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PubMed1984

The interaction of Brucella cell surface components with plant agglutinins.

Cells of all Brucella species were agglutinated by the basic protein-reactive lectins of Mangifera indica and Persea americana. Cells of non-smooth strains including B. ovis and B. canis but not smooth strains were also agglutinated by concanavalin A. These lectins also reacted in a similar pattern with lipopolysaccharide extracts of these organisms. The lectin from Bandeiraea simplicifolia precipitated with the lipopolysaccharide antigens of smooth Brucella organisms and with those of serologically cross-reactive strains of Escherichia coli, Pseudomonas maltophilia, Salmonella and Yersinia enterocolitica but not with antigenically unrelated strains.

Agglutination Tests↗

PubMed1989

Sero-prevalence of agglutinins to Listeria monocytogenes in Nigerian domestic animals.

A survey using tube agglutination test was conducted to determine the antibody prevalence to Listeria monocytogenes serotypes 1/2a, 1/2b, 1/2c, 3a and 4b in 1,190 serum samples of 8 animals species from various sources in Kano and Kaduna states of Nigeria. Following absorption with Staphylococcus aureus antigen to remove cross-reacting agglutinins, 52 (68.4 p. 100) of the horse samples were positive. Twenty-six (36.1 p. 100) pig, 52 (20.8 p. 100) cattle, 50 (20.0 p. 100) goat, 20 (20.0 p. 100) dog, serum samples were also positive. Free-ranging chickens had an antibody prevalence of 18 (32.1 p. 100) while those intensively managed had 3 (6.8 p. 100), a difference found to be statistically significant (P less than or equal to 0.01; X2). Sheep sera collected from Zaria abattoir had a prevalence of 30 (14.7 p. 100) while those from Ahmadu Bello University, Veterinary Teaching Hospital had 6 (13.0 p. 100) prevalence. The prevalence in camel was 4 (4.3 p. 100). Overall, of the 1,190 serum samples tested, 26 (21.9 p. 100) were sero-positive for L. monocytogenes agglutinins. Each species of animal tested for L. monocytogenes was positive for all five serotypes, except camel which was negative for serotype 3a. Fourty-four (53.0 p. 100) samples were positive at a titre of greater than or equal to 480 for serotypes 1/2a, 60 (58.3 p. 100) for 1/2b, 57 (52.3 p. 100) for 1/2c, 7 (13.7 p. 100) for 3a and 23 (39.0 p. 100) for 4b. It is concluded that L. monocytogenes infection is widespread in domestic animals in Nigeria.

Agglutination Tests↗

PubMed1989

AG alpha 1 is the structural gene for the Saccharomyces cerevisiae alpha-agglutinin, a cell surface glycoprotein involved in cell-cell interactions during mating.

We have cloned the alpha-agglutinin structural gene, AG alpha 1, by the isolation of alpha-specific agglutination-defective mutants, followed by isolation of a complementing plasmid. Independently isolated alpha-specific agglutination-defective mutations were in a single complementation group, consistent with biochemical results indicating that the alpha-agglutinin is composed of a single polypeptide. Mapping results suggested that the complementation group identified by these mutants is allelic to the ag alpha 1 mutation identified previously. Expression of AG alpha 1 RNA was alpha specific and inducible by a-factor. Sequences similar to the consensus sequences for positive control by MAT alpha 1 and pheromone induction were found upstream of the AG alpha 1 initiation codon. The AG alpha 1 gene could encode a 650-amino-acid protein with a putative signal sequence, 12 possible N-glycosylation sites, and a high proportion of serine and threonine residues, all of which are features expected for the alpha-agglutinin sequence. Disruption of the AG alpha 1 gene resulted in failure to express alpha-agglutinin and loss of cellular agglutinability in alpha cells. An Escherichia coli fusion protein containing 229 amino acids of the AG alpha 1 sequence was recognized by an anti-alpha-agglutinin antibody. In addition, the ability of this antibody to inhibit agglutination was prevented by this fusion protein. These results indicate that AG alpha 1 encodes alpha-agglutinin. Features of the AG alpha 1 gene product suggest that the amino-terminal half of the protein contains the a-agglutinin binding domain and that the carboxy-terminal half contains a cell surface localization domain, possibly including a glycosyl phosphatidylinositol anchor.

Agglutinins↗

PubMedDate not supplied

Serologic activity of fatty acid dependent antibodies in albumin-free systems.

Fatty acid dependent agglutinin (FADA) refers to serum with the special ability to cause agglutination of red blood cells in the presence of certain fatty acids. The agglutinating mechanism is unclear. It has been proposed that the agglutinin reacts with albumin that has been conformationally altered by sodium caprylate and that the immune complex is passively adsorbed onto red blood cells. This report presents data that contradicts the proposal assigning a specific role to albumin in the agglutinating mechanism. FADA were isolated by column chromatography of resolubilized euglobulin preparations. No evidence of contamination with albumin was obtained in those IgM fractions possessing FADA activity. We propose, as an alternative explanation, that the serologic activity of FADA depends upon the interaction of IgM agglutinins with haptenic fatty acids.

Antibody Specificity↗

PubMedDate not supplied

Comparative studies of the interaction between lectins and Leishmania in agglutination tests and enzyme-linked lectin-biotin assays (ELLBA).

It was demonstrated that soybean agglutinin and peanut agglutinin aggregated all the investigated species of Leishmania, including virulent and avirulent members of L. major in agglutination tests. Concanavalin A and Pisum sativum agglutinin were shown to aggregate L. species ZMA and L. major but showed no effect on L. gymnodactyli and L. mexicana amazonensis which were aggregated by wheat germ agglutinin, an extract from Ulex europaeus and Ricinus communis. There was no correlation between the results of ELLBA studied in agglutination tests. The results indicate that the surfaces of Leishmania strains and species are heterogeneous with respect to lectin binding. There are possibly two subsets of lectin receptors on the surface structures of Leishmania cells.

Agglutination Tests↗

PubMed1989

Alpha-agglutinin expression in Saccharomyces cerevisiae.

A polyclonal antiserum raised against purified alpha-agglutinin was made specific for alpha-agglutinin after adsorption with a cells. The adsorbed antiserum identified alpha-agglutinin peptides on Western blots and bound to cell surface alpha-agglutinin, inhibiting the binding of alpha cells to a cells. Using the antibody, we have determined that 1) the surface distribution of alpha-agglutinin on alpha cells is polar, 2) about 5 x 10(4) molecules/cell are constitutively expressed on strain X2180-1B (alpha) cells, and 3) treatment of alpha cells with the sex pheromone a-factor causes an increase in cell surface alpha-agglutinin, consistent with the a-factor induced increase in cell agglutinability.

Agglutinins↗

PubMed1983

The adhesive glycoprotein laminin is an agglutinin.

The glycoprotein laminin appears to function in the attachment of various epithelial cells to basement membranes. We examined whether its putative cell-adhesive activity could be analyzed in a simple, one-component model system--the agglutination of erythrocytes. Laminin is a potent agglutinin of aldehyde-fixed sheep and human erythrocytes, with half-maximal agglutination at 0.8 micrograms/ml in a standard hemagglutination assay. Inhibitors of this hemagglutinating activity include gangliosides and certain charged phospholipids. The spectrum of molecules is similar but not identical to inhibitors of the hemagglutinating activity of the adhesive glycoprotein fibronectin. Laminin is much less biologically active in three other assays for fibronectin biological activity involving cell spreading on tissue culture substrates, attachment of fibroblastic cells to type I collagen, and restoration of normal morphology to transformed fibroblasts. The adhesive glycoproteins laminin and fibronectin therefore differ markedly in biological activities in several specific adhesion assays; however, they resemble one another in binding to heparin, collagen, and cell surfaces and in their agglutinin activity.

Animals↗

PubMed1982

Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidia malaca Traust. hemagglutinins.

The carbohydrate specificities of Ascidia malaca serum hemagglutinins were determined by hemagglutination inhibition tests. Analysis of agglutinins against rabbit and human A, B, O erythrocytes suggests that the size of the combining site corresponds to a disaccharide with a specificity for saccharides containing a D-galacto configuration (D-melibiose, D-raffinose, D-galactose, alpha-lactose, lactulose, L-arabinose). No anomeric specificity was observed with oligosaccharides. Hydroxyl groups probably involved in hydrogen-bond formation with agglutinin binding site, were identified as carbons C2, C4, C5 and C6 of D-galactose. Absorption experiments showed that two distinct agglutinins with similar sugar specificity ranges were responsible for rabbit and human erythrocyte agglutination. The D-galactose specificity of the agglutinins allowed the isolation, by biospecific affinity chromatography of the serum, of a protein fraction demonstrated by polyacrylamide gel electrophoresis.

Animals↗

PubMed1979

Lectins in diagnostic microbiology: use of wheat germ agglutinin for laboratory identification of Neisseria gonorrhoeae.

A lectin slide agglutination test has been developed for the confirmatory identification of Neisseria gonorrhoeae. With wheat germ lectin as an agglutinin, 164 of 165 clinical isolates of N. gonorrhoeae gave a 3 to 4+ reaction within 6 to 8 min. Four gonococcal isolates, even though negative by the fluoresecent-antibody method, gave strong positive reactions with the wheat germ lectin. Among 23 isolates of Neisseria meningitidis tested, which included representatives of sero-groups A, B, C,D, X, Y, and Z, only one strain in group X gave a false-positive reaction. The nonpathogenic species of Neisseria, as well as Branhamella catarrhalis, all showed negative reactions with the wheat germ agglutinin. The novel method provides a simple, rapid, and inexpensive means for the laboratory diagnosis of gonorrhea and obviates the need for performing second-stage sugar fermentation studies or utilizing the more expensive fluorescent-antibody techniques.

Acetylglucosamine↗

PubMed1983

Comparative studies of Trypanosoma cruzi and T. cruzi-like stocks from different South American countries using lectins.

The agglutination behaviour of four-day-old epimastigote culture forms of 34 Trypanosoma cruzi, and T. cruzi-like stocks from Brazil, Chile, Colombia, Ecuador and Peru were tested with 15 carbohydrate-specific lectins. We distinguished intraspecifically two groups of agglutination reactions: Group 1 includes stocks which react with Triticum vulgaris and Aaptos papillata II (wheat germ agglutinin: WGA-type). Group 2 includes stocks agglutinated by Arachis hypogaea and Aaptos papillata II (peanut lectin: PNA-type). The agglutination reactions with lectins from Triticum vulgaris and Aaptos papillata II correlate with the presence of N-acetylneuraminic acid on the cell surface. After treatment with neuraminidase, the WGA-type is agglutinated by PNA but not by lectins from Triticum vulgaris and Aaptos papillata II. Further results demonstrate that a certain zymodeme pattern can be correlated with carbohydrate determinants.

Agglutination Tests↗

PubMed1996

Seroprevalences of brucellosis, Q-fever and toxoplasmosis in slaughter livestock in Trinidad.

Serum samples obtained from livestock (cattle, chickens, pigs, sheep, goats and water buffaloes) slaughtered at various slaughter houses in Trinidad were screened for agglutinins to three zoonosis causing pathogens. Of a total of 751 sera tested, 2 (0.3%) originating from chickens were positive for Brucella abortus agglutinins using the Rose Bengal test (RBT), but both were negative by the tube serum agglutination test (SAT). Thirty-six (4.8%) of 749 sera were positive for Coxiella burnetii agglutinins by the capillary agglutination test (CAT) with the highest prevalence, 11.3%, detected in pig sera and the lowest, 0%, found in sheep and goat sera. The difference was not statistically significant (P > or = 0.05; chi 2). Of the 131 sera tested, 26 (19.8%) contained Toxoplasma gondii agglutinins with prevalences ranging from 5.5% in pigs to 42.9% in goats. It was concluded that livestock in Trinidad are free of B. abortus infections, but C. burnetii and T. gondii infections exist and are being documented for the first time in the island.

Animals↗

PubMed1986

Anaplasma marginale, Eperythrozoon wenyoni: lectin reactions with bovine erythrocytes.

Normal bovine erythrocytes were agglutinated with four of five lectins specific for different oligosaccharides. The order of reactivity was wheat germ greater than ricin greater than soybean greater than peanut. Concanavalin A did not agglutinate normal bovine erythrocytes. After neuraminidase treatment of normal bovine erythrocytes, each lectin agglutinated the cells with decreased concentrations of lectin, verifying that partial removal of sialic acid exposes more of each lectin's binding sites or alters the binding site such that fewer molecules of lectin are required to initiate agglutination. A change in agglutination of erythrocytes using soybean agglutinin and peanut agglutinin occurred when cells were obtained from cattle infected with Eperythrozoon wenyoni. The results suggested that an alteration in erythrocyte membranes occurred as a result of this infection as manifested by the increased recognition of both the soybean agglutinin and peanut agglutinin receptor carbohydrates. A similar effect was indicated with erythrocytes obtained during an acute Anaplasma marginale infection; however, an ensuing reticulocytosis masked the effect, requiring the use of fluoresceinated lectins to verify that increased binding of each lectin occurred with infected cells when compared to normal cells.

Anaplasmataceae Infections↗

PubMed2005

Effect of staurosporine on N-glycosylation and cell adhesion to fibronectin of SW480 human colorectal adenocarcinoma cells.

As N-glycosylation of tumor cell surface proteins affects metastasis of the cells, it was considered that the suppression of metastasis by staurosporine, a protein kinase C inhibitor, is partly caused by changes in N-glycosylation. To examine this possibility, we studied the glycosylation of membrane proteins of SW480 human colorectal adenocarcinoma cells before and after treatment with staurosporine by lectin blot analysis. The results showed that the reactivity of leuko-agglutinating phytohemagglutinin and Datura stramonium agglutinin, both of which bind to highly branched N-linked oligosaccharides characteristic of cancer cells, decreases significantly in the staurosporine-treated cells. In accordance with this, the gene expression of the N-acetylglucosaminyltransferase V, which synthesizes the GlcNAcbeta1-->6 branch of highly branched N-linked oligosaccharides decreased by 30-40% in the drug-treated cells. Since a decrease in the lectin binding was found in several glycoproteins including fibronectin (FN)-receptor, effect of the changes in N-glycosylation of the cells on cell adhesion to FN-matrix was examined. The results showed that the number of cells attached to FN-matrix increases upon treatment of the cells with staurosporine, indicating that the change of N-glycosylation of the FN-receptor promotes cell adhesion to the extracellular matrix, which may lead to the suppression of metastasis of cancer cells.

Adenocarcinoma↗

PubMed1986

Fc receptor-independent phagocytosis by mouse macrophages of erythrocytes sensitized with a lectin from a marine invertebrate.

A lactose-specific lectin present in the haemolymph of the colonial ascidian Botrylloides leachii was tested for its ability to act as an opsonin for the phagocytosis of erythrocytes by mouse macrophages. Sensitization of sheep or mouse erythrocytes with one agglutinating dose of the invertebrate agglutinin enhanced significantly the clearance of these cells from the circulation of mice, as did treatment with specific antibody. By measuring the adhesion and phagocytosis of 51Cr-labelled erythrocytes by monolayers of macrophages in vitro, it was shown that the B. leachii agglutinin was highly opsonic, promoting the ingestion of erythrocytes by the macrophages with an initial efficiency similar to that of specific antibody. The adherence and ingestion of antibody-coated erythrocytes was severely inhibited by blocking Fc receptors on the macrophages with soluble immune complexes, whereas the binding and ingestion of lectin-coated erythrocytes was unaffected by this treatment. The results demonstrate that invertebrate lectins can act as efficient opsonins for the uptake of particles by vertebrate phagocytes and that it is not necessary for particles to bind to Fc receptors for phagocytosis to be induced.

Animals↗

PubMed1993

Recombinant vaccines against ovine footrot.

For the past 20 years footrot vaccines have evolved from simple bacterins to highly specific recombinant DNA (rDNA) fimbrial vaccines. The development of these vaccines has left a trail of discoveries, challenges and solutions; these processes continue as we move closer to understanding the requirements of a footrot vaccine. The initial whole cell vaccines were unsuccessful due to the short duration of immunity and incorporation of limited serotypes. A multistrain vaccine eliminated the problem of serotype inclusion, although the duration of immunity in many cases is still inadequate. The proteases of Dichelobacter nodosus appear to be cross protective; however, little is known of their ability to protect sheep against footrot. The major protective immunogen is the bacterial fimbriae, which also forms the basis for the K-agglutination serotyping system. K-agglutinin titre correlates directly with resistance to challenge. The protective fimbrial epitope is conformationally dependent, suggesting little advantage in the development of synthetic peptide vaccines. To enhance the efficiency of vaccine production D. nodosus fimbrial genes were eventually cloned and successfully expressed in Ps. aeruginosa. Monovalent vaccines based on recombinant fimbriae are omnipotent, inducing high levels of agglutinins and long lasting immunity. In multivalent vaccines, on the other hand, incorporation of each additional serogroup into the vaccine results in reduced efficacy both in terms of reduced K-agglutinin titres and reduced protection following challenge. The least effective are multivalent formulations representing all major serogroups. In addition, considerable genetic variation has been observed in the ability of sheep to respond optimally to each serogroup in a multivalent vaccine. Results show that the limitation of the sheep to mount an effective immune response, rather than the quality or quantity of the immunogen, limits the efficacy of current footrot vaccines. Studies are being undertaken to examine in detail the immune response of sheep to potentially highly effective footrot vaccines.

Animals↗

PubMed1993

Course of infection and humoral immune reaction in calves infected orally with different Salmonella serovars.

5 groups of five calves each were orally infected with the salmonella serovar S. agona, S. dublin, S. enteritidis, S. infantis or S. typhimurium. The course of infection and the humoral immune response against 5 antigen preparations of the homologous and the 4 heterologous salmonella serovars were monitored in each group. Antibodies against two different protein antigens and against two differently prepared LPS antigens were determined by ELISA and the level of H-agglutinin was assessed by micro agglutination test. All 5 serovars proved to be virulent for calves. The specificity of antibodies produced following the infection are not always consistent with the Kauffmann-White scheme. There was a relation of age and strain for infection on immune response, whereas the severity of infection did no correlate with an increase of antibody production. The serological tests used were good for investigation of a defined host-parasite-interaction but not satisfactory for serovar specific diagnosis of salmonella infection in cattle.

Animals↗

PubMed1970

Detection of foot-and-mouth disease virus antibodies. I. "Passive" hemagglutination test.

A passive hemagglutination test has been developed to detect and measure foot-and-mouth disease virus (FMDV) antibody by using glutaraldehyde as a coupling reagent. An optimal concentration of 10 to 40 mug of virus per ml with 0.25% glutaraldehyde at 25 C for 1 hr was established for the sensitization of sheep erythrocytes. A reaction time of 18 hr at 4 C or 2 hr at 37 C induced good agglutination in the presence of specific antibody. Sensitization was carried out in phosphate buffer, whereas agglutination and preadsorption of nonspecific agglutinins from sera were performed in gelatin (0.1%, w/v)-stabilized, phosphate-buffered saline. An optimal pH of 7.2 was also established for all reactions. Antibodies derived from guinea pigs hyperimmunized by infecting with FMDV, types A, O, and C were both virus-and type-specific. Preliminary experiments showed that strain A-119 and strain A-24 Cruzeiro could also be distinguished by hemagglutination. Parallel hemagglutination and complement-fixation tests showed the former to be two to four times more sensitive than the latter.

Aldehydes↗

PubMed1989

Indirect immunoglobulin G (IgG) and IgM enzyme-linked immunosorbent assays (ELISAs) and IgM capture ELISA for detection of antibodies to lipopolysaccharide in adult typhoid fever patients in Pakistan.

Sera from 339 adult febrile patients in Pakistan were tested for antibodies to Salmonella typhi lipopolysaccharide by indirect immunoglobulin G (IgG) and IgM enzyme-linked immunosorbent assay (ELISA) and IgM capture ELISA. A total of 55 patients had S. typhi cultured from their blood, 20 had S. typhi cultured from their stool, 24 were blood or stool culture positive for S. paratyphi A, 41 were culture negative but clinically diagnosed as having enteric fever, 41 had gastrointestinal or urinary tract infections, 41 were clinically diagnosed as having malaria, 20 were smear-positive patients with malaria, 58 had respiratory infections, and the remaining 39 individuals were placed in a miscellaneous group who did not have Salmonella infection. The sensitivities of the indirect IgG ELISA, indirect IgM ELISA, and IgM capture ELISA determined with specimens obtained from the blood culture-positive patients with typhoid fever (positive controls) were 80, 64, and 62%, respectively. The specificities of the assays determined with sera from the patients with respiratory infections (negative controls) were 95, 95, and 97%, respectively. The percentage of smear-positive patients with malaria who were positive by these assays was lower than that in the negative control group. The percentages of individuals in the other patient categories who were positive by these tests were between those obtained with the positive and negative controls. Of the positive controls, 26 were positive by both IgM assays, 9 were IgM positive only by indirect ELISA, and 8 were IgM positive only by IgM capture ELISA. A total of 70% of the positive control patients who were tested for O agglutinins by the Widal tube agglutination assay were positive; however, 29% of the negative control patients were also positive. The indirect IgG ELISA was the single most effective test for the serodiagnosis of typhoid fever in this population.

Adolescent↗