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PubMed1980

The binding of lectins to sheep tissues and circulating cells: peanut agglutinin, a marker for presumptive T-lymphocytes.

A study was undertaken into the binding of 7 fluorescein (FITC)-labelled, lectins to sheep tissues and cells. Wheat germ agglutinin (WGA), conconavalin A (con A) and Ricinus communis agglutinin (RCA) bound strongly to all sheep tissues and circulating cells, while Dolichos biflorus (DBA) and Ulex europaeus (UEA) did not bind at all. Peanut agglutinin (PNA) and soybean agglutinin (SBA) bound to thymus and lymph node cell suspensions and to a proportion of circulating cells, but only weakly to the other sheep tissues tested. PNA and SBA bound to polymorphs and monocytes, making it necessary to treat whole blood with carbonyl-iron and magnet to remove the phagocytic cells before purfication of the peripheral blood leucocytes (PBL). PNA bound to 40 to 50% of carbonyl-iron treated PBL and to 65 to 70% of the cells in efferent popliteal lymph. Using a rhodamine-labelled anti-sheep lg reagent greater than 98% of PNA + cells in lymph and carbonyl-iron treated PBL were sIg-. Furthermore, using an FITC-labelled F(ab')2 anti-sheep Ig reagent, the sum of the 0/0 PNA+cells and sIg+ cells in individually labelled preparations was equal to the percentage of cells labelled when both reagents were added simultaneously. Cells binding PNA were found in more dense regions of buoyant density gradients and were less adherent to nylon wool than cells having surface immunoglobulin (sIg). Approximately 20 to 30% of PBL and 10 to 20% of the cells in lymph were PNA-/sIg- and these were termed 'null' cells. Although Con A induced sheep PBL to transform in tissue culture, PNA, SBA and WGA all failed to stimulate the incorporation of 3H-thymidine at the concentrations tested. Sorting lymph cells from BCG vaccinated sheep into PNA+ and PNA- subpopulations showed that the cells able to transform in vitro to the specific antigen, purified protein derivative (PPD) or the mitogen phytohemagglutinin (PHA) were in the PNA+ but not PNA- population.

Age Factors↗
PubMed1998

Evaluation of the stoichiometry and energetics of carbohydrate binding to Ricinus communis agglutinin: a calorimetric study.

High-sensitivity isothermal titration calorimetry has been used to investigate the thermodynamics of binding of Ricinus communis agglutinin to galactose, lactose and their derivatives in the temperature range 280.5-298 K. The present study unequivocally establishes the carbohydrate-binding stoichiometry of the tetrameric agglutinin from castor bean as two, i.e. the (As-sB)2-type tetramer of the agglutinin has two equivalent sites that are non-interacting and independent. The site binding constants range from 2.2x10(3) M-1 at 282 K for galactose to 4.84x10(4) M-1 at 281 K for N-acetyl-lactosamine. The binding enthalpies range from -21.9 kJ. mol-1 at 293 K for 4-methylumbelliferyl-beta-galactoside to -50.2 kJ. mol-1 at 292.9 K for thiodigalactoside. The observation of limited entropy-enthalpy compensation for binding of the sugars to the lectin indicates that reorganization of water molecules plays an important role in binding. As the slope of the compensation plot is greater than unity, the reactions are largely enthalpically driven. These studies show that the stronger binding of N-acetyl-lactosamine than lactose is due to a favourable interaction between the acetamido group of the reducing-end N-acetylglucosamine of the former and the corresponding loci in the agglutinin molecule. Preferential binding of methyl-beta-galactoside over methyl-alpha-galactoside also indicates the apolar nature of the interaction with the methyl group of the former sugar.

Calorimetry↗
PubMed1973

Transformation of neuraminidase-treated lymphocytes by soybean agglutinin.

Transformation of mouse-spleen lymphocytes in the presence of soybean agglutinin is markedly enhanced after their treatment with neuraminidase (EC 3.2.1.18). Incubation of the cells with the enzyme also facilitates their agglutination by the lectin. The soybean agglutinin-induced agglutination and transformation is inhibited specifically by N-acetyl-D-galactosamine. New specific binding sites for soybean agglutinin were shown to appear after neuraminidase treatment. It is postulated that the transformation of neuraminidase-treated mouse-spleen lymphocytes induced by soybean agglutinin is caused by the binding of the lectin to galactosyl residues exposed by the action of neuraminidase on the cell membrane.

Animals↗
PubMed1978

Ligands containing heavy atoms: perturbation of phosphorescence of a tryptophan residue in the binding site of wheat germ agglutinin.

Information on the structure of binding sites of wheat germ agglutinin was obtained on the basis of fluorescence and phosphorescence changes of tryptophan residues induced by the binding of several thiomercuribenzoate derivatives of glycosides. The thiomercuribenzoate derivatives bind selectively to wheat germ agglutinin in the same way as the corresponding sugars. Using the thiomercuribenzoate of di-N-acetyl-beta-chitobiose, it was found that: (i) the fluorescence of tryptophan residues was drastically quenched at both 298 and 77 K; (ii) the phosphorescence intensity was strongly enhanced at 77 K; (iii) the phosphorescence lifetime was markedly decreased. A similar effect was observed with the thiomercuribenzoate of N-acetyl-beta-D-glucosamine. These changes were completely reversed upon addition of 1-O-methyl-di-N-acetyl-beta-chitobioside. The thiomercuribenzoate of beta-D-glucose had no effect at all, and the thiomercuribenzoate of tri-N-acetyl-beta-chitotriose had a limited effect. These results are interpreted as a specific heavy atom effect due to a close contact between one tryptophan residue of the protein and the heavy atom of the bound ligand. They are consistent with the view that: (i) binding sites of wheat germ agglutinin may be divided in three subsites, A, B, and C; (ii) a tryptophan residue is in the binding site at subsite C; and (iii) this residue and the ligand are in close contact. This new method, using the enhancement of spin-orbit coupling due to the selective perturbation induced in a tryptophan residue by a ligand containing a heavy atom, has proved to be suitable for locating the tryptophan residue in the binding site of wheat germ agglutinin and can probably be extended to other sugar-binding proteins.

Binding Sites↗
PubMed1983

Differential agglutination by soybean agglutinin of human leukemia and neuroblastoma cell lines: potential application to autologous bone marrow transplantation.

Normal human bone marrow cells were mixed with radioactively labeled tumor cells from different leukemia and neuroblastoma cell lines, and the cell mixtures were separated by differential agglutination with soybean agglutinin. It is shown that the cell fraction unagglutinated by soybean agglutinin, which was previously found to be capable of reconstituting the hematopoietic system of lethally irradiated recipients, can be purged of tumor cells with varying efficiency depending on the tumor cell expression of soybean agglutinin receptors as detected by flow cytofluorimetry with fluoresceinated soybean agglutinin.

Animals↗
PubMed1987

Isolation and characterization of a cDNA clone encoding wheat germ agglutinin.

Two sets of synthetic oligonucleotides coding for amino acids in the amino- and carboxyl-terminal portions of wheat germ agglutinin were synthesized and used as hybridization probes to screen cDNA libraries derived from developing embryos of tetraploid wheat. The nucleotide sequence for a cDNA clone recovered from the cDNA library was determined by dideoxynucleotide chain-termination sequencing in vector M13. The amino acid sequence deduced from the DNA sequence indicated that this cDNA clone (pNVR1) encodes isolectin 3 of wheat germ agglutinin. Comparison of the deduced amino acid sequence of clone pNVR1 with published sequences indicates isolectin 3 differs from isolectins 1 and 2 by 10 and 8 amino acid changes, respectively. In addition, the protein encoded by pNVR1 extends 15 amino acids beyond the carboxyl terminus of the published amino acid sequence for isolectins 1 and 2 and includes a potential site for N-linked glycosylation. Utilizing the insert of pNVR1 as a hybridization probe, we have demonstrated that the expression of genes for wheat germ agglutinin is modulated by exogenous abscisic acid. Striking homology is observed between wheat germ agglutinin and chitinase, both of which are proteins that bind chitin.

Journal Article↗
PubMed2000

Cold agglutinin disease in a patient with uterine sarcoma.

Cold agglutinin disease is a rare clinical scenario. It is usually associated with infection, drug reaction, and hematologic malignancy, such as non-Hodgkin lymphoma or lymphocytic leukemia. We report a case of cold agglutinin disease in a patient with solid-tumor uterine sarcoma. Immunological dysregulation has been proposed as the pathogenesis for this disease. We also summarize recently reported cases of cold agglutinin disease, the underlying conditions, and advances in the management of cold agglutinin disease.

Adrenal Cortex Hormones↗
PubMed1980

A New Bacterial Agglutinin from Soybean: I. ISOLATION, PARTIAL PURIFICATION, AND CHARACTERIZATION.

A new bacterial agglutinin was isolated from seeds of the soybean cultivar Clark. Purification was carried out by ammonium sulfate precipitation and ion-exchange chromatography. The agglutinin is a heat-labile glycoprotein most active at pH 4.0. Addition of Ca(2+), Mn(2+) and Mg(2+) did not enhance the agglutinating activity of this glycoprotein. Gel electrophoresis in the presence of sodium dodecyl sulfate showed that the agglutinin is composed of two subunits of approximately 50,000 daltons each. In the undissociated state, it agglutinates Xanthomonas phaseoli var. sojensis, the causal agent of bacterial pustule disease of soybean, at concentrations as low as 10 micrograms protein per milliliter but has no hemagglutinating activity. The agglutinin could be distinguished from previously reported soybean lectins on the basis of solubility in ammonium sulfate, lack of hemagglutinating activity, molecular weight, hapten specificity, and immunological determinants.

Journal Article↗
PubMed1982

Occurrence and characterization of lympho-agglutinins in Indian plants.

A survey of the occurrence of lympho-agglutinins was carried out on seeds of 150 species of wild and cultivated plants. Potent agglutinins were detected in 17 extracts by employing lymphocytes of man, guinea pig, goat and sheep in the bioassay. Except for one species each of Mimosoideae, Euphorbiaceae and Clusiaceae, all the agglutinins were found in fabaceous seeds. Two of the agglutinins, namely, Parkia biglandulosa and Erythrina arborescens, were found to be monospecific for guinea pig and human lymphocytes, respectively, while the others agglutinated lymphocytes of 2-4 different species. The agglutination inhibition tests revealed the predominance of galactose (or its derivatives) binding lectins over those specific for glucose-mannose series.

Acetylgalactosamine↗
PubMed1975

Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers.

Wheat germ agglutinin was found to agglutinate cells of Escherichia coli PAT 84, Micrococcus luteus, Staphylococcus aureus H, and of S. aureus 52A5, but not cells of S. aureus 52A2. Interaction of wheat germ agglutinin with a soluble linear peptidoglycan secreted by Micrococcus luteus and with the teichoic acid of S. aureus H was demonstrated by agar gel diffusion, quantitative precipitation and inhibition of hemagglutination of trypsinized rabbit erythrocytes. No interaction could be demonstrated with the teichoic acid from a phage-resistant mutant (S. aureus 52A2) which lacks A-acetyl-D-glucosamine residues. All interactions were specifically inhibited by low concentrations of chitotriose (GlcNAcbeta1 leads to 4GlcNAcbeta1 leads to 4GlcNAc) and the bacterial cell wall tetrasaccharide, GlcNAcbeta1 leads to 4MurNAcbeta1 leads to 4GlcNAcbeta1 leads to 4MurNAc. Hemagglutination-inhibition experiments showed that the linear peptidoglycan and the teichoic acid of S. aureus H were several thousand times more potent inhibitors of wheat germ agglutinin than was N-acetyl-D-glucosamine. Comparison of the efficiency of different saccharides in inhibition of hemagglutination and precipitation of polymers by wheat germ agglutinin, strongly suggests that secondary, non-specific interactions contribute to the binding of the lectin to the polymers.

Agglutination Tests↗
PubMed1966

Light-chain heterogeneity of cold agglutinins.

Cold agglutinins with specificity to I or to i antigens of humanadult or cord-blood erythrocytes produced during the course of Mycoplasma pneumoniae infection and infectious mononucleosis contain light chains of K and L types. However, cold agglutinin isolated from the serums of patients with chronic cold-agglutinin hemolytic anemia contains only type K light chains. The experimental evidence suggests that some cold agglutinins contain both types of light chains in the same molecule.

Anemia, Hemolytic↗
PubMed1985

Trypanolytic activity, agglutinins, and opsonins in sera from animals refractory to Trypanosoma lewisi.

An examination of sera from a range of animals refractory to Trypanosoma lewisi showed that some contain trypanolytic activity and agglutinins for this trypanosome. Trypanolytic activity was demonstrated in bovine, sheep, and rabbit serum. These sera were shown to also contain agglutinins. The trypanolytic activity in all three sera was abolished by heat inactivation at 56 degrees C for 30 min. Studies with bovine serum showed that the lytic activity was totally inhibited by the addition of EDTA but was only partially inhibited by ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid-Mg2+, suggesting the involvement of both classical and alternate pathways of complement activation. Serum from the natural host, the rat but not mouse serum, was capable of inhibiting the trypanolytic activity of bovine serum. The agglutinins in bovine serum were specific, since they could be adsorbed out with T. lewisi but not T. musculi. They fractionated on gel filtration in the position expected for 19S antibodies. By using opsonization measuring techniques, it was found that mouse serum lacked opsonins to T. lewisi, although opsonic activity was detectable in human serum. The absence of agglutinins, trypanolysins, and opsonins in mouse serum suggests that other factors prevent the infection of mice by T. lewisi. From these findings, it would appear that the inability of T. lewisi to infect a range of mammals, with the exception of mice, could be due to the presence of antibodies, the ability to activate complement through the alternative pathway, or both. The absence of these recognition factors and the ability to evade the effects of alternative pathway activation may be important factors in the ability of this parasite to establish infections in rats.

Animals↗
PubMed1986

Identification of two new hemagglutinins of Escherichia coli, N-acetyl-D-glucosamine-specific fimbriae and a blood group M-specific agglutinin, by cloning the corresponding genes in Escherichia coli K-12.

Genes encoding the Escherichia coli IH11165 hemagglutinins with specificity for terminal N-acetyl-D-glucosamine and blood group M antigen, respectively, were cloned by a cosmid cloning procedure. A 22-kilobase-pair subclone expressed both hemagglutination specificities in the nonhemagglutinating E. coli HB101 recipient strain. Derivatives obtained by insertion and deletion mutagenesis expressed either one of the two hemagglutination specificities. Both agglutinins were purified; the agglutinin recognizing terminal N-acetyl-D-glucosamine was associated with a new type of fimbria (G fimbria) with an apparent subunit molecular mass of 19.5 kilodaltons, whereas the blood group M agglutinin (M agglutinin) was nonfimbrial and had an apparent subunit mass of 21 kilodaltons.

Acetylglucosamine↗
PubMed1980

Role of lipopolysaccharide in wheat germ agglutinin-mediated agglutination of Neisseria meningitidis and Neisseria gonorrhoeae.

Wheat germ agglutinin, having specificity for N-acetyl glucosamine, agglutinated known nonencapsulated Neisseria meningtidis strains, but failed to agglutinate encapsulated strains of all serogroups tested Presence of a capsule, therefore, blocked wheat germ agglutinin agglutination of N. meningitidis strains. In contrast, Neisseria gonorrhoeae strains were strongly agglutinated, providing additional evidence for nonencapsulation of N. meningitidis strains. In contrast, Neisseria gonorrhoeae strains were strongly agglutinated, providing additional evidence for nonencapsulation of N. gonorrhoeae. Purified lipopolysaccharide from a single N. meningitidis and N. gonorrhoeae strains tested. Thus, in absence of capsular polysaccharide wheat germ agglutinin agglutinates Niesseria strains through interaction with lipoplysaccharide in the outer membrane. Of 34 nongroupable throat N. meningitidis isolates, 10 failed to agglutinate in wheat germ agglutinin, suggesing that at least some nongroupable. N. meningitidis strains may possess capsule-like materials.

Agglutination↗
PubMed1989

Comparison of hemagglutinin and agglutinin schemes for the serological classification of Haemophilus paragallinarum and proposal of a new hemagglutinin serovar.

Ninety-five isolates of Haemophilus paragallinarum were classified serologically by a hemagglutinin serotyping scheme, and the results were compared with results from agglutinin serotyping of the same isolates. Of the isolates, 65 were from Australia, 5 were from Japan, 6 were from the Federal Republic of Germany, 7 were from the United States, and 12 were from South Africa. Seven hemagglutinin serovars, HA-1 to HA-7, corresponding to agglutinin serovars A (HA-1, HA-2, and HA-3), C (HA-4, HA-5, and HA-6), and B (HA-7) have been described. Only one of the seven hemagglutinin serovars was found among the Australian isolates. This was serovar HA-5, comprising 49 isolates. Fifteen Australian isolates, all from southeast Queensland and northern New South Wales, were found to belong to a new hemagglutinin serovar. This was designated HA-8 and represented a fourth subgroup of agglutinin serovar A. Of the 95 isolates examined, only 1 did not produce a hemagglutinating antigen and was nonserotypeable by the hemagglutinin system. This compared favorably with the agglutinin scheme, which serotyped only 60 of the 95 isolates, with 29 nonserotypeable and 6 autoagglutinating.

Agglutination Tests↗
PubMed1999

Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells.

BACKGROUND: Dietary lectins can alter the proliferation of colonic cells. Differentiation is regulated by adhesion molecules which, being glycosylated, are targets for lectin binding. AIMS: To examine the effects of dietary lectins on differentiation, adhesion, and proliferation of colorectal cancer cells. METHODS: Differentiation was assessed in three dimensional gels, adhesion by aggregation assay, and proliferation by 3H thymidine incorporation. The role of the epithelial cell adhesion molecule (epCAM) was studied using a specific monoclonal antibody in blocking studies and Western blots. The human colon cancer cell lines LS174T, SW1222, and HT29 were studied. RESULTS: The cell line LS174T differentiated in the presence of Vicia faba agglutinin (VFA) into gland like structures. This was inhibited by anti-epCAM monoclonal antibody. Expression of epCAM itself was unaffected. VFA as well as wheat germ agglutinin (WGA) and the edible mushroom lectin (Agaricus bisporus lectin, ABL) significantly aggregated LS174T cells but peanut agglutinin (PNA) and soybean agglutinin (SBA) did not. All lectins aggregated SW1222 and HT29 cells. Aggregation was blocked by the corresponding sugars. Aggregation of cells by VFA was also inhibited by anti-epCAM. VFA, ABL, and WGL inhibited proliferation of all the cell lines; PNA stimulated proliferation of HT29 and SW1222 cells. In competition studies all sugars blocked aggregation and proliferation of all cell lines, except that the addition of mannose alone inhibited proliferation. CONCLUSION: VFA stimulated an undifferentiated colon cancer cell line to differentiate into gland like structures. The adhesion molecule epCAM is involved in this. Dietary or therapeutic VFA may slow progression of colon cancer.

Adenocarcinoma↗
PubMed1987

Histochemical reactivity of soybean agglutinin with blood group antigens and their precursor substances in acinar cells of human pancreas.

In human pancreas, soybean agglutinin (SBA) conjugated to horseradish peroxidase reacted with the acinar cells secreting blood group A and/or H antigen, but not with those secreting only B antigen. For detailed histochemical characterization of SBA staining, the effects of treatment with unlabeled lectins and of digestion of certain enzymes on SBA staining were investigated in formalin-fixed, paraffin-embedded pancreatic tissue from individuals of different blood groups. Pre-incubation of sections with unlabeled Dolichos biflorus agglutinin to block A antigen eliminated subsequent SBA staining in the cells secreting A antigen, although failing to induce any effects in those secreting H antigen. In contrast, pre-incubation with unlabeled Ulex europaeus agglutinin-I (UEA-I) to block H antigen abolished SBA staining in cells secreting H antigen but not in those secreting A antigen. Treatment with galactose oxidase yielded the same results as those with unlabeled UEA-I, i.e., SBA reactivity was significantly diminished in cells secreting H antigen but not in those secreting A antigen. Digestion with beta-galactosidase resulted in a slight decrease of SBA staining in the cells secreting H antigen. Accompanying the decrease of SBA staining, reactivity with Griffonia simplicifolia agglutinin-II (GSA-II) appeared for the first time in the enzyme-susceptible, SBA-reactive cells secreting H antigen. Pre-treatment with galactose oxidase abolished this effect of beta-galactosidase. The GSA-II reactivity disclosed by treatment with galactosidase was completely eliminated by digestion with beta-N-acetylhexosaminidase, indicating that GSA-II staining after digestion with galactosidase is due to exposed penultimate beta-N-acetyl-D-glucosamine residues. These results demonstrate that at least two substances react with SBA in acinar cells of human pancreas, one being terminal beta-N-acetyl-D-galactosamine residues of A antigen, and the other being terminal beta-D-galactose-(1----3 or 1----4)-beta-N-acetyl-D-glucosamine dimers in the precursor of blood group H antigen. Such dimers may exist in close proximity to L-fucose residues of H antigen, since unlabeled UEA-I blocked SBA staining.

ABO Blood-Group System↗
PubMed2006

Development of mixed-type autoimmune hemolytic anemia and Evans' syndrome following chicken pox infection in a case of low-titer cold agglutinin disease.

We describe a patient with low-titer cold agglutinin disease (CAD) who developed mixed-type autoimmune hemolytic anemia (AIHA) and idiopathic thrombocytopenia following chicken pox infection. At least 1 year before admission to hospital, the patient had mild hemolytic anemia associated with low-titer cold agglutinins. A severe hemolytic crisis and thrombocytopenia (Evans' syndrome) occurred several days after infection with chicken pox, and the patient was referred to our hospital. Serological findings revealed the presence of both cold agglutinins and warm-reactive autoantibodies against erythrocytes, and the diagnosis was mixed-type AIHA. Following steroid therapy, the hemoglobin (Hb) level and platelet count improved. The patient was closely followed over a 10-year period with recurrent documented hemolysis after viral or bacterial infections. Warm-reactive autoantibodies have not been detected in the last 2 years, and only the immunoglobulin M anti-I cold agglutinins with a low titer and wide thermal amplitude have remained unchanged. Therefore, the patient has received at least 10 mg prednisolone daily to maintain a Hb level of 10 g/dL. To the best of our knowledge, no adult case of low-titer CAD that has evolved into mixed-type AIHA and Evans' syndrome after chicken pox infection has been previously reported in the literature.

Anemia, Hemolytic, Autoimmune↗