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PubMed1985

Interaction of human erythrocyte Band 3 with Ricinus communis agglutinin and other lectins.

Agglutination and competition studies suggest that human erythrocyte Band 3 can interact with both mannose/glucose- and galactose-specific lectins. Purified Band 3 reconstituted into lipid vesicles binds concanavalin A, but the nonspecific binding component, measured in the presence of alpha-methylmannoside, is very high. This glycoprotein also carries binding sites for the galactose-specific lectin Ricinus communis agglutinin. Binding was inhibited poorly by lactose, but much more effectively by desialylated fetuin glycopeptides, suggesting that the lectin recognizes a complex oligosaccharide sequence on Band 3. The glycoprotein bears two separate classes of binding sites for R. communis agglutinin. High-affinity binding sites exist which show strong positive cooperativity and correspond in number to the outward-facing Band 3 molecules. A low-affinity binding mode is abolished by 40% ethyleneglycol, suggesting the involvement of hydrophobic lectin-glycoprotein interactions. Studies on binding of R. communis agglutinin to human erythrocytes indicate positively cooperative binding to 7 X 10(5) very-high-affinity sites per cell, and lectin binding is completely inhibitable by lactose. Based on its binding characteristics in vesicles, it seems likely that Band 3 forms the major receptor for this lectin in human erythrocytes. Properties such as positive cooperativity thus appear to be a common feature of the interaction of Band 3 with a variety of lectins of different specificity, both in erythrocytes and lipid bilayers.

Anion Exchange Protein 1, Erythrocyte↗
PubMed1973

Agglutination of Sindbis virus and of cells infected with Sindbis virus by plant lectins.

We have examined the agglutination of Sindbis virus and of chick and hamster cells infected with Sindbis virus by two of the plant lectins, concanavalin A and Ricinus communis agglutinin. Both lectins agglutinate the virus by binding to the polysaccharide chains of the envelope glycoproteins. Both chick and hamster cells exhibit increased agglutination by the lectins after infection by Sindbis virus. In the case of chick cells infected with Sindbis virus, this increase in agglutinability occurs between 3 and 5 h after infection. Infected and mock-infected cells bind the same amount of (3)H-labeled concanavalin A, which suggests that the increase in agglutination after infection is due to rearrangements at the cell surface rather than to insertion of new lectin binding sites per se.

Agglutination↗
PubMed2005

Yersinia Yop-specific IgA antibodies in Hungarian blood donors.

Sera of 112 healthy Hungarian blood donors were tested for the presence of Yersinia enterocolitica and Y. pseudotuberculosis-specific agglutinins by tube agglutination, and for that of yersinia outer membrane protein (Yop)-specific IgA antibodies by ELISA. The positive results of this latter assay were confirmed by immunoblot. Only one sample gave a positive agglutination reaction with Y. enterocolitica antigen (group 03) and four exhibited an equivocal reaction with Y. pseudotuberculosis antigens (groups II and IV). Contrary to the low incidence of agglutinins, 15.1% of the samples showed a positive Yop-specific IgA reaction, while further 5.3% samples fell into the equivocal range by ELISA (17 and 6 specimens, respectively). Eleven of these samples (9.8% of all specimens tested) were also positive by immunoblot for the presence of Yop-specific IgA antibodies. These data suggest a higher incidence of yersinia infections than the 1.0-1.4 per 10(5) population predicted on the basis of stool culture results.

Adult↗
PubMedDate not supplied

[Survey of anti-Leptospira agglutinins in workers from the city of Londrina-Paraná, Brazil].

Serum samples were obtained from 249 individuals in Londrina-Paraná, Brazil. The sera were analysed for leptospiral agglutinins by microscopic agglutination tests and 22.1% were positive. Of these positives per group were 24.6% for butchers, 25.9% for farm workers, 17.2% for children and 22.2% for servants. The agglutinin titers ranged from 1:200 to 1:3200. The highest titers were obtained for the serovars sejroe (butchers), grippotyphosa (farm workers), javanica, canicola, panama, wolffi and pyrogenes (children) and butembo (servants).

Abattoirs↗
PubMed1993

Separation of bacteria using agglutinins isolated from invertebrates.

The agglutination of a selection of Gram-positive and Gram-negative bacteria by the haemolymph and coelomic fluid from several invertebrates was studied. The haemolymph from Lumbricus terrestris and Limulus polyphemus caused the strongest agglutination of most of the bacteria studied. When the agglutinating fraction of Lim. Polyphemus was liganded to magnetic microspheres 53% of the cells in pure cultures of Listeria monocytogenes C200, 15% of Salmonella enteritidis 37782, 92% of Staphylococcus aureus NCDO 949, 19% of Escherichia coli E4936/76 and 65% of E. coli W2-2 were adsorbed to the beads. The immobilized haemolymph from Lumb. terrestris adsorbed 42% of Salm. enteritidis 37782, 64% of E. coli 4936/76 and 27% of Staph. aureus NCDO 1499 cells and the coelomic fluid from Haemopsis sanguisuga adsorbed 42, 48 and 50% of these cultures respectively. With immobilized Haem. sanguisuga agglutinins, 21-27% of Staph. aureus NCDO 2044 cells were recovered from full-fat pasteurized milk and 20-51% from braising steak. Immobilized Lim. polyphemus agglutinins recovered 17-34% of Staph. aureus cells from raw egg. The potential of agglutinins isolated from invertebrates for enhancing rapid microbiological assays of foods is discussed.

Agglutination Tests↗
PubMed1980

Lectin-mediated aggregation of liposomes containing glycolipids with variable hydrophilic spacer arms.

Synthetic glycolipids containing a cholesterol anchor group attached via a spacer group to a sugar moiety can be incorporated into small unilamellar liposomes, rendering them susceptible to agglutination by the appropriate multivalent lectin [Rando, R. R., Orr, G. A., & Bangerter, F. W. (1979) J. Biol. Chem. 254, 8318-8323; Rando, R. R., & Bangerter, F. W. (1979) J. Supramol. Struct. 11, 295-309]. We report here on the role of spacer arm length in rendering these liposomes susceptible to agglutination. In order to eliminate the ambiguities inherent in using hydrophobic or charged spacer groups, we have synthesized a hydrophilic, ethylene glycol based amino acid (8-amino-3,6-dioxaoctanoic acid) for these studies. The Ricinus communis agglutinin (ricin) mediated agglutination of these beta-galactoside-containing glycolipids was studied. A spacer arm length of four atoms will not support agglutination under any conditions. A seven-atom spacer will support agglutination, but only at high phospholipid concentrations (0.24 mumol/mL) with a pseudo-first-order rate of agglutination of 0.0079 min-1. With 13 and 22 atom spacer groups, the pseudo-first-order rate constants were 0.4 min-1 and 1.3 min-1, respectively, at a phospholipid concentration of 0.06 mumol/mL. Under conditions where the liposomes containing the glycolipid with the 13-atom hydrophilic spacer arm were completely agglutinated by ricin, 9.3% of the total available sugar moieties of the liposome were bound to ricin. This means that, on the average, 38 interliposomal bonds were formed in an aggregate.

Agglutination↗
PubMed1969

Antibody response of animals to Mycoplasma pneumoniae measured by latex agglutination.

The standardization, application, and usefulness of latex agglutination for Mycoplasma pneumoniae antibody titration were investigated and compared with tetrazolium reduction inhibition and complement fixation. The sera of guinea pigs and monkeys reacted in a specific fashion, whereas rabbit serum required pretreatment to eliminate its nonspecific agglutinin. Human serum given such pretreatment still contained a nonspecific agglutinin. The latex agglutination procedure compared favorably with complement fixation and metabolic inhibition tests for evaluating vaccine antigenicity.

Animals↗
PubMed1974

Cell surface galactosyltransferase and lectin agglutination of thymus and spleen lymphocytes.

Lectin agglutination and cell surface galactosyltransferase (EC 2.4.1.67; 1-O-alpha-D-galactosyl-myo-inositol:raffinose galactosyltransferase) enzyme activity have been studied with thymus and spleen lymphocytes of neonatal rats. Thymus lymphocytes were more agglutinable by concanavalin A than by wheat germ agglutinin, whereas spleen lymphocytes were more agglutinable by wheat germ agglutinin than by concanavalin A. Thymus lymphocytes, but not spleen lymphocytes, of neonatal rats could be blast transformed by concanavalin A. Cell surface galactosyltransferase activity was present on both types of lymphocytes, but was greatly increased on thymus cells after blast transformation. The differences in lectin agglutination suggest a difference in the surface membranes of thymus and spleen lymphocytes. The increase in cell surface galactosyltransferase activity with blast transformation of thymus lymphocytes may be related to the exteriorization of the Golgi apparatus into the plasma membrane.

Agglutination↗
PubMed1979

Spectrum of Escherichia coli agglutinins in dam's sera, colostrum and calf's sera in Fresian cows and buffaloes in Egypt.

Sera collected from 18 pregnant buffaloes and Fresian cows during the last two weeks before parturition and from the newborn calves during the first two weeks after birth. All the samples together with the colostral whey of the first three days were examined for the presence of E. coli agglutinins using the tube agglutination and passive hemagglutination tests. The latter test was more sensitive and demonstrated higher titres in all cases, and consequently more O groups. Agglutinins to various E. coli O groups were detected in all samples. It is worthy to note that agglutinins to all E. coli O groups used as antigens were detected in 13 dam's sera, 17 colostrum and in one buffaloe calf. The titres were higher in colostrum than in dam's or calf's sera. The highest titre was 1:640. The O groups 101, 115, 117, and 26 were the most common among Fresian cows whereby the O groups 101 and 115 showed the highest titres. In buffaloes the O groups 101, 115, 8 and 26 were the most common with the O8 having the highest titre.

Agglutination Tests↗
PubMed1970

Antileptospiral agglutinins produced in rabbits.

Agglutinating antibodies produced in an adult rabbit in response to intravenous injections of live Leptospira sp. (serotype biflexa, strain Waz), consisted of a 19S component (present at day 6 after inoculation) and a 7S component (present at day 6 after inoculation). Both 19S and 7S antibodies persisted in the serum until the conclusion of the observations (day 216). The 19S antibody was completely destroyed by 2-mercaptoethanol but the 7S antibody was only partially sensitive to 2-mercaptoethanol.The serum proteins present in the 19S and 7S serum fractions were determined by immunoelectrophoresis and cellulose acetate electrophoresis. Elution of the serum components from cellulose acetate membranes directly confirmed that the beta-migrating IgM was the 19S serum component with leptospiral agglutinating activity and that gamma-migrating IgG was the 7S serum component with antileptospiral agglutinating activity.

Animals↗
PubMed1986

Calcium-dependent salivary agglutinin with reactivity to various oral bacterial species.

Human parotid agglutinins from three individuals were isolated by adsorption to and desorption from strains of Streptococcus mutans belonging to serotypes a, b, c, d, and e and strains of Lactobacillus casei, Actinomyces viscosus, and Streptococcus sanguis. The desorption was achieved by suspending centrifuged saliva-coated microorganisms in 10 mM phosphate buffer (pH 6.8) containing 0.154 M sodium chloride. After another centrifugation, agglutinin activity was recovered in the supernatants. The L. casei strain was not agglutinated by any of the agglutinin extracts or by saliva, but all the other strains were agglutinated to a variable extent. However, all strains, including the nonagglutinating L. casei strain, adsorbed and desorbed agglutinins active for other strains. The agglutinin extracts from S. mutans serotype c, S. sanguis, and A. viscosus were purified and characterized by electrophoretic and immunological techniques. The purified preparations were positively stained for protein and carbohydrate, and the molecular weights were estimated to be 440,000. All agglutinin extracts needed calcium in the range of 0.1 to 0.5 mM to be active, and for a single strain, all agglutinins gave the same degree of agglutination, indicating that the isolated agglutinins may be of the same molecular species, a hypothesis that was also confirmed by the preliminary characterization of the purified agglutinins. This type of agglutinin, which seems to exert its activity among various bacterial species, could be important in mediating bacterial coaggregation and thus may add to the effect of specific agglutinins in the clearance of bacteria from the human mouth.

Actinomyces↗
PubMed1982

Functional and phenotypic properties of subpopulations of murine thymocytes. I. The bulk of peanut agglutinin-positive Lyt-1,2,3 thymocytes lacks precursors of cytotoxic T lymphocytes responsive to interleukin 2 (T cell growth factor).

Thymocytes were separate according to their surface phenotype and tested for cytotoxic T lymphocyte (CTL) precursor function by stimulation with allogeneic or hapten-coupled cells, with or without addition of T cell growth factor (interleukin 2). The data show that only a minor subpopulation of thymocytes agglutinated by peanut agglutinin, expressing relatively high amounts of H-2K antigen, contained CTL precursors. The remaining population, approximately 80%, could not be induced to generate CTL, even in the presence of interleukin 2.

Animals↗
PubMed1975

The surface membrane of Leishmania. I. The effects of lectins on different stages of Leishmania braziliensis.

The infective stages of Leishmania braziliensis, amastigotes and promastigotes subcultured a limited number of times, were agglutinated by Ricinus communis agglutinin and Concanavalin A. These results suggest that terminal ligands similar or identical with alpha-D mannose, alpha-D glucose (specific receptors for Con A), and alpha-D galactose (specific receptor for RCA) are present in the surface membrane of L. braziliensis. Noninfective promastigotes from the same stock, but subcultured approximately 500 times, were not agglutinated by RCA suggesting either the absence of the alpha-D galactose groups in the surface membrane or their presence in a very reduced number. Agglutination with soybean agglutinin, wheat germ agglutinin, or phytohemagglutinin P was not observed in any of the L. braziliensis forms tested. The difference in polysaccharide residues on the surface membrane of L. braziliensis may be related to the different pathogenic properties of the cell.

Agglutination↗