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PubMed1980

Interactions of pseudomonas aeruginosa hemagglutinins with Euglena gracilis, Chlamydomonas reinhardi, and Tetrahymena pyriformis.

The galactosephilic and mannosephilic hemagglutinins of Pseudomonas aeruginosa adsorbed onto Euglena gracilis, Chlamydomonas reinhardi, and Tetrahymena pyriformis. Furthermore, peroxidase binding to the 3 protozoan species was shown to be mediated by these lectins. Binding of Pseudomonas lectins to E. gracilis and C. reinhardi caused their specific agglutination, whereas no agglutination was observed with T. pyriformis, even after treatment by papain or by NaF. Added to the culture medium, the Pseudomonas hemagglutins stimulated growth of E. gracilis and T. pyriformis due to their binding to these protozoa; this effect was partly inhibited by the specific sugar.

Adsorption↗
PubMed1978

Immunochemical studies on the specific agglutinogens of Staphylococcus aureus. I. Isolation and characterization of antigen h1.

The specific Staphylococcus aureus agglutinogen h1 has been purified and shown to be a protein with a molecular weight of about 95,000. Chemical analysis revealed all the common amino acids, except tyrosine and the sulphur-containing ones. The purified h1 antigen was strongly immunogenic in rabbits. The antiserum produced one precipitation line on double diffusion in agar against a suspension of bacteria. It also agglutinated bacteria of the h1-containing strains, as well as tanned sheep erythrocytes sensitized with h1, in high dilutions. Antibodies to other known staphylococcal antigens were not detected. The identity between h1 and Pillet's type 9 antigen was confirmed.

Agglutination↗
PubMed1974

Mammalian hepatic lectin.

A rabbit hepatic protein that specifically binds asialoglycoproteins is also a lectin that agglutinates untreated human and rabbit erythrocytes and neuraminidase-treated erythrocytes from rat, mouse, and guinea pig. Both binding of asialoglycoproteins and agglutination of erythrocytes appear to involve reaction on the same active sites of the hepatic protein.

Agglutination↗
PubMed1990

Surface array proteins of Campylobacter fetus block lectin-mediated binding to type A lipopolysaccharide.

Campylobacter fetus strains with type A lipopolysaccharide (LPS) and a surface array protein layer (S+) have been found to be pathogenic in humans and animals. Spontaneous laboratory mutants that lack surface array proteins (S-) are sensitive to the bactericidal activity of normal human serum. The ability of lectins to determine the presence of the S-layer and differentiate LPS type was assessed. We screened 14 lectins and found 3 (wheat germ agglutinin, Bandeiraea simplicifolia II, and Helix pomatia agglutinin) that agglutinated S- C. fetus strains with type A LPS but not S- strains with type B or type C LPS or S+ strains. However, the S+ type A strains were agglutinated after sequential water extraction, heat, or pronase treatment, all of which remove the S-layer, whereas there was no effect on the control strains. Specific carbohydrates for each lectin and purified LPS from a type A C. fetus strain specifically inhibited agglutination of an S- type A strain. In a direct enzyme-linked lectin assay, binding to the S- type A LPS strain was significantly greater than binding to the S+ strain (P = 0.01) or to a Campylobacter jejuni strain (P = 0.008). Consequently, these results indicate that the three lectins bind to the O side chains of C. fetus type A LPS but that the presence of the S-layer on intact cells blocks binding.

Agglutination Tests↗
PubMed1991

Monoclonal antibody characterization of a leukoagglutinin produced by Renibacterium salmoninarum.

Renibacterium salmoninarum causes a chronic disease of salmonid fish known as bacterial kidney disease. High concentrations of bacterially produced extracellular protein (ECP) are present in plasma, kidney, and spleen tissue of naturally and experimentally infected fish. ECP agglutinated salmonid leukocytes in vitro at concentrations which correspond to levels found in highly infected fish. Association of biological activity with the structure of the major protein constituent of ECP, p57, was accomplished by monoclonal antibody (MAb) analysis. Location of the antigenic binding sites recognized by the MAbs was determined by two-dimensional electrophoresis and Western immunoblotting of the proteolytic breakdown fragments of p57. Eight MAbs have been classified into three groups on the basis of their differential recognition of these proteolytic breakdown products. Group I MAbs bound a region proximal to the amino terminus of the protein. Two of these MAbs were also able to block leukoagglutinating activity. Group III MAbs bound to a region associated with the bacterial cell surface, while group II MAbs bound a region between group I and group III. These analyses have allowed the identification of potential structural and functional regions of p57.

Agglutination↗
PubMed1981

Sexual agglutination in Saccharomyces cerevisiae.

Treatment of either mating type of Saccharomyces cerevisiae with the appropriate sex pheromone increased cell-cell binding in a modified cocentrifugation assay. Constitutive agglutination of haploids was qualitatively similar to pheromone-induced agglutination. Regardless of exposure to pheromone, agglutinable combinations of cells exhibited maximal binding across similar ranges of ionic strength, pH, and temperature. Binding of all combinations was inhibited by 8 M urea, 1 M pyridine, or 0.05% sodium dodecyl sulfate. From alpha-cells we solubilized and partially purified an inhibitor of a-cell agglutinability. This inhibitor reversibly masked all a-cell adhesion sites and inactivated pheromone-treated and control cells with similar kinetics. The inhibitor behaved as a homogeneous species in heat inactivation experiments. Based on these results, we proposed a model for pheromone effects on agglutination in S. cerevisiae.

Agglutination↗
PubMed1992

Antibodies for trypsinized human red blood cells in human sera.

During studies of agglutination of trypsinized human red blood cells (RBC) by anti-Rh sera, it was noticed that some human sera without Rh antibodies agglutinated these erythrocytes. Of 933 normal and pathological sera subsequently screened, 116 produced such agglutination. The agglutinins were of IgM nature and were directed against an antigen exposed or created by tryptic digestion of RBC. They reacted equally well with autologous as with allogeneic trypsinized RBC and were different from T agglutinins and from Paul-Bunnell antibodies. The mode of formation of these antibodies remains unknown.

Antibodies↗
PubMed1983

Serological studies on Vibrio fluvialis.

The serology of 138 strains of Vibrio fluvialis was studied. Eighteen O-antigenic groups were defined among them and it was shown that the H antigens of all the strains were identical regardless of the biovar. The presence of mucoid antigen, which inhibits O agglutination, was found in some strains. As all O antisera for V. fluvialis contained some R antibody, all diagnostic O sera must be absorbed with R organisms before use. Some O antigens of V. fluvialis were identical with those of certain Vibrio cholerae serovars.

Africa↗
PubMed1979

[Presence of lectin-like substances in the basement membrane of the human kidney glomerulus].

Crude extracts from the human glomerular basement membranes solubilized by pepsin or bacterial collagenase agglutinate normal or transformed human cells. Cytoagglutination is inhibited by N-acetyl-osamines. These properties are reminiscent of lectins. When agglutinated cells are incubated for an additional 20 hrs. period in minimal serum free medium but in presence of these basement membrane extracts, they attach to the glass and spread out.

Agglutination↗
PubMed2002

[BjCHI1 from Brassica juncea displays both chitinase and agglutination activity].

The proteins encoded by the Brassica juncea chitinase gene BjCHI1 and its derived genes BjCHI2 and BjCHI3 were expressed by Multi-copy Pichia expression system. The chitinase activity of FPLC purified BjCHI1, BjCHI2 and BjCHI3 were tested and the results showed that all the three proteins degraded both CM-chitin-RBV and colloidal chitin. The Km values of BjCHI1, BjCHI2 and BjCHI3 for CM-chitin-RBV were estimated as 0.799 mg/mL, 0.544 mg/mL and 0.793 mg/mL, respectively. When the colloidal chitin was used as substrate, the Km values were 0.281 mg/mL, 0.388 mg/mL and 1.643 mg/mL, respectively, indicating chitin-binding domain can increase affinity of chitinase to insoluble substrate. In the agglutination activity assay, only BjCHI1 shows activity when the protein concentration was more than 33 micrograms/mL, while BjCHI2 and BjCHI3 without agglutination activity even when the concentration was increased as high as 800 micrograms/mL. This means that the two chitin-binding domains in BjCHI1 are essential for agglutination and BjCHI1 is the first protein which shows both chitinase and agglutination activity identified so far in plants.

Agglutination↗
PubMed1991

A 220 kDa coelomocyte aggregating factor involved in Holothuria polii cellular clotting.

Agglutinating molecules are released by Holothuria polii coelomocytes. In our in vitro system we observe that release depends on the number of coelomocytes but it seems not to be time- and temperature-dependent. The factor responsible for agglutination was isolated from an Edds isotonic solution coelomocyte suspension medium and purified by ammonium sulfate precipitation, gel filtration and ion exchange chromatography; it had a molecular mass of about 220 kDa on an sodium dodecyl sulfate polyacrylamide gel. The purified factor agglutinates sea cucumber coelomocytes suggesting that it could be involved in the first phase of clotting events.

Agglutination↗