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PubMed1994

Interactions with lectins and agglutination profiles of clinical, food, and environmental isolates of Listeria.

On the basis of preliminary trials with 14 collection strains of Listeria, five lectins (Canavalia ensiformis, concanavalin A; Griffonia simplicifolia lectin I; Helix pomatia agglutinin; Ricinus communis agglutinin; and Triticum vulgaris wheat germ agglutinin) were selected to set up a microtiter agglutination assay. The lectin agglutination profiles of 174 clinical, food, and environmental strains of Listeria monocytogenes, Listeria innocua, and Listeria seeligeri were investigated. Data on the standard determination of the antigenic structure were available for clinical strains; nonclinical isolates were assigned to serogroup 1 or 4 with commercial antisera. The listeria-lectin interaction was related to serological type rather than species; in particular, the strains assigned to serogroup 1 or belonging to serovars 1/2a, 1/2b, 1/2c, 3a, 3b, and 7 were never agglutinated by G. simplicifolia lectin I. The five-lectin set proved to be capable of detecting differences between serologically identical isolates of L. monocytogenes. Of the 150 isolates of this species, 144 were distributed over 15 different lectin agglutination profiles and 6 autoagglutinated, the overall typeability being 96%. However, the profiles encountered among L. monocytogenes isolates were not randomly distributed. With strains assigned to serogroup 1 or belonging to serovars 1/2a, 1/2b, 1/2c, and 3b, the clinical isolates fell into only two of the eight patterns recorded overall; with strains of serogroup 4 and serovar 4b, food and environmental isolates were distributed over eight of the nine patterns found in total, while clinical isolates were distributed over five patterns. In a comparative study of 15 epidemiologically relevant isolates of L. monocytogenes from five distinct outbreaks, strains with identical phage types and/or DNA fingerprints displayed identical lectin profiles. The heterogeneity of agglutination profiles may form the basis of a new approach to L. monocytogenes typing.

Agglutination↗
PubMed1988

Benefit of a 37 degree C extracorporeal circuit in plasma exchange therapy for selected cases with cold agglutinin disease.

Plasmapheresis is commonly advocated in cold agglutinin disease with life-threatening hemolysis. Some clinicians, however, are reluctant to use this therapy because of perceived technical problems and risks attendant with the temperature of the extracorporeal circulation. In this study we report our experience of two patients with severe life-threatening hemolysis and in whom plasma exchange was not feasible due to red blood cell autoagglutination in the extracorporeal circuit. A method is described involving the use of blood warmers and the Fenwal CS-3000 blood cell separator with its 37 degrees C centrifuge compartment. The use of plasma exchange in this manner is a safe and beneficial form of adjunctive therapy and should be considered for patients with cold agglutinin disease at risk for extracorporeal agglutination or hemolysis.

Adolescent↗
PubMed1983

A latex agglutination test for lectin binding.

Blood group A + H substance purified from hog gastric mucin was fixed to polystyrene particles by physical absorption to produce a lectin-agglutinable latex. Agglutination of this latex by soybean agglutinin, concanavalin A, and wheat germ agglutinin is specifically inhibited by the respective monosaccharide haptens and is not affected by known noninhibitory sugars. The sensitivity of the assay, a function of particle loading and latex concentration, approaches that of the hemagglutination test. NaCl, NaHCO3, NH4CO3, NH4-acetate, and Tris-HCl up to a concentration of 1 M do not interfere with the test. The latex suspension is stable for several months and can be stored in freeze-dried form.

ABO Blood-Group System↗
PubMed1970

Preparation and characterization of the plasma membrane of pig lymphocytes.

Lymphocyte plasma membrane was isolated from minced pig mesenteric lymph node by differential centrifugation and by centrifuging through a sucrose density gradient. The yield of membrane was approx. 0.1% (dry wt. relative to wet wt. of lymph node). The purified material had a sucrose density of 1.14g/cm(3) and consisted mainly of smooth vesicles. The membrane fraction contained, apart from protein and lipid, 59mug of carbohydrate, 11mug of sialic acid and 28mug of RNA/mg of protein; no DNA was detected. The cholesterol/phospholipid molar ratio was 1.01. Specific activities (mumol of product/h per mg of protein) of 5'-nucleotidase, succinate dehydrogenase, acid phosphatase and glucose 6-phosphatase were 10.1, 0, 0.51 and 0.30 respectively. The membrane vesicles were aggregated by an antiserum against pig lymphocytes and adsorbed the agglutinins to whole lymphocytes present in the antiserum; the membrane fraction was 28 times as effective as whole cells (on a dry wt. basis) in removing the lympho-agglutinins. Antisera against the membrane fraction agglutinated whole lymphocytes. It is concluded that the preparation represents the plasma membrane of small lymphocytes. The plasma membrane of pig thymocytes was isolated by using the same procedure. Its properties were similar to those of the lymphocyte plasma membrane.

Acid Phosphatase↗
PubMed1981

Lectins activate lymphocyte pyruvate dehydrogenase by a mechanism sensitive to protease inhibitors.

The mitogenic lectins concanavalin A and phytohemagglutinin were found to stimulate pyruvate oxidation in rat mesenteric lymphocytes. Marked cell agglutination accompanied this response. Wheat germ agglutinin, a nonmitogenic lectin, also aggregated lymphocytes but did not cause alteration of pyruvate oxidation. Cell lysates from lectin-treated cells retained their ability to oxidize pyruvate at an elevated rate, indicating that the observed stimulation of pyruvate oxidation was not due to increased transport of labeled pyruvate into the cells. Pyruvate oxidation activity in such lysates was readily sedimented in a mitochondria-enriched cellular fraction, indicating that it reflects mitochondrial pyruvate dehydrogenase. Stimulation of this activity by lectins in intact lymphocytes was inhibited when the cells were incubated under conditions expected to inhibit trypsin-like proteases. Thus, esters of arginine, but not of alanine or tyrosine, blocked stimulation of pyruvate dehydrogenase by the lectins. The data indicate that pyruvate dehydrogenase is activated in lymphocytes treated with mitogenic lectins by a mechanism involving one or more proteolytic reactions. The similarity between the results presented here and those recently reported for insulin action on its target cells [Seals, J. R. & Czech, M. P. (1980) J. Biol. Chem. 255, 6529-6531] suggests that these systems may have similar modes of transmembrane signalling.

Animals↗
PubMed1981

Characterization of populations of promastigotes of Leishmania donovani.

Promastigotes of Leishmania donovani cultured for either 3 or 10 days in vitro and inoculated intracardially into golden hamsters with an equal number of organisms from either population showed a 7-fold difference in infectivity when compared at both 10 and 16 days post-infection. Reproducible histochemical staining for the promastigote enzymes glucose-6-phosphate dehydrogenase (G6PDH) and peptidase after polyacrylamide gel electrophoresis showed two isoelectric variants of G6PDH (Bands 1 and 2) that displayed a 45% decrease (Band 1) and a 60% increase (Band 2) in total activity when 3- and 10-day-old promastigotes were compared. Peptidase activity, present in a single band, increased 7-fold in 10-day-old promastigotes. A decrease in the lectin-induced agglutination of promastigotes by castor bean agglutinin (RCA60), specific for D-galactose and N-acetyl-D-galactosamine, was seen when 3- and 10-day-old promastigotes are compared. Antisera raised against sonicated 10-day-old promastigotes showed a unique precipitin band between the antiserum and sonicated 10-day-old promastigotes not found between the antiserum and sonicated 3-day-old promastigotes.

Acetylgalactosamine↗
PubMed1997

Inhibitory effects of nucleoside 5'-alkylphosphates on sexual agglutination in Saccharomyces cerevisiae.

Among various nucleoside 5'-alkylphosphates, uridine 5'-hexadecylphosphate (UMPC16) and adenosine 5'-hexadecylphosphate (AMPC16) inhibited the sexual agglutination between a and alpha haploid cells of Saccharomyces cerevisiae. The effect of AMPC16 accompanied severe growth inhibition of the yeast cells but it was not observed with UMPC16. Sexual agglutination was not inhibited by the presence of UMPC16 or AMPC16 when the yeast cells had been pretreated with the mating pheromone. UMPC16 was characterized as a specific inhibitor of sexual agglutination without direct influence on the agglutinin function, being distinguishable from any of those ever known.

Adenine Nucleotides↗
PubMed1977

Incidence of leptospirosis in the detroit rat population.

The rat population (Rattus norvegicus) in the city of Detroit was surveyed to determine the incidence of leptospirosis. Four methods of survey were used--serological, direct examination of urine, culture of urine, kidney and brain, and histopathological examination. Of 358 sera tested by the microscopic-agglutination test, 277 (77.4%) had significant agglutinins for serotype icterohaemorrhagiae. Significant differences were found between adult and young animals in both incidence and antibody titers, titers of 1:50 or higher being present in 90.3% and 38.8%, respectively, of adult and young rats. Examination of freshly drawn urine by dark field microscopy revealed that 59.6% of the animals were shedding leptospirae. When stained with Steiner's silver stain, 91.9% of the kidney sections were positive for leptospirae, showing this to be the most sensitive test of those used. Leptospirae were isolated from one or more cultures of kidney, urine, or brain from 221 (59.2%) of the 358 rats examined.

Animals↗
PubMed1989

Purification of the inducible alpha-agglutinin of S. cerevisiae and molecular cloning of the gene.

The alpha-agglutinin responsible for mating type-specific agglutination of S. cerevisiae alpha-cells has been purified to homogeneity. The glycoprotein released from the cell surface under mild conditions has a relative molecular mass of 200 to 300 kDa as determined by SDS-gel electrophoresis. The protein moiety corresponds to 68.2 kDa. With an oligonucleotide corresponding to the N-terminal amino acid sequence, the alpha-agglutinin gene has been cloned and sequenced. From the DNA sequence, a protein of 631 amino acids with 12 potential N-glycosylation sites is predicted. The carboxy terminal one-third of the protein is not required for agglutination activity.

Agglutination↗
PubMed1957

Physical properties of the red cell agglutinins in acquired hemolytic anemia.

The sera of 8 patients with acquired hemolytic anemia associated with elevated levels of cold agglutinins were studied by various procedures of zone electrophoresis. The agglutinating activity was found associated with proteins of variable mobility in the different cases. The majority represented "fast" gamma-globulins. The 4 sera with the highest titers of cold agglutinins showed distinguishable abnormal electrophoretic components. The titers correlated with the height of the abnormal components. Ultracentrifugal analysis of the electrophoretic fractions indicated that the cold agglutinins were associated with proteins having a sedimentation coefficient of approximately 19 S. The abnormal component from the serum with the highest biological activity showed almost no contamination with lower molecular weight proteins. The amount of 19 S material found correlated with the titer of agglutinating activity. The high molecular weight character of the cold agglutinins was confirmed by procedures of density gradient zone centrifugation. The biological activity sedimented with proteins of the 19 S class in all the sera including those of relatively low titer with which no abnormal electrophoretic components were observed. Dissociation of the abnormal high molecular weight components was possible by means of certain sulfhydryl compounds. This resulted in disappearance of cold agglutinin activity. Some of the cases could be classified as macroglobulinemias because of the very large content of high molecular weight components. However, the same disease picture occurred without recognizable elevation of these components. The sera of 3 patients with severe acquired hemolytic anemia of the warm type associated with warm incomplete antibodies failed to show similar abnormal electrophoretic components and the antibody activity sedimented with proteins of the 7 S class.

Agglutinins↗
PubMedDate not supplied

Occurrence of granulocyte cytotoxins and agglutinins.

Granulocyte cytotoxic activity in sera from over 257 patients was shown to be distinct from HL-A lymphocytoxic activity. Granulocyte cytotoxins occur in approximately 25 per cent of sera from patients having leukemia, 45 per cent with aplastic anemia, 22 per cent with kidney disease on hemodialysis, and 19 per cent of pregnant women. By testing sera on the same panel of cells, the granulocyte cytotoxic activity was shown not to be associated with granulocyte agglutination activity or lymphocytotoxic acitivty. It is likely that granulocyte cytotoxins and granulocyte agglutinins will be useful in transfusion and bone marrow transplantation as a separate tool from the more widely used lymphocyte cytotoxicity reaction.

Agglutination Tests↗
PubMed2000

Biochemical characterization of sialoprotein "anti-agglutinin" purified from boar epididymal and seminal plasma.

Sialoprotein "anti-agglutinin," previously shown to inhibit sperm head-to-head agglutination, is found in both boar epididymal and seminal plasma. The present report characterizes anti-agglutinin by mass spectrometry, by N-terminal amino acid sequence analysis, and by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and Western blotting techniques to assess phosphate content of the molecule. Anti-agglutinin had the SDS-PAGE mobility of approximately 25 kDa. By electrospray ionization-mass spectrometry, however, mass spectra of anti-agglutinin were characterized by two major peaks (19,379-19,382 Da and 19,395-19,397 Da) and several minor peaks. Mass spectrometry of tryptic peptide fragments of deglycosylated anti-agglutinin and amino acid sequence analysis revealed that the protein has a unique peptide-mass fingerprinting of fragments (12,668 Da, 5,209 Da, 1,226 Da, and 1,168 Da) and a novel N-terminal amino acid sequence (KTDDY AISGA KEEEF YDYME ELYAV), respectively. Additionally Western blot techniques, using commercially available monoclonal antibodies, were used to detect presence of phosphothreonine and phosphoserine substituents, but two different monoclonal antibodies did not detect phosphotyrosine. Moreover, treatment with two different alkaline phosphotases converted the molecule, as assessed by SDS-PAGE and detection by silver stain, from the parent form of about 25 kDa to forms of approximately 19 kDa (similar to that assigned by mass spectrometry) and/or 15 kDa. Original antiserum generated toward, and reacting with native anti-agglutinin, reacted only with 19 kDa form. These results are consistent with the conclusion that the native anti-agglutinin may be a novel protein that is phosphorylated at serine and/or threonine residues.

Agglutinins↗
PubMed1983

A comparative study of different Leishmania tropica isolates from Iran: correlation between infectivity and cytochemical properties.

Five isolates of Leishmania tropica from southwest Iran were studied to identify correlates among human disease, animal infectivity, and surface biochemistry. Clinical patterns of the disease in humans differed. One striking strain, LT-249, produced a small dry lesion which did not heal during four years of observation. Infectivity of these L. tropica for mice was correlated with lectin agglutination patterns and interaction with macrophages. There was also a significant difference among the five isolates regarding infectivity for BALB/c mice; isolate LT-249 was not infective whereas all the others were. All isolates agglutinated with Concanavalin A (Con A), Ricinus communis and soybean agglutinin but not with four other lectins listed. However, Leishmania isolate LT-249 showed much poorer agglutination with all lectins than did the other four isolates. Two isolates were selected for detailed study of attachment to macrophages, one, LT-249, which was not infective and one, LT-252, which was infective for BALB/c mice. The number of promastigotes which attached to macrophages in vitro was the same, but the mechanism of attachment differed since only the LT-252 bound predominantly by Con A-mannose receptor interaction. These results indicate a correlation among animal infectivity, lectin agglutination, and promastigote-macrophage attachment. In particular one isolate of L. tropica which caused prolonged infection in humans was not infective in BALB/c mice, showed poor agglutination with lectins, and bound to macrophages by a different mechanism than did other isolates from the same region.

Agglutination↗
PubMed1986

Culturing and extraction of Coprococcus comes, absorption of serumagglutinins by soluble fractions and relation between agglutinins and antibodies in sera of patients with Crohn's disease.

Agglutinating antibodies to Coprococcus comes and three other obligately anaerobic coccoid rods from the intestinal flora are used in the diagnosis of Crohn's disease. Further studies on the pathogenetic role as well as the development of more sensitive and specific methods for detecting antibodies require extraction of the antigen fractions. Culturing methods to obtain C. comes with optimal antigen presentation and isolation of soluble antigen fractions were therefore developed. Hot water extraction of whole cells and subsequent removal of proteins with trichloroacetic acid provided a fraction that absorbed serum agglutinins, was useful for an enzyme-linked immunosorbent assay and induced agglutinating antibodies in rats.

Agglutination Tests↗