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PubMed1985

Effects of suramin on the immune responses to sheep red blood cells in mice. II. In vitro studies.

The effect of Suramin on the secondary in vitro response to sheep erythrocytes (SRBC) was studied. Spleen cells from mice which were treated with Suramin immediately prior to sensitization with SRBC failed to respond to an in vitro SRBC challenge. This Suramin-induced immunosuppression is not related to a defect in macrophage or B-cell function(s). Suramin does not interfere with the induction by SRBC of radioresistant and radiosensitive helper-T-cell subpopulations. Cell separation studies, using wheat germ agglutinin, showed radiosensitive helper-T-cell function in the nonagglutinated fraction while the radioresistant helper activities are carried out by the agglutinated subpopulation. Evidence is presented that Suramin administration results in a suppressive T-cell activity which can be demonstrated in the subpopulation agglutinated by wheat germ agglutinin. The role of such suppressive T cells in the inhibitory effect exerted by Suramin on the cell-mediated delayed-type hypersensitivity response to SRBC is discussed.

Animals↗
PubMed1977

Effect of physical properties of milk fat globules on Brucella ring test sensitivity.

Variations in Brucella milk ring test reactions have been attributed to size and disparity in size of fat globules, fat content of milk, inhibitory factors, and cream-rising capacity. Physical properties of milk fat globules were studied in individual milk samples that had diverse sensitivities for detection of Brucella agglutinins. Size or disparity of globule size could not be correlated with the milk ring test sensitivity. Inhibitory and enhancing creaming factors could be transferred from the cream to the skim milk and reacted with other cream to show changes in sensitivity. The proportion of clustered milk fat globules was related directly to the quantity of agglutinins detected by the test. Sensitivity of the test was attributed to a fat globule agglutinin that caused clustering and to an inhibitory factor.

Agglutination Tests↗
PubMed1979

Mannose-contaminating agglutinin for Actinomyces viscosus and Actinomyces naeslundii.

Rapid agglutination of Actinomyces viscosus and Actinomyces naeslundii cells by D-mannose solutions was observed during studies of their attachment to mammalian cells in vitro. The specificity of the agglutination reaction was studied by slide agglutination tests and by measuring the rate of decrease in optical density of bacterial phosphate buffer suspensions caused by the setting of bacterial aggregates. Actinomyces cells were agglutinated by protein-containing mannose solutions of several chemical suppliers. Solutions of sugars other than D-mannose and solutions of mannitol and mannan all failed to agglutinate A. viscsus and A. naeslundii. "Mannose-enhanced" agglutination was impaired by boiling or autoclaving the mannose but was not affected by heating the bacteria, the presence of chloramphenicol, running the assay in the cold, or incorporating any of several commercially purchased sugars in the reaction mixture. During these hapten inhibition experiments, only 6-deoxy-L-talcose-containing extracts of an A. viscosus strain retarded the rate of mannose-enhanced agglutination. Protein-containing fractions of D-mannose mother liquors also agglutinated cells of A. viscosus and A. naeslundii. Other species of oral gram-positive rods were not agglutinated by mannose solutions. Together the data indicate that plant seed-derived D-mannose contains a protein-associated agglutinin for A. viscosus and A. naeslundii which may function via a "lectin-like" selective affinity for the unique cell wall sugar 6-deoxy-L-talose.

Actinomyces↗
PubMed1975

Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers.

Wheat germ agglutinin was found to agglutinate cells of Escherichia coli PAT 84, Micrococcus luteus, Staphylococcus aureus H, and of S. aureus 52A5, but not cells of S. aureus 52A2. Interaction of wheat germ agglutinin with a soluble linear peptidoglycan secreted by Micrococcus luteus and with the teichoic acid of S. aureus H was demonstrated by agar gel diffusion, quantitative precipitation and inhibition of hemagglutination of trypsinized rabbit erythrocytes. No interaction could be demonstrated with the teichoic acid from a phage-resistant mutant (S. aureus 52A2) which lacks A-acetyl-D-glucosamine residues. All interactions were specifically inhibited by low concentrations of chitotriose (GlcNAcbeta1 leads to 4GlcNAcbeta1 leads to 4GlcNAc) and the bacterial cell wall tetrasaccharide, GlcNAcbeta1 leads to 4MurNAcbeta1 leads to 4GlcNAcbeta1 leads to 4MurNAc. Hemagglutination-inhibition experiments showed that the linear peptidoglycan and the teichoic acid of S. aureus H were several thousand times more potent inhibitors of wheat germ agglutinin than was N-acetyl-D-glucosamine. Comparison of the efficiency of different saccharides in inhibition of hemagglutination and precipitation of polymers by wheat germ agglutinin, strongly suggests that secondary, non-specific interactions contribute to the binding of the lectin to the polymers.

Agglutination Tests↗
PubMed1979

Age-related cell surface changes in human diploid fibroblasts revealed by lectin-mediated red blood cell adsorption assay: a lectin survey.

Two types of age-related cell surface changes could be demonstrated in human diploid fibroblasts with the two methods of the lectin-mediated red blood cell (RBC) adsorption assay: the fibroblast coating method (in which RBCs are adsorbed to lectin-coated fibroblasts) and the RBC coating method (in which lectin-coated RBCs are adsorbed to fibroblasts). With the fibroblast coating method, concanavalin A and agglutinin L from Phaseolus vulgaris gave a change in RBC adsorption which did not occur throughout the phase II period, but increased with the advance of the phase III period (type I). With the RBC coating method, these lectins gave another type of change in RBC adsorption which increased continuously from early phases of cell passage up through cell senescence (type II). Ricinus communis agglutinin 120 also gave the type I change in RBC adsorption with the fibroblast coating method. On the other hand, even with the fibroblast coating method, Phaseolus vulgaris agglutinin E and wheat-germ agglutinin gave the type II change in RBC adsorption. Soy bean agglutinin and Bauhinia purpurea agglutinin gave only a restricted amount of RBC adsorption. Lens culinaris agglutin, pokeweed mitogen, Dolichos biflorus agglutinin, Lotus tetragonolobus agglutinin, Limulus polyhemus agglutinin and divalent succinylated concanavalin A did not give any RBC adsorption throughout the life span of human diploid fibroblasts.

Cell Membrane↗
PubMed1995

Differences of phenotype and gene frequency by C system in canine species.

The canine C blood group was determined by an agglutination reaction with a plant agglutinin extracted from the seeds of Clerodendron trichotomum (CTL). A positive agglutination reaction was classified as type C and a negative reaction as type c. In this study, the C phenotype and the gene frequency of C were examined in 377 dogs (224 purebred dogs of 29 breeds and 153 mongrel dogs) that were bred in Utsunomiya-city, Tochigi Prefecture. Phenotype C was less frequent than phenotype c in every purebred dog. A variation in C gene frequency was observed among the purebred dogs. The highest frequency of C allele was in the Yorkshire Terrier (0.202), followed by Beagle, Shiba (0.091), Maltese (0.085), Shi Tzu (0.051) and Shetland Sheepdog (0.036). The C blood group system as a genetic marker may provide useful information for bleed identification, genetic studies between breeds, and pedigree certification.

Animals↗
PubMed1997

A new high molecular weight agglutinin from garlic (Allium sativum).

Erythrocyte agglutination by lectins from Allium sativum was inhibited only by mannose of the sugars tested. However, asialofetuin was more effective inhibitor of agglutination as compared to mannose. This led to the use of an asialofetuin-silica affinity column to isolate agglutinins of 110 and 25 kDa (ASA110 and ASA25). While ASA25 is a dimeric protein comprising of subunits of 12.5 and 13.0 kDa, ASA110 is a glycoprotein of two identical subunits of 47 kDa. ASA110 revealed to have a high content of aspartic acid, glycine, leucine and serine but low content of cysteine and methionine. It contains 14 residues of neutral sugars in addition to 43 residues of hexosamines per mole of lectin and requires metal ions for its functional conformation. Serological cross-reactions with other species showed some common epitopes of ASA110 and ASA25 present in A. porrum, A. ascalonicum, Narcissus alba, PHA and Con A but not in A. cepa. ASA110 with CHO cells indicated it to be weakly cytotoxic with LD50 of 160 microg/ml.

Amino Acids↗
PubMed1987

Identification of glycoprotein components of alpha-agglutinin, a cell adhesion protein from Saccharomyces cerevisiae.

Several glycoproteins which inhibit the agglutinability of Saccharomyces cerevisiae mating type a cells were partially purified from extracts of mating type alpha cells. These proteins, called alpha-agglutinin, were labeled with 125I-Bolton-Hunter reagent. The labeled alpha-agglutinin showed specific binding to a cells. Such specific binding approached saturation with respect to agglutinin or cells and was inhibited in the presence of excess unlabeled alpha-agglutinin. Nonspecific binding was similar in a and alpha cells, was neither saturable nor competable, and was three- to fourfold less than the specific binding to a cells at maximum tested agglutinin concentrations. The major a-specific binding species had a low electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels and had an apparent molecular weight of 155,000 by rate zonal centrifugation. Endo-N-acetylglucosaminidase H digestion of the purified glycoprotein complex converted the low-mobility material to four major and several minor bands which were resolved by polyacrylamide gel electrophoresis. All but two minor peptides bound specifically to a cells. Analyses of agglutinin from mnn mutants confirmed the deglycosylation results in suggesting that the N-linked carbohydrate portion of alpha-agglutinin was not necessary for activity.

Agglutination↗