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PubMed1975

The serology of Bordetella bronchiseptica isolated from pigs compared with strains from other animal species.

The serology of freshly isolated strains of Bordetella bronchiseptica from pigs and some other animal species was studied by the agglutination and agglutinin absorption tests. Differentiation was made between heat stable O-antigens and heat labile K-antigens. All the strains examined contained a common O-antigen (1). In addition, three heat stable antigens were detected. The heat labile antigens of freshly isolated strains were found to be very different. The major antigens 2 and 3 were not found in combination. A common weak K-antigen (1) was found in all strains. The pig strains were found to be serologically identical (0, 1, 2; K 1, 2). The same serotype was isolated from a rabbit. Another rabbit strain was found to be similar to a strain isolated from an SPF-rat (O, 1, 3; K 1, 3, 4). The antigenic pattern found in two cat strains was O 1, 3; K 1, 3. Typing of freshly isolated strains from pigs with monospecific factor sera confirmed that all the strains so far examined were serologically identical. This uniform serology hampers epidemiological studies of porcine bordetellosis by antigenic analysis. The occurrence of serologically different serotypes of B. bronchiseptica is of significance in the diagnostic bacteriology since the final diagnosis must be confirmed by a serological test.

Agglutination Tests↗
PubMed1977

Autoagglutinin produced by organ fragment cultures of mouse spleen.

Mouse spleen fragment microcultures produced a heat-labile substance which agglutinated syngeneic erythrocytes. The substance reacted with an antigen present on some strains of mouse erythrocytes and on rat erythrocytes, but absent from other strains of mouse erythrocytes and from guinea pig, rabbit or sheep erythrocytes. Agglutination was inhibited by antisera to mouse immunoglobulins except for antisera specific to mouse IgM which enhanced agglutination. The agglutinin sedimented with 19 S Ig on ultracentrifugation and was destroyed by pretreatment with mercaptoethanol. Using a rosette assay increased numbers of cells, specifically binding syngeneic erythrocytes by means of a surface Ig receptor were demonstrated in spleen fragment microcultures. It is considered that the agglutinin is a noncomplement-activating IgM autoantibody and that the precursors of the cells producing the autoantibody are detected by the rosette assay.

Animals↗
PubMed1979

Cholesterol levels and plasma membrane fluidity in 3T3 and SV101-3T3 cells.

Polyene antibiotics such as filipin selectively inhibit wheat germ agglutinin-induced agglutination of transformed and malignant cells compared to normal cells (Hatten ME, Burger MM: Biochemistry 18: 739, 1979). Since filipin binds specifically to cholesterol, we measured cholesterol levels in 3T3 cells and SV101-3T3 cells. SV101-3T3 cells contained 50-100% more cholesterol per cell than 3T3 cells. Both cell types were starved for cholesterol by growth in lipid-depleted medium plus 25-hydroxycholesterol. The cholesterol level of SV101-3T3 cells decreased by 30-50%, while the level in 3T3 cells remained constant. Filipin-stained SV101-3T3 cells revealed bright patches of filipin under fluorescence microscopy. These patches were absent in 3T3 cells and in SV101-3T3 and 3T3 cells starved for cholesterol. We selectively labeled plasma membranes of these cells with a spin label analog of phosphatidylcholine. The spin label indicated differences in plasma membrane fluidity that may be related to the different cholesterol levels in 3T3 and SV101-3T3 cells.

Animals↗
PubMed1984

Schistosoma mansoni: agglutination of sporocysts, and formation of gels on miracidia transforming in plasma of Biomphalaria glabrata.

The resistance or susceptibility of Biomphalaria glabrata strains to strains of Schistosoma mansoni, the human blood fluke, are evidenced by the responses of snail hemocytes to sporocysts of the schistosome, both in vivo and in vitro. It is now reported that living sporocysts of the PR1 strain of S. mansoni agglutinate in the plasma of all tested strains of B. glabrata, in contrast to fixed sporocysts which agglutinate only in plasma from resistant snail strains. The agglutinating activity in resistant plasmas is not divalent cation dependent, and was not inhibited by the 26 carbohydrates and four amino acids tested. In addition, the observation that gelatinous deposits develop on transforming miracidia-sporocysts in B. glabrata plasmas is also reported. Both the agglutination and gel-formation phenomena may facilitate recognition of, and attacks on, sporocysts, thereby contributing to susceptibility and resistance in this host-parasite system.

Agglutination↗
PubMed1984

Analysis and in vivo assay of B. abortus agglutinating and non-agglutinating antibodies.

Studies were made of physicochemical and immunochemical characteristics of Brucella abortus agglutinating and non-agglutinating antibodies in the sera of cattle repeatedly injected with living B. abortus (Strain 1119). Both agglutinating and non-agglutinating antibody were shown to be IgG1, and by immunodiffusion against rabbit anti-cattle gamma-globulin, agglutinating antibody gave a precipitation line of identity with that given by non-agglutinating antibody. Whilst agglutinating antibody increased clearance of antigen from the blood of passively protected mice, non-agglutinating antibody did not enhance clearance. Determination of the spleen infection index in mice pre-treated with agglutinating and non-agglutinating antibody showed that in animals passively immunized with non-agglutinating antibody the number of living (infecting) bacteria was approximately 4 times higher than in the case of agglutinating antibody. The possible potentiation of chronic B. abortus infection by non-agglutinating antibody is discussed.

Agglutination↗
PubMedDate not supplied

Adjuvant properties of polysaccharides: effect of iota-carrageenan, pectic acid, pectin, dextran and dextran sulphate on the humoral immune response in the rat.

Iota-carrageenan can both enhance agglutinating antibody responses and trigger reaginic antibody production against a protein associated antigen in rats. The present study investigates the strain specificity of this phenomenon and compares the adjuvanticity of high and low molecular weight iota-carrageenan with a series of structurally distinct polysaccharides (pectin, pectic acid, dextran and dextran sulphate). Using ovalbumin as the test antigen, high molecular weight iota-carrageenan induced a potent ovalbumin specific reaginic antibody response in PVG and Hooded Lister strain rats, an intermediate response in Sprague Dawley rats and a weak response in DA, AO and F344 strain rats. Further studies in PVG rats revealed that the nature and magnitude of the antibody response induced was influenced by the type of polysaccharide carrier used. Thus, whereas, high molecular weight carrageenan enhanced the agglutinating antibody (agglutinin) response and simultaneously elicited de novo reaginic antibody production to co-administered ovalbumin, low molecular weight carrageenan facilitated reaginic antibody production but had no effect on the agglutinin response. Pectin and dextran had no effect on the agglutinin response and failed to elicit reaginic antibody production. Conversely, pectic acid and dextran sulphate enhanced the agglutinin response and elicited a transient reaginic anti-ovalbumin response.

Adjuvants, Immunologic↗
PubMed1984

Isolation and characterization of Vicia faba lectin affinity purified on chitin column.

A lectin from early long pod var. of Vicia faba seed has been purified to homogeneity on chitin. The purified lectin is shown to be homogeneous in nature by Bio Gel P - 150 gel filtration, fast protein liquid chromatography and polyacrylamide gel electrophoresis. The lectin is a glycoprotein with molecular weight of 51,000. The lectin molecule is possibly composed of two types of subunits devoid of any covalent linking through sulfhydryl groups, with molecular weights 9,000 and 15,000 respectively in the ratio 2:2. The purified lectin shows a high affinity for N-acetyl-D-glucosamine (GlcNAc). Amino acid analyses show that cysteine and methionine are absent, and a high proportion of aspartic acid and glutamic acid are present in the protein molecule. The extinction coefficient of the purified lectin is 7.22. The lectin behaves as a 'cold agglutinin' displaying stronger agglutination than the naturally occurring ABO agglutinin in the cold.

Amino Acids↗
PubMed1977

Cell-mediated mitogenic response induced by leukoagglutinin and Lens culinaris lectin in mouse lymphocytes.

The proliferative response of mouse lymphocytes to syngeneic cellular stimulation upon membrane modification with lectins was studied. Brief pretreatment of stimulator cells (mitomycin-C-treated spleen cells) followed by mixed culture with syngeneic cortisone-resistant thymocytes resulted in a significant proliferative response in the thymocytes. This effect was not due to a soluble mediator and was similar to the mitogenic response after Con A-induced membrane modification reported previously. Because of its general characteristics, we refer to this response as cell-mediated mitogenic response (CMMR). Cell contact between stimulator and responder cells was necessary but not sufficient for the induction of the response. The lectins that generated CMMR were T-cell mitogens. CMMR was generated in all the syngeneic combinations tested and even in allogeneic combinations. No detectable cytotoxic activity towards syngeneic targets cells was produced after CMMR. Moreover, CMMR in allogeneic combinations led to the suppression of the generation of specific cytotoxic lymphocytes. Population analysis with antibodies against T or B cells, nylon wool fractionation of stimulator cells, and tests with peritoneal macrophages and with spleen cells from athymic mice revealed that CMMR depends predominantly on the interaction between responder T cells and stimulator Ig-positive lymphocytes.

Agglutination↗
PubMed1986

A New Lectin from Meadow Saffron (Colchicum automnale).

A lectin has been isolated from tubers of the meadow saffron (Colchicum autumnale). It is an octameric protein (M(r) 100,000) composed of 4A- and 4B-subunits of M(r) 15,000 and 10,000, respectively. It is a glycoprotein with 4.4% carbohydrate, the main sugars are (N-acetyl-) glucosamine, mannose, fucose, and xylose. Although the Colchicum autumnale agglutinin (CAA) agglutinates human red blood cells, it has a much higher activity with rabbit erythrocytes. With respect to its carbohydrate-binding specificity CAA behaves rather unusually as it is inhibited by lactose, galactose, N-acetylgalactosamine and related sugars when assayed with human red blood cells but not in assays with rabbit erythrocytes.

Journal Article↗