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PubMed1982

Sexual agglutination factors from the yeast Pichia amethionina.

Pichia amethionina is a heterothallic yeast isolated from necrotic cactus tissue. Haploid cells of opposite mating type, designated alpha and alpha, agglutinate strongly when mixed. The agglutination factors of the two cell types have been solubilized from the cell walls by beta-glucanase digestion and then partially purified by affinity adsorption to the opposite cell type and by gel filtration. From alpha-cells was obtained a large, heat-stable glycoprotein with the ability to agglutinate alpha-cells. This alpha-agglutinin was inactivated by mercaptoethanol, probably because the recognition sites are linked to the glycoprotein core by disulfide bonds. Digestion of alpha-cells with beta-glucanase released a large heat-labile glycoprotein that did not agglutinate alpha-cells but did inhibit agglutination of alpha-cells by alpha-agglutinin. Subtilisin digestion of this alpha-factor released a carbohydrate-free protein of 27,000 daltons that retained the biological activity of the factor. These agglutination factors are sex- and species-specific and are not found on the surface of heterozygous diploid cells.

Agglutinins↗
PubMed1984

[Effect of levamisole on the formation of agglutinins against salmonellosis in weaned lambs].

In order to follow up the effect of levamizol on the titer of agglutinins a killed vaccine of Salmonella abortus ovis; S. enteritidis, and S. typhimurium strains was used under protection of antidenaturating agents (80 per cent sac charose) and levamizol ICI at the rate of 10 mg per kg body mass. Experiments were carried out with a total of 20 rabbits and 36 weaned lambs, divided into groups and injected with vaccine, vaccine and levamizol simultaneously, vaccine with levamizol following on the 3rd day, and vaccine and levamizol following on the 7th day, respectively. Results obtained by means of slow agglutination and hemagglutination showed that agglutinins had highest titers in the groups that received vaccine and levamizol simultaneously. The changes established with histologic investigations of the rabbits confirmed the importance of the simultaneous application of vaccine and levamizol for the immunologic 'reconstruction' of the body. Immunoelectrophoretic investigations concerning the globulins of the various groups did not point to essential differences having anything to do with the use of levamizol.

Agglutinins↗
PubMed1989

Pseudothrombocytopenia induced by a monoclonal IgM kappa platelet agglutinin.

Pseudothrombocytopenia is an in vitro phenomenon usually associated with anticoagulant (EDTA)-dependent IgG platelet agglutinins. A low Coulter platelet count was investigated in a 63-year-old woman with multiple sclerosis and a monoclonal IgM kappa gammopathy. An unusual type of EDTA- and temperature-independent IgM platelet agglutinin was identified by in vitro agglutination of donor platelets and was removed by immunoabsorption.

Agglutinins↗
PubMed1998

Axenic cultivation and partial characterization of Leishmania braziliensis amastigote-like stages.

Leishmania braziliensis strain M2903 was adapted for growth and serially maintained as amastigotes at 34 degrees C in modified UM-54 medium, with growth curves exhibiting typical log and stationary phases. In late passages, amastigote growth took place in the absence of supplementary haemin and was unaffected when the initial medium pH was adjusted between 5.4 and 6.3. In contrast to promastigotes, which were elongated and exhibited very long free flagella endowed with the paraflagellar rod (PFR), axenic amastigotes were rounded to ovoid and displayed a short flagellum restricted to the pocket area. The absence of PFR in axenic amastigotes was confirmed in Western blots and confocal immunofluorescence microscopy, by lack of reactivity with mAb 1B10. The antibody, which specifically labelled the paraflagellar structure, recognized a 70/72 kDa doublet in Trypanosoma cruzi epimastigotes and two 70/74 kDa related proteins in L. braziliensis promastigotes. Surface 125I-labelling experiments identified promastigote-specific components (> 100, 74, 45/47 and 28 kDa) and at least 1, a 76 kDa polypeptide was specific for the amastigote stage. While axenic amastigotes were agglutinated by both peanut (PNA) and Lens culinaris (LCA) agglutinins, respectively at 50 and 12.5 micrograms/ml, promastigotes were not agglutinated by PNA and agglutinated in the presence of LCA at concentrations of 100 micrograms/ml and higher. Axenic amastigotes infected rat bone marrow-derived macrophages and were avidly taken up by J774 cells, from which numerous organisms, able to proliferate at 34 degrees C in UM-54 medium, could be recovered 48 h later.

Adaptation, Biological↗
PubMedDate not supplied

Amphotericin B-induced carbohydrate changes on the Trypanosoma cruzi surface membrane.

Changes in the cell surface carbohydrates of Trypanosoma cruzi epimastigotes induced by Amphotericin B (AmB) were assessed by chemical methods and by agglutination assay employing a panel of highly purified lectins of various sugar specificities. Escherichia coli K12 with mannose-sensitive fimbriae was also used as an agglutination probe. Amphotericin B caused a decrease in the total carbohydrate content of all glycoconjugate fractions isolated. Exposure to AmB strongly affected the mannose/galactose ratio (1:5) in the CHCl3/methanol/H2O soluble fraction. These sugars in 1.4:1 ratio were the major hexose components of control cells. The decrease in the mannose content (48 to 15%) after AmB treatment agrees with the marked decrease in the T. cruzi cell surface receptors for fimbriated E. coli K12. Also, an increase in the galactose content (74%) as compared with control cells (34%) is in agreement with the peanut agglutinin and Euonymus europaeus lectins agglutination results. Differences in the cell surface carbohydrates induced by AmB could be associated with alterations in the membrane structure and organization.

Agglutination Tests↗
PubMed1998

Platelet cold agglutinins: a flow cytometric analysis.

Spontaneous EDTA-independent cold platelet agglutination is a rare phenomenon that produces pseudothrombocytopenia when blood samples are analyzed in automated cell counters. We report a case of platelet cold agglutinins and an analysis by flow cytometry. A 49 year old woman presented with abnormal vaginal bleed secondary to uterine fibroids. Platelet clumping was observed in blood samples taken in EDTA-, heparin- and citrate-containing tubes. In flow cytometric tests, patient serum agglutinated 16% of normal platelets at 22 degrees C, and 7% of platelets after incubation at 37 degrees C; in contrast, 3% and < 1% of platelets were agglutinated at 22 and 37 degrees C, respectively, after incubation with normal serum. Minimal agglutination (< 10%) was observed with patient serum at a titre of 1:5 or at temperatures > 30 degrees C. After incubation at 4 degrees C, IgM antibody and C3 were increased on the patient's platelets; no significant amount of IgM or C3 was detected on normal platelets. The specificity of the platelet cold agglutinin was determined by competitive inhibition by monoclonal anti-CD41(GPIIbIIIa). Before the addition of monoclonal antibody, patient's serum agglutinated 16% of normal platelets at 22 degrees C; after addition of anti-CD41 only 2% of the platelets were agglutinated. This blocking effect was not observed with anti-CD42. The patient's platelets functioned normally as determined by CD62 and CD63 expression in response to thrombin, normal platelet aggregation in response to collagen, ADP, and ristocetin, and a normal template bleeding time. In summary, platelet agglutination by a platelet cold agglutinin was quantitated by flow cytometry, the responsible antibody was characterized as a low titre IgM with minimal activity > 30 degrees C, and competitive binding studies supported the GPIIbIIIa complex as the binding site for the antibody. Since the antibody did not affect platelet function, we believe that these patients will not suffer complications from their platelet cold agglutinin, but it could pose a problem under circumstances such as cardiac surgery with hypothermia.

Adenosine Diphosphate↗
PubMed2003

Extraction of a monospecific Coombs-reagent from chicken eggs.

During the last ten years the extraction of specific antibodies (ab) from the yolk of eggs of immunised chickens is more and more accepted as an useful alternative to the immunisation of mammals. The subject of this work is the immunisation of chickens with human IgG and the extraction of specific anti human IgG ab from egg yolk in order to obtain monospecific Coombs reagent. 12 Leghorn hens (25 weeks old) were immunised with intact human IgG (INTACGLOBIN). The chickens were immunised with 100 microg IgG/animal once per week for a period of seven weeks. The highest titre was observed after the 5th immunisation, the following immunisations achieved no further titre increase. The IgY purification was performed according to the method of Akita and Nakai (1993). The resulting IgY preparation was tested for the presence of hetero-agglutinine by means of direct agglutination using human erythrocytes of all blood groups. Thereafter 58 blood donors were tested by means of direct or indirect Coombs-test using a reference reagent (DAKO) and a Coombs reagent isolated from chicken eggs (IgY antibodies). No differences have been found between the results obtained using both Coombs reagents. Presented results show that there is a possibility to produce Coombs-reagent in chickens. Advantages of this method are: 1) non invasive antibody sampling by egg collection instead of bleeding the animal (refinement of antibody production); 2) decreasing amount of animals necessary to produce high amounts of reagent; 3) IgY-preparation contains no hetero-agglutinine in contrast to serum ab from mammals, therefore additional step in reagent production e.g. the absorption of hetero-agglutinins is not necessary.

Animal Testing Alternatives↗
PubMed1972

Neoplastic transformation in vitro of a clone of adult liver epithelial cells into differentiated hepatoma-like cells under conditions of nutritional stress.

Differentiated epithelial cells in contact-inhibited monolayers derived from adult rat liver have been transformed in vitro into epithelioid neoplastic cells under conditions of nutritional stress. The transformed cells maintain their differentiated quality and manufacture serum proteins. They differ from control cultures in the following properties: They are aneuploid, can be agglutinated by wheat-germ agglutinin and concanavalin A, can grow in suspension, and are able to form colonies in semisoft agar. There is no intercellular communication at permeable junctions between the cells; this is demonstrable by electrical measurement or by injection of fluorescein. The cells show invasiveness in culture, and are not inhibited by contact with normal cells. The characteristics of the hepatocytes after transformation in vitro resemble those of epithelioid cells derived from a transplantable hepatoma.

Agglutination↗
PubMed1986

Characteristics of a galactose-binding hemagglutinin (lectin) from hemolymph of Spodoptera exigua larvae.

Hemolymph from Spodoptera exigua larvae agglutinates rabbit and human O erythrocytes. The agglutinin appears to be naturally occurring i.e., injury (by injection) or injection of larvae with fungal cells does not induce an increase in titer of hemolymph samples. Hemagglutinin activity is destroyed by heat or EDTA, and galactosidic carbohydrates inhibit agglutination of both red blood cell types. The agglutinin was purified by affinity chromatography using an Affi-Gel ovalbumin column. Binding to the column is calcium (cation) dependent. SDS gel electrophoresis shows that the agglutinin is a minor component of whole hemolymph represented by two bands with molecular weights of 30,500 and 31,000 daltons. Fluorescence microscopy using rhodamine-labeled agglutinin indicates that the agglutinin binds to fungal cell wall surfaces known to have galactose residues (e.g., Paecilomyces ochraceus), and that binding is specifically inhibited by galactose. There is no specific binding to fungal walls known to lack galactose residues (e.g., Paecilomyces ochraceus, Nomuraea rileyi). The agglutinin may be involved in the immune response of the insect e.g., by opsonization of microbial (fungal) surfaces which render the invading cells more susceptible to phagocytosis or agglutination.

Animals↗
PubMed1985

Legume agglutinins that bind to Rhizobium meliloti.

A protein found in seeds and roots of alfalfa (Medicago sativa) was implicated in the specificity of the infection process, based on its binding to the symbiont Rhizobium meliloti. We found an agglutinin with similar properties in seeds and roots of sweet clover (Melilotis alba). The sweet clover differed from alfalfa in nodulation by a mutant strain of R. meliloti, but the agglutinins were indistinguishable by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Rhizobium agglutination, and cross-reactivity to antibodies. Similar agglutinins binding R. meliloti were found in seeds of legumes from different cross-inoculation groups, including soybean (Glycine max), cowpea (Vigna unguiculata), pea (Pisum sativum L), and mung bean (Vigna mungo). The agglutinins from these legumes were recognized by antibodies raised against the agglutinins of alfalfa and sweet clover. Seeds of corn (Zea mays) and tomato (Lycopersicon esculentum) contained a protein similar to the legume agglutinin, but it did not react with the antibodies. We conclude that the alfalfa agglutinin is representative of a common legume protein and that there is no evidence for its role in specificity or nodule initiation.

Adsorption↗
PubMed1983

Purification and partial characterization of a Fucus Vesiculosus agglutinin.

Fucus vesiculosus agglutinin has been purified to homogeneity by conventional chromatographic procedures and characterized as a mucopolysaccharide with 90% carbohydrate content. Estimated molecular weight is about 2 X 10(6) daltons. It has no sub-unit structure and its isoelectric point is 3.2. It contains 1.23% S, 0.24% Ca and 0.06% P. Agglutinin mediated sheep red blood cell agglutination was inhibited only by glycoproteins with complex lateral oligosaccharide chains resembling some of the oligosaccharide chains found in the erythrocyte membrane glycoproteins. Metaperiodate treatment of the sheep red cells rendered them non-agglutinable. Sequential degradation of the oligosaccharide chains with glycosidases suggests that inner mannose residues are implicated in the receptor binding-sites for the agglutinin. Consequently we think that this agglutinin can be a lectin or a lectin-like molecule with complex saccharide specificity.

Carbohydrates↗
PubMed1983

The reactivities of Bauhinia purpurea and Lens culinaris lectins to mouse B Lymphocytes and their subsets.

The use of lectins for the separation of murine spleen lymphocyte subsets was examined. Bauhinia purpurea agglutinin was found to be effective for the enrichment of B cells by differential agglutination. When the differential agglutination technique using lectins was applied to the separation of B cell subsets, Lens culinaris agglutinin was found to be able to fractionate B cells into high responding and low responding subsets for dextran sulfate. A different expression of cell surface IgD was also observed between the cell populations showing different agglutinability with Lens culinaris agglutinin.

Animals↗
PubMed1986

Enhancement of cell-cell contact by a nonmitogenic lectin increases blastogenic response and IL-2 release by mitogen-stimulated mouse thymocytes.

We have examined the influence of peanut agglutinin (PNA), a lectin which agglutinates but does not stimulate mouse thymocytes, on the responsiveness of these cells to concanavalin A (Con A) or galactose oxidase stimulation. Binding low amounts of PNA on unseparated mouse thymocytes pretreated with neuraminidase highly enhances the mitogenic response and the level of interleukin 2 release in the culture medium upon Con A stimulation. We have shown that PNA present on the cell surface acts as a crosslinking agent which favors intercellular binding between accessory cells (macrophages) and thymocytes, leading through this enhanced cooperation by cell-cell contact to an enhanced blastogenic response.

Adjuvants, Immunologic↗
PubMed1982

Purification and partial characterization of an agglutinin from Phaseolus coccineus var. 'alubia'.

An agglutination from seeds of 'alubia', a Mexican strain of Phaseolus coccineus, has been purified by affinity chromatography using physically entrapped stroma. The protein appears to be homogeneous by electrophoresis, molecular sieve chromatography and ultracentrifugation. A molecular species of approx. Mr 112,000, with S values of 6.25, 4.52, 4.63 and 4.65 at pH 2.5, 4.5, 7.0 and 9.5, respectively, consisting of four similar subunits (28 kDa), and containing 20% W/W glucosamine, is found to be responsible for the hemagglutinating capacity of 'alubia' extracts. No sugar able to inhibit agglutination has been found. The possibility that hemagglutination by Ph. coccineus var. 'alubia' involves cell receptors other than simple carbohydrate structures must therefore be considered.

ABO Blood-Group System↗