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PubMed1984

Rhizobium meliloti competitiveness and the alfalfa agglutinin.

We have isolated two types of isolates having identical colony morphologies from stock cultures of two different Rhizobium meliloti strains. One isolate was agglutinated at a high-dilution titer (HA, highly agglutinable) of the alfalfa agglutinin and was sensitive to phage F20, and the other was agglutinated at a lower agglutinin titer (LA) and was sensitive to phage 16B. All LA isolates from the original slant produced nodules on alfalfa earlier than did HA strains from the original slant. When these HA and LA strains were mixed and used as the inoculum in both vermiculite and field soil in the laboratory, LA strains were always the predominant strains recovered from the nodules. LA strains were obtained from HA cells by selection for resistance to phage F20, and HA strains were obtained from LA cells by selection for resistance to phage 16B. All of the strains with the HA phenotype that were derived from LA strains by phage selection had the nodulation properties of the HA strains from the original slant. Two classes of strains with the LA phenotype were obtained from HA cells by phage selection. One was identical to the original LA strains from the slant, and the other had the nodulation properties of the HA strains. Thus, we have shown that some cell surface properties change the nodulation abilities of R. meliloti strains and, furthermore, that specific phages can be used to enrich for more competitive rhizobia.

Agglutination↗
PubMed1976

The importance of agglutinin production in mice in the determination of the definitive serotype of Bordetella pertussis.

A schedule for the routine serotyping of strains of Bordetella pertussis based on agglutinin production in mice to the K-antigens has been worked out. Mice have been found as satisfactory as rabbits but far more economical for the production of the very small volumes of serum which are required. Agglutinin production, used in conjunction with direct agglutination, provides definitive information about serotype.

Age Factors↗
PubMed1976

The effect of chloroform on Brucella abortus agglutinins in whey.

Defatting milk for the Brucella abortus whey agglutination test with chloroform caused some reduction in the titre in i.u./ml. in 42 of 57 samples and this reduction exceeded 50% in seven. Though this procedure will probably rarely affect the final interpretation of the test defatting the milk by centrifugation is preferred.

Agglutination Tests↗
PubMed1988

Lipooligosaccharides (LOS) of Neisseria gonorrhoeae and Neisseria meningitidis have components that are immunochemically similar to precursors of human blood group antigens. Carbohydrate sequence specificity of the mouse monoclonal antibodies that recognize crossreacting antigens on LOS and human erythrocytes.

We have used mouse mAbs, 3F11 and 06B4, that are specific for highly conserved epitopes of Neisseria gonorrhoeae lipooligosaccharides (LOS) to identify immunochemically similar structures on human erythrocytes. mAb 3F11 agglutinated erythrocytes from all randomly selected adult humans, while mAb 06B4 agglutinated only 80% of the same specimens. The antibodies had an activity with erythrocytes similar to human cold agglutinins in that agglutination occurred at 4 degrees C and decreased with increasing incubation temperature. Human infant erythrocytes were agglutinated less well, but enzymatic treatment of either infant or adult cells resulted in an increase in expression of the 3F11- and 06B4-defined epitopes. Both antibodies bound to a series of neutral glycosphingolipids from human erythrocytes and neutrophils that have a type 2 (Gal beta 1----4GlcNAc) or N-acetyllactosamine structure. Neither antibody bound to glycosphingolipids from human meconium, which have a type 1 (Gal beta 1----3GlcNAc) structure. The antibodies were unable to bind to N-acetyl-lactosamine glycosphingolipids with a nonreducing terminal sialic acid or a Gala1----3Gal disaccharide. Antibody binding also was blocked by the presence of fucose linked to the penultimate glucosamine residue of N-acetyllactosamine glycosphingolipids. Although both antibodies bound to linear and branched-chain N-acetyllactosamine glycosphingolipids, 3F11 had a higher affinity for branched structures than did 06B4. The activity of 3F11 with human adult and infant treated and untreated erythrocytes with N-acetyllactosamine glycosphingolipids, and with LOS was very similar, if not identical, in specificity to 1B2, an mAb prepared from mice inoculated with a linear N-acetyllactosamine glycosphingolipid.

Adult↗
PubMed1967

Antigenic relationship of Brucella ovis and Brucella melitensis.

Immune sera were prepared in rabbits by the injection of living and acetone-killed cells of Brucella ovis and smooth and rough B. melitensis. The use of whole-cell antigens in agglutination and agglutinin-absorption tests revealed little relationship between B. ovis and smooth B. melitensis, although there was extensive cross-agglutination between B. ovis and rough B. melitensis. The use of water-soluble antigens prepared from ultrasonically treated cells of the three strains revealed extensive cross-reactions in indirect hemagglutination, agar gel precipitation, and immunoelectrophoresis tests, as well as in allergic skin tests in rabbits. The most definitive results were obtained with the immunoelectrophoresis technique. B. ovis antigen produced at least 11 lines with its homologous serum. All were removed by absorption of the serum with rough B. melitensis antigen. All but three were removed by absorption with smooth B. melitensis antigen. Smooth B. melitensis antigen produced 11 lines with its homologous serum, and all but 3 were removed by absorption with B. ovis antigen. Rough B. melitensis produced nine lines with its homologous serum, and eight were removed by B. ovis antigen. The extensive cross-reactions between soluble antigens of B. ovis and B. melitensis are added evidence that B. ovis belongs in the genus Brucella.

Animals↗
PubMed1980

Characterization of mouse helper and suppressor T cell subsets separated by lectins.

Concanavalin A (Con A)-activated cells were fractionated by separating cells that agglutinate with peanut agglutinin (PNA) which binds preferentially to the sugar sequence beta-D-Gal-(1 leads to 3)-D-GalNAc. PNA-agglutinable cells were found to exert a significant suppressor effect on the primary antibody response to sheep red blood cells, whereas PNA-nonagglutinable cells did not affect the antibody response. It was also found that PNA-agglutinable suppressor cells were sensitive to treatment with anti-Thy 1.2 and complement (C), anti-I-J antiserum and complement, and anti-Ly 2.2 antiserum and complement. These results suggest that the PNA-agglutinable suppressor cells, separated from Con A-activated cells, were T cells and that these suppressor T cells possess abundant beta-galactosyl residues exposed on the cell surface, not masked by sialyl residues. Furthermore, it was found that antigen-specific suppressor cells were also separable by use of the agglutinability with PNA. The PNA-agglutinable suppressor T cell activity was eliminated by treatment of the Con A-activated PNA-agglutinable cells with anti-asialo GM1 and complement, anti-Forssman antiserum and complement, and anti-globoside antiserum and complement, but not by treatment with anti-GM1 antiserum and complement. Conversely, the helper T cell activity that was induced by Lens culinalis agglutinin and separated by Limulus polyphemus agglutinin, was eliminated by treatment of the cells with anti-GM1 and complement, but not by the treatment with the other anti-glycolipid antisera and complement.

Animals↗
PubMedDate not supplied

Biological characteristics of the Calliphora vomitoria agglutinin.

The galactose specific agglutinin from Calliphora vomitoria was found to be expressed in the haemolymph of all the larval instars, but could not be detected at any other time during the life cycle. The haemagglutinating activity was insensitive to wounding of the tegument or injection of saline; however, a significant increase in haemagglutinating titre could be induced upon inoculation of the haemocoel with biotic or abiotic particulate material. The agglutinin also actively agglutinated several bacterial species and appeared capable of playing a role in particle--haemocyte interaction. The presence of the purified agglutinin significantly increased the attachment of fetuin-derivatized beads to haemocytes in vitro, and this activity could be specifically reduced by the addition of galactose, suggesting that the agglutinin may act as an opsonin.

Animals↗
PubMed1983

Transplantation for severe combined immunodeficiency with HLA-A,B,D,DR incompatible parental marrow cells fractionated by soybean agglutinin and sheep red blood cells.

Three patients with severe combined immunodeficiency (SCID) received transplants of HLA haplotype-mismatched parental bone marrow depleted of T lymphocytes by differential agglutination with soybean agglutinin (SBA) and subsequent E-rosette depletion. Two patients achieved durable engraftment with reconstitution of both humoral and cell-mediated immunity. Neither of these patients developed graft versus host disease (GVHD). The third patient achieved only a transient engraftment with concomitant development of mitogen-responsive lymphocytes of paternal origin. Our experience indicates that depletion of T lymphocytes by this technique can abrogate the potential of histoincompatible marrow grafts to induce lethal GVHD without limiting immunologic reconstitution. It also provides further evidence of nonimmune mechanisms of graft resistance that may necessitate preparative treatment of patients with SCID before transplantation with HLA-mismatched marrow cells.

Bone Marrow Transplantation↗
PubMed1978

Characterization of an agglutinin from human serum.

After exposure to serum, an agglutination of mitochondria from yeast, liver, heart and kidney was observed. The degree of agglutination was dependent on the ratio between the amount of serum proteins and mitochondrial protein. The serum protein which induced agglutination was bound irreversibly to the mitochondria, was heat stable and partly resistant to acidification. Maximal agglutination was observed at an ionic strength equal to 40 mM Tris, at pH 6.0-7.5. Preincubation of mitochondria with calcium ions at slightly acidic pH prevented the agglutination. Neuraminidase treatment of either serum or mitochondria had no effect upon the agglutination.

Agglutinins↗
PubMed1972

Concanavalin A agglutination of intestinal cells from the human fetus.

Concanavalin A markedly agglutinated isolated epithelial cells from the intestine of the human fetus but not from the intestine of the adult. Wheat germ agglutinin only moderately agglutinated cells from the intestine of an adult. These results extend the studies of concanavalin A agglutination of embryonic cells to human tissue, and they suggest that concanavalin A may be reacting with a common antigen on the fetal cell membrane.

Age Factors↗
PubMed1992

Cell surface saccharide differences in drug-susceptible and drug-resistant strains of Trichomonas vaginalis.

Surface carbohydrates of drug-resistant and drug-susceptible strains of Trichomonas vaginalis were analysed using lectins. The presence of D-GalNAc, D-Gal and mannose-like residues was detected in T. vaginalis. Marked differences in exposed surface carbohydrates were documented, e.g. wheat germ agglutinin (WGA) selectively agglutinated the drug-susceptible strain whereas drug-resistant parasites reacted preferentially with concanavalin A (Con A). In drug-resistant, but not in drug-susceptible strains, trypsinization induced the appearance of soybean agglutinin. Binding studies using fluorescein-labelled WGA and Con A essentially confirmed the agglutination experiments. Both the intense cell agglutination and the fluorescent WGA-binding displayed by a drug-susceptible strain, were completely nullified by neuraminidase treatment, suggesting the presence of an exposed sialic acid moiety on the T. vaginalis surface.

Agglutination Tests↗
PubMed1977

Bacteriophage-resistant mutants of Escherichia coli K12 with altered lipopolysaccharide. Studies with concanavalin A.

Three classes of mutants of Escherichia coli K12, isolated by selection for resistance to lipopolysaccharide-specific bacteriophages, were agglutinated by Concanavalin A which is presumed to interact with the lipopolysaccharide component of the outer membrane. Wheat germ and soy bean agglutinins did not agglutinate the parent or mutant strains. The adsorption of certain bacteriophages was also inhibited by Concanavalin A. The pattern of inhibition of adsorption of bacteriophages suggests that non-specific masking of receptors may occur, as well as specific masking of terminal glucose residues. Although bacteria were agglutinated by Concanavalin A, the permeability of the outer membrane seemed unaffected.

Adsorption↗
PubMed1995

Purification and basic characteristics of sialidase from Tritrichomonas mobilensis.

Sialidase, produced by Tritrichomonas mobilensis, a colonic parasite of squirrel monkeys, was purified by adsorption on human RBCs in ice-cold culture supernatant followed by release in PBS at 37 degrees C. The enzyme was purified by size-exclusion chromatography of RBC-eluted material giving a single peak with sialidase activity of molecular weight approx. 630 kDa, representing a quadrimer of the complex of three subunits. SDS-PAGE under reducing conditions showed three bands of 56, 61, and 66 kDa, identical with the molecular weight of the three subunits of T. mobilensis sialic acid-specific lectin (Babál et al., 1994). The enzyme treatment changed the agglutination of human RBCs by other lectins: created agglutinability with galactose-specific peanut agglutinin, but did not change agglutination with alpha 2,6 sialic acid linkage-specific Sambucus nigra lectin and linkage nonspecific TML. A 4-fold decrease of the agglutination with alpha 2,3 sialic acid linkage-specific Maackia amurensis lectin was observed. Histochemistry of kidney glomeruli after T. mobilensis sialidase treatment showed peanut agglutinin positivity on membranes of podocytes indicating selectivity for alpha 2,3 linked sialic acid. The sialidase did not hydrolyze colominic acid and was inhibited by 2,3-dehydro-2-deoxy-NeuAc. Divalent cations were not required for activity. The enzyme activity was optimal at pH 6.5-7 with RBCs as substrate and could be stored for 1 year at 4 degrees C.

Animals↗
PubMed1985

Differential binding of soybean agglutinin to human neuroblastoma cell lines: potential application to autologous bone marrow transplantation.

Normal human bone marrow cells were mixed with neuroblastoma cells from four different human cell lines, and the cell mixtures were separated by differential agglutination with soybean agglutinin (SBA). The unagglutinated cell fraction, previously shown to be highly enriched for the hematopoietic pluripotential stem cells and capable of reconstituting lethally irradiated adult patients with acute leukemia, was further fractionated by affinity chromatography on the lectin conjugated to Sepharose 6MB beads. Two independent assays, one using radiolabeling of the tumor cells and the other based on cloning of the neuroblastoma cells on agar, showed that the agglutination step alone removes 64-76% of the radiolabeled neuroblastoma cells and 85-98% of the clonogenic cells from the tumor/bone marrow cell mixture. Passage of the unagglutinated radiolabeled cells through SBA-Sepharose columns results in further purging of 28-53% of the neuroblastoma cells. Thus a combination of the two methods affords only one-log depletion for the neuroblastoma cells, compared to a three-log depletion achieved for a T-cell leukemia line CEM tested in parallel. It seems therefore that the agglutination technique, or the use of SBA-Sepharose columns, can be used only as a preliminary step for the purging of neuroblastoma cells from involved human bone marrow preparations. Staining with fluorescein isothiocyanate-conjugated SBA of nine different neuroblastoma cell lines, including the four tested in the fractionation studies, showed that more than 98% of the cells, of all the cell lines tested, specifically bind to the lectin, whereas no specific binding can be detected on the stem cell-enriched bone marrow cell fraction. However, the total number of receptors on the neuroblastoma cells is small compared to that of line CEM or normal granulocytes, which are strongly agglutinated by SBA. It seems therefore that the quantitative difference in the total number of SBA receptors is a crucial factor for purging by the agglutination technique or by affinity chromatography. Although these results show limitations to the use of both methods, this study establishes that all neuroblastoma cell lines tested express receptors for the lectin. Improved purging of neuroblastoma cells may possibly be achieved by targeting SBA-bound toxins or magnetic spheres to these receptors.

Agglutination↗
PubMed1971

Cyclic membrane changes in animal cells: transformed cells permanently display a surface architecture detected in normal cells only during mitosis.

A membrane site exposed only during mitosis in normal 3T3 cells, but exposed in all polyomavirus transformed 3T3 (Py3T3) cells, has been detected The site was identified by the specific binding of a wheat-germ agglutinin conjugated with fluorescein isothiocyanate. The receptor site has been studied previously. It binds wheat-germ agglutinin, causing the selective agglutination of Py3T3 cells, but not normal 3T3 cells. A short treatment with low concentrations of trypsin exposes cryptic sites in 3T3 cell membranes; this permits agglutination of these cells. The experiments reported here indicate that these sites normally are exposed during a brief period of the cell cycle for 3T3 cells. Specific hapten inhibitors of agglutination also inhibit the binding of the conjugated agglutinin and prevent fluorescence.

Animals↗
PubMed1984

Diagnostic value of interactions between members of the family Neisseriaceae and lectins.

The lectin slide agglutination test for Neisseria gonorrhoeae has been modified and improved. Results show that wheat germ agglutinin and soybean lectin agglutinate 100% (193 of 193 tested) of clinical isolates of N. gonorrhoeae. Lectin-reactive meningococci can be readily identified by the hydrolysis of gamma-glutamyl-beta-naphthylamide. Branhamella catarrhalis, Neisseria lactamica, Neisseria sicca, Neisseria subflava, Neisseria perflava, and meningococcal serogroups A, B, C, X, Y, and Z do not interfere with the positive identification of N. gonorrhoeae. The frequently encountered problem of autoagglutination of members of the family Neisseriaceae may be circumvented by a short treatment of cellular suspensions with DNase. Based on agglutination assays, the enzyme treatment did not result in a loss of wheat germ agglutinin receptors from the bacteria. The lectin agglutination test, coupled with the gamma-glutamyl aminopeptidase assay, is proposed as a rapid and accurate means of identifying clinical isolates of gonococci.

Agglutination Tests↗