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PubMed1987

A new agglutinin from the Tulipa gesneriana bulbs.

Two agglutinins with different agglutinating activity exist in Tulipa gesneriana bulbs. One is the T. gesneriana lectin which agglutinates yeasts as reported previously [Oda, Y. and Minami, K. (1986) Eur. J. Biochem. 159, 239-245]. The other agglutinin is a new one which agglutinates animal erythrocytes and was purified from the tulip bulbs using affinity chromatography on thyroglobulin-Sepharose 4B. The agglutinin agglutinated mouse and rat erythrocytes at a minimum concentration of 2 micrograms/ml and 30 micrograms/ml respectively, but did not agglutinate erythrocytes from other animals and yeasts even at a concentration of 1000 micrograms/ml. The agglutinin appeared homogeneous by disc gel electrophoresis at pH 4.3 and gel filtration. Its relative molecular mass was determined by gel filtration to be approximately 40,000. It was suggested that the agglutinin was composed of two different subunits of 26 kDa and 14 kDa by sodium dodecyl sulfate/polyacrylamide gel electrophoresis analysis. Binding of radioiodinated agglutinin to mouse erythrocytes indicated that the presence of a high-affinity site with a dissociation constant of 2.00 X 10(-9) M. In inhibition experiments thyroglobulin glycopeptides were the most potent inhibitors; thyroglobulin was also a potent inhibitor. Orosomucoid and mucin showed weak inhibition. The other glycoproteins, glycopeptides and sugars examined showed no inhibition.

Agglutination Tests↗
PubMed1979

Biological activity of secretory IgA--comparison of agglutinating specificity with SIgA and Ca++-dependent agglutinin--.

Ca++-dependent bacterial agglutinin was isolated from the human parotid saliva by gel filtration of Sepharose 2B. The agglutinin appeared in the void volume fractions. Treatment of this agglutinin with EDTA resulted in the loss of its ability to agglutinate the bacteria. Standardized solutions of the agglutinin were tested for the agglutinating activity against 18 strains of oral indigenous bacteria. It was found that the agglutinin exhibited varying degrees of activity to all the test strains and the activity was generally higher than that of secretory IgA. It was also found that the receptor sites of the Ca++-dependent agglutinin for Str. sanguis and Str. mitis were identical whereas SIgA contained a number of available binding sites, for different bacterial species.

Adult↗
PubMed1983

Degradation of the microbial and salivary components participating in human dental plaque formation by proteases elaborated by plaque bacteria.

Twenty-eight strains of facultative, Gram-positive, sporulating bacilli which produce caseinolytic enzymes were isolated from human early dental plaque. A major component of the extracellular caseinolytic enzymes elaborated by strong producers seemed to be neutral zinc proteases. The extracellular proteases inactivated glucosyltransferase of Streptococcus mutans and inhibited the synthesis of adherent glucans from sucrose. The enzymes also degraded the Strep. mutans cell-surface receptor for dextran and glucan, the receptor for salivary agglutinins, located on Streptococcus sanguis cells, and the surface component of Actinomyces viscosus cells involved in co-agglutination with Strep. sanguis cells. The enzymes hydrolysed human whole saliva proteins, which seemed to result in loss of the ability to agglutinate Strep. sanguis cells.

Actinomyces↗
PubMed1981

Lectin binding by Giardia lamblia.

Surface carbohydrates of Giardia lamblia were examined using six plant lectins chosen because of their specificity for major carbohydrates moieties. The binding to axenically grown G. lamblia trophozoites was assessed in both a quantitative microagglutination assay and a fluorescence assay. Of the six lectins tested, wheat germ agglutinin (WGA) agglutinated the highest percentage (22.9 +/- 3.7%) of live trophozoites, and fluorescein-labeled WGA (100 micrograms/ml) bound to 98 +/- 5% of them. Since the carbohydrate specificity of WGA includes both N-acetyl-D-glucosamine (GlcNAc) and sialic acid, inhibition experiments were performed. GlcNAc inhibited he binding of WGA to G. lamblia in both assays to a greater extent than did sialic acid. Binding of WGA was not altered by prior treatment of trophozoites with neuraminidase, suggesting that WGA was binding to GlcNAc moieties on G. lamblia and not to sialic acid. The remaining five lectins either bound nonspecifically or exhibited low percentages of binding. The apparent presence of GlcNAc but not sialic acid or other exposed surface carbohydrates may be important in the interaction of G. lamblia with its human host.

Agglutination↗
PubMed1993

[The sperm-agglutinating activity of the fractions of saline root extracts from Arum maculatum].

Our previous investigations have demonstrated that saline extract of Arum maculatum contains lectin (sperm agglutinin) which agglutinates human ejaculated spermatozoa of the type tail to tail and head to tail. By means of speed liquid chromatography (Mono S XP 5/5) eight fractions (I-VIII) were obtained. The sperm-agglutinating activity of the fractions was investigated against frog testicular spermatozoa and testicular and epididymal spermatozoa of man, rabbit, rat and mouse. The fractions did not agglutinate frog spermatozoa. Fraction I agglutinated rabbit, rat and murine spermatozoa; fraction II-rabbit and rat spermatozoa; fraction VII-only human spermatozoa, and fraction VIII-human, as well as animal spermatozoa. The fractions III, IV, V, VI had no sperm-agglutinating activity. These data could be explained by the assumption that the differences in the sperm-agglutinating activity of the fractions are due to isoforms (called also isolectins) of the phytospermagglutinin, contained in the saline extract of Arum maculatum.

Animals↗
PubMed1987

Interaction between Candida agglutinins and antifungal agents.

Antifungal agents alter the function and morphology of Candida cell membranes and cell walls. We observed that brief (30 minute) exposure to either amphotericin B or clotrimazole inhibited the agglutination of Candida blastoconidia by murine bronchoalveolar lavage fluid. This inhibition required continuous drug presence. Neither amphotericin nor clotrimazole inhibited Candida agglutination by concanavalin A or pooled human serum. These results demonstrate that antifungal drugs can produce rapid changes in the surface characteristics of some fungi.

Agglutination↗
PubMed1988

A galactose specific agglutinin from the hemolymph of the snail Achatina fulica: purification and characterization.

A galactose specific agglutinin has been detected in the hemolymph of the snail Achatina fulica fulica Bowdich. The agglutinin, which agglutinates rabbit erythrocytes, has been purified by affinity chromatography on crosslinked guargum followed by gel filtration on a Biogel P-200 column. The purified agglutinin has a native molecular weight of 210,000 and comprises of non covalently linked identical subunits of molecular weight 15,000. The pI of the agglutinin was found to be 8.1. The activity of the agglutinin is independent of divalent cations. The inhibition of hemagglutination data reveals that 2-deoxy-D-galactose is the most potent inhibitor of the agglutinin followed by galactose and lactose.

Animals↗
PubMed1981

Interaction with lectins and differential wheat germ agglutinin binding of pyocin 103-sensitive and -resistant Neisseria gonorrhoeae.

Strains of Neisseria gonorrhoeae were treated with pyocin 611 131 (pyocin 103) from Pseudomonas aeruginosa PA103, and isogenic resistant variants were isolated. The interaction of pyocin-sensitive and isogenic pyocin-resistant strains with wheat germ agglutinin (WGA) agglutinated all pyocin-sensitive, but not pyocin-resistant, strains. Binding of WGA to three pyocin-sensitive strains and their isogenic pyocin-resistant variants was examined quantitatively by using fluorescein-conjugated lectin. Pyocin-resistant strains maximally bound one-third to one-eighth the quantity of WGA bound by isogenic-sensitive strains. Linear Scatchard plots revealed homogeneous WGA-binding sites on three pyocin-sensitive and one pyocin-resistant strains. Biphasic Scatchard plots, obtained with two pyocin-resistant strains, show that WGA-binding sites in these strains are heterogeneous. The number of WGA-binding sites for pyocin-sensitive organisms ranged from 8 x 10(5) to 1 x 10(6) sites per coccus and from 1 x 10(5) to 3 x 10(5) sites per coccus for pyocin-resistant strains. The apparent association constant for WGA binding to pyocin-sensitive strains ranged from 3 x 10(6) to 6 x 10(6) liters/mol and from 6 x 10(6) to 1 x 10(7) liters/mol for pyocin-resistant strains. Gonococcal lipopolysaccharide was shown to serve as the pyocin 103 receptor by inhibition of pyocin activity. Lipopolysaccharide from a pyocin 103-resistant strain was not able to inhibit pyocin 103 activity. Pyocin 103 resistance was correlated with a structural alteration involving N-acetylglucosamine residues in gonococcal lipopolysaccharide. Based on interactions with wheat germ, soybean, and ricin lectins, a model of lipopolysaccharide structure in N. gonorrhoeae is presented.

Agglutination↗
PubMed1982

Enrichment for CFU-C from murine and human bone marrow using soybean agglutinin.

Mouse bone marrow and spleen cells agglutinated by soybean agglutinin (SBA) or peanut agglutinin (PNA) were previously shown to be enriched for spleen colony-forming cells (CFU-S) and sufficiently depleted of graft-versus-host reaction producing cells to allow hematologic reconstitution of lethally irradiated allogeneic recipient mice. A similar enrichment for cells capable of forming colonies in soft agar culture (CFU-C) has now been found in the SBA-agglutinated fraction of mouse bone marrow cells, in contrast to the finding that in human bone marrow the majority of the CFU-C are in the fraction not agglutinated by SBA. Cytofluorometric studies with fluorescein-labeled SBA (FITC-SBA) revealed that the majority of both mouse and human bone marrow cells bind the lectin. Experiments mixing the human marrow fractions separated by SBA reveal that true enrichment for CFU-C is achieved in the unagglutinated fraction, as opposed to a possible depletion of a suppressor cell population. Granulocytic, monocytic, and mixed cell colonies were all enriched in the SBA-unagglutinated cell fraction from human bone marrow.

Animals↗
PubMed1979

Characterization of yeast agglutinins in lavage fluid from lungs of rabbits.

Rabbits were challenged intratracheally with 10(8) Candida albicans or Torulopsis glabrata, and their lungs were lavaged 5, 60, and 120 min later. Initial lavage samples showed significant agglutination of yeasts, followed by the development of larger aggregates in association with alveolar macrophages. To investigate this early agglutination reaction, lungs of normal rabbits were lavaged with heparinized saline, and after alveolar macrophages were discarded, the cell-free lavage fluid was centrifuged at 25,000 g to recover a small, whitish, surface-active pellet (F fraction). The supernatant was concentrated 15-fold by vacuum dialysis (P fraction). When Candida species, T. glabrata, and Saccharomyces cerevisiae were incubated with the F fraction, serial colony counts decreased eight- to 20-fold with every yeast species tested except S. cerevisiae and Candida krusei. Decrease in colony counts was associated with yeast agglutination. The F fraction was further separated by ethanol-ether extraction, and yeast agglutination was seen only in the protein-rich fraction. Further separation of this protein-rich fraction by polyacrylamide gel electrophoresis yielded three bands, one of which, with a molecular size of about 10(4) daltons, agglutinated C. albicans. IgA in the P fraction also agglutinated C. albicans, although not as dramatically as the F fraction.

Agglutination↗
PubMed1985

Lectin binding to human gastric adenocarcinomas and adjacent tissues.

The binding of lectins to paraffin sections of nine gastric carcinomas and adjacent mucosa was examined by fluorescence microscopy. A battery of nine lectins was employed, and both intestinal and diffusely infiltrating tumors were tested. Wheat germ agglutinin and Ricinus communis agglutinin I appeared to bind to both mucus and nonmucus glycoproteins; these lectins labeled tumor cells, benign epithelial cells, and nonepithelial tissues strongly and consistently. Peanut agglutin, soybean agglutinin, Dolichos biflorus agglutinin, Bandeiraea simpifolica agglutinin, and Ulex europaeus agglutinin I bound extensively to mucosubstances in vacuoles and apices of benign epithelial cells but often bound to tumor cells focally and in some cases not at all. Neuraminidase digestion enhanced lectin staining in some tumors; but in others, especially those of the diffusely infiltrating type, neuraminidase digestion did not enhance the staining of tumor cells. The results suggest that the decrease in the proportion of tumor cells labeling with lectin relative to superficial epithelial cells can be due either to the oversialylation of mucoproteins or to the loss of glycosylating enzyme activity. Concanavalin A did not bind to mucosubstances in the vacuoles or apices of benign epithelium, but bound to mucus vacuoles of metaplastic epithelium and to coarse cytoplasmic granules in two of the tumors examined. This suggests either the abnormal addition of mannose to mucus glycoprotein or the production of a distinct glycoprotein by some gastric tumors.

Concanavalin A↗
PubMed1979

A method for specific detection of autoantibodies to the zona pellucida in infertile women.

Human antibodies to porcine erythrocytes were found to bind to porcine but not to human zonae pellucidae, whereas human isohemagglutinins bound to human but not to porcine zonae. On the basis of the binding behavior of agglutinins, it was found that the immunofluorescence of porcine zonae produced by selected sera from infertile women was due to an antibody of different specifity from that which agglutinated pig red blood cells. However, no serum component other than heteroagglutinin was contained in selected sera from control subjects which fluoresced porcine zonae. Since the component was present in the immunoglobulin G fraction, bound to human zonae, and was reactive with zona-specific antigen(s), it was judged an autoantibody to zonae. Thus a method for specific detection of autoantibodies to zonae has been developed by indirect membrane immunofluorescence using porcine ova as targets.

Absorption↗
PubMed2002

Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily.

Salivary agglutinin is encoded by DMBT1 and identical to gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties. This 300-400 kDa glycoprotein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR-interspersed domains (SIDs), 2 CUB (C1r/C1s Uegf Bmp1) domains, and a zona pellucida domain. We have searched for the peptide domains of agglutinin/DMBT1 responsible for bacteria binding. Digestion with endoproteinase Lys-C resulted in a protein fragment containing exclusively SRCR and SID domains that binds to S. mutans. To define more closely the S. mutans-binding domain, consensus-based peptides of the SRCR domains and SIDs were designed and synthesized. Only one of the SRCR peptides, designated SRCRP2, and none of the SID peptides bound to S. mutans. Strikingly, this peptide was also able to induce agglutination of S. mutans and a number of other bacteria. The repeated presence of this peptide in the native molecule endows agglutinin/DMBT1 with a general bacterial binding feature with a multivalent character. Moreover, our studies demonstrate for the first time that the polymorphic SRCR domains of salivary agglutinin/DMBT1 mediate ligand interactions.

Agglutination↗