germ agglutinin, and (2) that significant amounts of sialic acid can be removed from the granule surface with neuraminidase. Glycoproteins located in the granule membrane, and not glycolipids, are the molecules that mediate wheat germ agglutinin agglutination. The possible involvement of granule surface carbohydrate in the process of exocytosis is discussed.

Adrenal Medulla↗
PubMed1980

Interaction of lectins with Neisseria gonorrhoeae.

Fifty-four strains of Neisseria gonorrhoeae were examined for their ability to be agglutinated by various lectins. Wheat germ agglutinin, ricin, soybean lectin, and peanut agglutinin agglutinated all strains tested. Dolichos biflorus, Sophora japonica, Maclura pomifera, Ulex Europaeus, Lens culinaris, Canavalia ensiformis, Phaseolus lunatus, and Bandeiraea simplicifolia BS I and BS II lectins either failed to agglutinate or agglutinated some strains but not others. Agglutination of gonococci by wheat germ agglutinin, ricin, and soybean lectin is sugar specific and most effectively inhibited by ligands known to interact with lectin combining sites. Lectin reactive groupings appear to be independent of antigenic determinants conferring Gc serogroup specificity. Interactions with wheat germ agglutinin and ricin suggest the occurrence of multiple beta-linked N-acetyl-D-glucosamine (D-GlcNAc) and beta-D-galactosyl (beta-D-Gal) units as common structural features of gonococcal cell envelope polysaccharide. Interactions with soybean agglutinin, peanut agglutinin, and Dolichos biflorus lectins suggest that alpha-N-acetyl-D-galactosamine (alpha-D-GalNAc) units and beta-D-Gal linked to GalNAc and (or) GlcNAc may also occur as structural features of the polysaccharide components of the cell envelope of some gonococci.

Agglutination↗
PubMedDate not supplied

Separation of normozoospermic human spermatozoa into subpopulations by selective agglutination with peanut agglutinin.

Incubation of human spermatozoa of normozoospermic origin with the galactose specific lectin peanut agglutinin (PNA) resulted in agglutination of the majority of sperm. This finding enabled separation of sperm into two subpopulations. The major one, accounting for 87.0 +/- 12.7 (SD)% consisted of agglutinating sperm (PNA+), while the minor subpopulation (PNA-) did not bind the lectin. The correlation between the percentages of PNA- sperm and acrosome-damaged sperm, as detected by light microscopy prior to separation, was analysed and an overlapping has been found. Light and electron microscopy examination revealed that the PNA- cells were either acrosomeless or possessed severely damaged acrosomes while the PNA+ sperm were mostly free of such pathologies. Following treatment of sperm with fluorescin-conjugated PNA the single cells lacked any labeling while the agglutinates exhibited fluorescence. However, the binding of the lectin to sperm was non-uniform and differences in fluorescence intensity at various parts of the head have been observed. The sialic acid content in PNA+ sperm was found to be significantly higher (7.5 +/- 2.2 micrograms/10(8) sperm) as compared to PNA- sperm (2.1 +/- 0.6 micrograms/10(8) sperm). It was suggested that sialic acid content could be a biochemical indicator of acrosomal integrity. Separation of sperm by selective PNA agglutination might be valuable for elimination of sperm affected by acrosomal pathologies from the ejaculate.

Galactose↗
PubMed1986

Partial characterisation of a soluble haemagglutinin from human diarrhoeal isolates of Aeromonas.

A soluble haemagglutinin has been identified in cell-free culture supernates of human diarrhoeal isolates of Aeromonas sobria, A. hydrophila and A. caviae. It was oligomeric; a major peak of haemagglutinating activity had an apparent mol. wt of 780,000 but there was haemagglutinating activity throughout the mol. wt range less than 40,000- greater than 10(6). Human group O, A and B, horse, rabbit, chicken and rat erythrocytes, but not those of sheep and cow, were agglutinated by the soluble haemagglutinin, in contrast to the cell-bound agglutinin. Agglutination was inhibited by fetuin, a complex glycoprotein, but not by simple sugars. The haemagglutinating activity was not affected by 0.5 M NaCl, dithiothreitol or the presence or absence of Ca++. It was unrelated to the haemolytic, enterotoxigenic and proteolytic activities present in cell-free extracts of A. sobria. All A. sobria, 73% of A. hydrophila and 68% of A. caviae strains tested produced this soluble haemagglutinin. A. caviae does not appear to be an enteric pathogen, therefore this soluble haemagglutinin alone is unlikely to be a virulence factor in Aeromonas spp.

Adult↗
PubMed1979

Interaction of wheat-germ agglutinin with streptococci and streptococcal cell wall polymers.

Wheat-germ agglutinin agglutinates all strains of group A and group C streptococci, a part of the strains tested of groups B and E and some strains of other streptococcal groups. It also agglutinates peptidoglycan of several streptococcal groups and precipitates some group-specific carbohydrates of streptococcal cell walls as well as some teichoic acid extracts. The basis for agglutination and precipitation of streptococci and streptococcal cell wall polymers appears to be the interaction of the combining sites of the agglutinin with N-acetyl-D-glucosamine residues present in the cell wall polymers, either in terminal or in internal positions respectively.

Acetylglucosamine↗
PubMed1979

Human cold agglutinins against "cryptic" erythrocyte antigens.

Two examples of human IgM cold agglutinins agglutinated human RBC only after enzyme treatment in vitro. Proteases were optimally effective, neuraminidase was also effective. The cold agglutinins did not coat native RBC but were directed against "cryptic" RBC determinants. The cold agglutinins belonged to the anti -I/-i complex indicating a "new" type of I/i determinants. They were strongly accessible to cold agglutinin interaction on native RBC of a patient with congenital dyserythropoietic anaemia. Enzyme treatment of RBC was shown to be not only suited for defining cold agglutinin specificities but also essential for detecting the "new" type of cold agglutinins, obviously causing autoimmune haemolytic anaemia in vivo.

Aged↗