Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “AGGLUTININS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 199 records · Page 11Linked to original sources
PubMed1981

An evaluation of the specificity of salivary agglutinins.

Four bacterial strains collected from tooth surface, oral buccal mucosa, skin of the upper lip, and rectum were used to evaluate the specificity of salivary agglutinins. A saliva sample was absorbed with each of the strains, and the remaining supernatants were tested for agglutinin activity against all strains. The effect of concanavalin A and pH on the S. mutans and S. mitior agglutinins was studied. The conclusion was drawn that the agglutinins for the S. mutans and S. mitior strains differed but that the S. mitior strain rested carried a receptor site for the S. mutans agglutinin without becoming agglutinated. The S. mutans agglutinin seems to have either unsubstituted mannopyranosyl or N-acetylated glucopyranosyl residues as structural components.

Agglutinins↗
PubMed1982

Comparison fo agglutinin titers for Streptococcus mutans in tears, saliva, and serum.

The agglutinin titers for three Streptococcus mutans serotypes (AHT, BHT, and 10449, representing serotypes a, b, and c, respectively) were measured in the saliva, tears, and serum of 19 human subjects. Naturally occurring S. mutans agglutinins were routinely present in all fluids tested in the absence of overt local stimulation by antigen. The immunoglobulin A nature of this secretory agglutinin activity was suggested by blocking with alpha heavy-chain-specific antiserum and by the demonstration of S. mutans-reactive immunoglobulin A in the saliva and tears by indirect immunofluorescence. This finding is consistent with stimulation and antigen commitment of immunoglobulin A precursor lymphocytes at remote sites and subsequent homing to the lacrimal system. The relationship of anti-AHT agglutinins to anti-10449 agglutinins differed among the body fluids tested. The tears had more agglutinins for strain AHT than for strain 10449, whereas the reverse was true for saliva and serum. A possible explanation is local antigen-driven expansion of AHT-reactive committed lymphocytes in the lacrimal tissues.

Adult↗
PubMed1976

The role of complement in the clearance of cold agglutinin-sensitized erythrocytes in man.

To define the pathophysiologic mechanisms of cold agglutinin disease, we investigated a human model of this syndrome in normal volunteers and in patients with diminished levels of serum complement. Subjects received intravenous injections of autologous, chromated (51Cr) erythrocytes which had been exposed in vitro to purified cold agglutinin preparations and to fresh autologous serum (as a source of complement). In vitro tests confirmed that such cells were coated with activated complement components (C3b), but not with immunoglobulin. Studies of erythrocyte clearance and simultaneous organ scanning showed that erythrocytes sensitized with low levels of cold agglutinin primarily undergo reticuloendothelial sequestration by the liver rather than intravascular hemolysis. After the initial sequestration of C3b-coated erythrocytes, a fraction of the cells are released back into the circulation and survive normally thereafter. Both phenomena are dose dependent and closely follow the sequestration and release pattern observed with IgM isoagglutinin sensitization. Experiments that used heated autologous serum as a source of B3 inactivator demonstrated that functionally intact C3b is required for hepatic sequestration. Erythrocytes coated with C3d were not cleared from the circulation. In vitro assays that sued human macrophage monolayers suggested that the intrahepatic conversion of C3b to C3d is responsible for the release of sensitized erythrocytes back into the circulation. The clearance of cold agglutinin-sensititzed erythrocytes was compared to the clearance mediated by IgM isoagglutinin. We found that the rate of complement fixation by an IgM antibody proceeds rapidly in vivo that the time for complement activation is not a factor in limiting the rate of hepatic sequestration. The major limiting factor appears to be the rate of liver blood flow. Maximal in vitro coating of erythrocytes with C3d conferred protection from further cold agglutinin sensitization but not from IgM isoagglutinin-mediated clearance. This suggests a mechanism for the resistance to lysis observed in cells obtained from patients with the cold agglutinin syndrome and confirms the marked dependence of the site of C3 attachment on the site of membrane localization of the sensitizing antibody.

Agglutinins↗
PubMed1986

Identification of a Streptococcus sanguis receptor for salivary agglutinins.

The objective of this study was to characterize a fraction from oral streptococci containing receptor activity for salivary agglutinin molecules. Several species and strains of streptococci were disrupted in a Ribi press. The supernatant was nuclease-treated and subjected to differential centrifugation. Receptor activity in the fractions was measured by the inhibition of saliva-mediated bacterial aggregation. In addition, bacterial strains were tested for their ability to aggregate and to deplete saliva of agglutinin activity. Three patterns of activity were observed: Streptococcus sanguis M5 depleted saliva of agglutinin activity and aggregated well; Streptococcus sanguis CC5A depleted saliva of agglutinin but did not aggregate well; and Streptococcus faecalis S-161 neither depleted saliva of agglutinin nor did it aggregate. The 105,000 g supernatant fractions derived from Ribi-disrupted Streptococcus sanguis M5 and CC5A, but not from Streptococcus faecalis, showed dose-dependent inhibition of saliva-mediated aggregation. This inhibitory activity was non-dialyzable, had the same heat and trypsin sensitivity as that seen with intact bacteria, and was not due to enzymatic digestion of the salivary agglutinin. Iso-electric focusing revealed a single active region with a pI of 5.5 which was clearly separated from the bulk of the bacterial proteins.

Agglutination↗
PubMed1988

Binding of peanut agglutinin to neuroblastomas and ganglioneuromas: a marker for differentiation of neuroblasts into ganglion cells.

Binding of peanut agglutinin (PNA), concanavalin A, Ricinus communis agglutinin, wheat germ agglutinin, soybean agglutinin, Ulex europaeus agglutinin 1, and Dolichos biflorus agglutinin was assessed in tissue sections of 4 cases of neuroblastoma (NB) to determine whether there were any differences in lectin binding among immature neuroblasts, maturing neuroblasts, and ganglion cells. Only PNA binding proved to be useful. This was assessed more fully in 17 cases of NB and 7 ganglioneuromas. PNA bound to immature neuroblasts in only 4 of 12 stroma-poor NB but to maturing neuroblasts and ganglion cells in 5 of 5 stroma-rich NB. PNA bound to ganglion cells in all 7 ganglioneuromas. The NB were categorized as favorable (7 cases) and unfavorable (10 cases), using the patients' ages and the histologic appearance and mitotic-karyorrhetic index of the resected tumor, and this was correlated with PNA binding. PNA bound to 6 of 7 NB with a favorable, and 3 of 10 with an unfavorable histologic type of NB (p less than 0.05). These studies suggest that neuroblasts acquire the capacity to bind to PNA as they differentiate into ganglion cells and that PNA binding is indicative of a favorable histologic type of NB.

Age Factors↗
PubMedDate not supplied

Antityphoid agglutinins in African school aged children with malaria.

BACKGROUND: Salmonella antibodies are known to cross-react with other antigens including those from Escherichia coli. Malaria antigens may also have similar characteristics. OBJECTIVES: To establish antibody levels in malaria patients and controls and to decipher (if any), relationship(s) between significant agglutinin responses to the various antigens as outcome factor and malaria parasitaemia as exposure factor. STUDY SETTING: University of Benin Teaching Hospital and Egor Local Government Area of Edo state, Nigeria, between July and August, 1999. STUDY DESIGN: Prospective and a case control study. PATIENTS AND METHODS: Agglutinins against H and O antigens of Salmonella typhi, Salmonella paratyphi A, B and C were determined using the Widal test in 189 school aged children(5-16 years) with malaria (males, 54.0%; females, 46.0%) and 175 apparently healthy children,(52.0% males, and 48.0 %) of comparable age and gender distributions. Agglutination reaction at >1.80 were significantly more in malaria patients (52/189 or 27.5%) than in controls (28/175 or 16.0%) (x2 = 7.07; p<0.05). Agglutination reaction to various antigens were significantly higher in controls with malaria parasitaemia (10/36 or 27.8%) than those without parasitaemia (18/139 or 12.9%) (x2 = 4.57; p<0.02) (OR=2.59). Significant titres were also more in subjects and controls with malaria parasitaemia (62/235 or 26.38%) than in those without (18/139 or 12.94%) (x2=9.32; p< 0.05) (OR=2.41). At dilution of > or =1.80 children aged 9 -14 years (as compared to those < or =8 years of age) and more males (subjects and controls) had demonstrable agglutinins. At most serum dilutions, antibodies to H antigens were more commonly found in subjects and controls than agglutinins against O antigen of Salmonella typhi. Fifty percent of subjects and controls had demonstrable agglutination at approximate dilutions of 1:60 and 1:40 respectively. The number of subjects and controls that showed demonstrable agglutinins against Salmonella paratyphi antigens were less than 10.0% CONCLUSION: Enhanced agglutinin to DO and DH may be a phenomenon associated with childhood malaria.

Adolescent↗
PubMed1975

Studies on the specificity of agglutinins against human erythrocytes modified by Newcastle disease virus.

The specificity of agglutinins in human sera against human erythrocytes modified by Newcastle disease virus (NDV-O agglutinins) was studied with agglutination and agglutination inhibition techniques. Virus grown in both embryonic eggs and tissue culture was used in the experiments. The findings were compatible with the existence of four specificities of agglutinins. In some sera, including those from subjects recently inoculated with vaccines prepared in eggs, the agglutinins were directed against a component of the allantoic fluid. In high-titred infectious mononucleosis (IM sera the agglutinins were directed against antigenic groupings present in the Vic strain but not the B1 strain of NDV, whereas in certain other sera they were directed against antigens present in both of them. Finally, in some sera the agglutinins probably reacted with a red cell antigen uncovered by the viral neuraminidase.

Agglutinins↗
PubMed2004

[Molecular cloning and analysis of a monocot mannose-binding agglutinin from Zephyranthes grandiflora (family Amaryllidaceae)].

The monocot mannose-binding lectin can inhibit HIV from infecting the target cells. The total RNA of Zephyranthes grandiflora was extracted and reversely transcribed into cDNA. Degenerate primers were designed based on the conserved regions of other monocot mannose-binding agglutinins by homology alignment. The 694bp full-length cDNA of Zephyranthes grandiflora agglutinin (ZGA) was cloned by RT-PCR, 3' and 5' RACE (rapid amplification of cDNA ends). The start codon and stop codon of ZGA were at 37-39bp and 529-531bp respectively. The NCBI Blast analysis result showed that ZGA gene encoded a protein precursor with signal peptide, mature protein and C-terminal cleavage sequence. The mature ZGA protein contained 106 amino acids residues and its molecular weight was 11.6KD. The percentages of identity of the deduced mature ZGA protein with those of Galanthus nivalis agglutinin, Narcissus hybrid cultivar agglutinin, Lycoris radiate agglutinin and Clivia miniata agglutinin were 71.8%, 81%, 81.8% and 84.5%, respectively. Blocks analysis revealed that ZGA had three functional domains and three mannose-binding boxes (QDNY).

Agglutinins↗
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↗
PubMed1979

Characterization of sperm agglutinins in sera from infertile women.

Sperm agglutinins detectable by a tray agglutination technique in sera from women from infertile couples were characterized. Preparative zone electrophoresis of seven head-to-head-agglutinating sera revealed two patterns. In two sera sperm agglutinins were obtained in the gamma-globulin fraction, whereas in five sera the agglutinating activity was detected in the beta-globulin fraction only. By immunoaffinity chromatography, IgM and IgG sperm antibodies were demonstrated in the former two sera and also in two tail-to-tail-agglutinating sera. The beta"sperm agglutinin was not found to share physicochemical or immunological characteristics with beta-lipoprotein in the present investigation by ultracentrifugation, by precipitation of beta-lipoprotein with heparin and MnCl2, by absorption of beta-lipoprotein with colloidal silic acid, or by affinity chromatography on an anti-beta-lipoprotein column. An apparent neutralizing effect of anti-beta-lipoprotein by simple addition of antiserum to sera containing the beta-sperm agglutinin was shown to be due to a reaction with sperm components released from the spermatozoa by which the antiserum had been absorbed before use. These sperm components were found to neutralize the activity of the beta-sperm agglutinin only, whereas no effect was observed in sera containing sperm antibodies. By Sephadex G-200 fractionation the beta-sperm agglutinin was shown to have a high molecular weight (MW greater than or equal to 600,000). Ultrafiltration and dialysis experiments gave no evidence of involvement of low-molecular compounds in head-to-head agglutination.

Agglutination Tests↗
PubMed1985

Proteoglycans from bovine nasal and articular cartilages. Fractionation of the link proteins by wheat germ agglutinin affinity chromatography.

Two forms of link protein, 46 and 51 kDa, are present in proteoglycan aggregates from both bovine nasal and bovine articular cartilages. Studies reported here show that the link proteins bind to concanavalin A, Lens culinaris agglutinin, Ricinus communis agglutinin, soybean agglutinin, and wheat germ agglutinin lectins. When the link proteins are eluted from these lectins with appropriate competing sugars, the 46- and the 51-kDa link proteins elute together and no separation is achieved. However, when the link proteins bound to wheat germ agglutinin are eluted with a 0 to 4 M guanidine hydrochloride linear gradient, a good separation of the 46- and 51-kDa link proteins is achieved. Wheat germ agglutinin affinity chromatography has been used on a preparative scale to isolate the 51-kDa link protein from mature bovine articular cartilage to homogeneity, in amounts sufficient to examine its effect on proteoglycan aggregate size and stability in sedimentation velocity studies. Proteoglycan aggregates were reassembled from proteoglycan monomers and hyaluronate in the absence of link protein, in the presence of both 46- and 51-kDa link proteins, and in the presence of the individual 51-kDa link protein. The sizes of the aggregates were compared in terms of sedimentation coefficients (s(0)20). The stability of the aggregates was compared in terms of the per cent aggregate present at pH 7 and 5. At pH 7, the sedimentation coefficients (s(0)20) of link-free aggregates, aggregates formed with both link proteins, and aggregates formed with 51-kDa link protein were 72, 93, and 112 S, respectively. Thus, the 51-kDa link protein has a pronounced effect on aggregate size. The link-free aggregate was grossly unstable, and only 36% aggregate was present at pH 5. The aggregate formed with both link proteins was effectively stabilized against dissociation and 79% aggregate was present at pH 5. The aggregate formed with 51-kDa link protein was not effectively stabilized against dissociation, and only 60% aggregate was present at pH 5. Thus, despite its pronounced effect on aggregate size, the 51-kDa link protein does not effectively stabilize the proteoglycan aggregate against dissociation. These results suggest that the 51-kDa link protein may selectively increase aggregate size, while the 46-kDa link protein may be required to effectively stabilize the proteoglycan aggregate against dissociation.

Animals↗
PubMedDate not supplied

Human lymphocyte receptors detected by invertebrate agglutinins.

A review of recently published work is presented on the nature of the agglutination of human peripheral lymphocytes and cultured lymphoblastoid cells by the hemolymph agglutinins of two arachnoids, the Horsefoot (Limulus polyphemus), alias Horseshoe Crab, and the Saharan Scorpion (Androctonus australis). Microagglutination techniques were utilized to study the specificity of the whole serum and purified agglutinin(s) of Limulus and the whole serum agglutinin(s) of Androctonus. Peripheral human lymphocytes of patients with chronic lymphocytic leukemia (CLL) gave higher agglutination titers and scores than did normal cells, with both species of invertebrate agglutinins. However, human B cells gave higher, although overlapping degrees of agglutination, than T cells. The major cell membrane receptor site for agglutinins of both species was the sialic acid moiety, N-acetyl neuraminic acid. Selected literature on plant and invertebrate agglutinins (lectins) was reviewed. These lectins are underscored as valuable cell membrane probes of surface receptors of human lymphocyte subpopulations.

Agglutinins↗
PubMed1996

Trypanosoma cruzi and erythrocyte agglutinins: a comparative study of occurrence and properties in the gut and hemolymph of Rhodnius prolixus.

The activity of agglutinins found in the gut tissues and hemolymph of Rhodnius prolixus was tested using rabbit erythrocytes, Trypanosoma cruzi, or Trypanosoma rangeli as test particles. In addition, investigations were made of the influence of parasitic infection and insect diet on the agglutination titers. A range of physicochemical tests and carbohydrate-binding studies were performed and inhibitors were subsequently found for both the crop agglutinin (p-nitrophenol-derived sugars) and the hemolymph agglutinin (galactose-type sugars). As a result, affinity chromatography was utilized for an attempted purification of these agglutinins, and a one-step purification protocol for the R. prolixus hemolymph agglutinin has been developed. Preliminary results of some biological and physicochemical characteristics of this pure agglutinin are described. These results represent a starting point for future studies of lectin/parasite interaction in this reduviid-trypanosome model.

Animals↗
PubMed1977

Effects of wheat germ agglutinin on membrane transport.

(1) Low concentrations of wheat germ agglutinin are cytotoxic toward several tissue culture lines, including Chinese hamster ovary cells, Swiss 3T3 cells, mouse L cells and baby hamster kidney cells. The LD50 ranged from 1 to 5 microgram wheat germ agglutinin per ml. Similar concentrations of the lectin inhibited the transport of the non-utilizable amino acids alpha-aminoisobutyric acid and cycloleucine and inhibited the uptake of thymidine. In contrast, 2-deoxy-D-glucose uptake was not altered and colchicine uptake was enhanced. (2) The inhibition of alpha-aminoisobutyric acid uptake occurred within minutes after lectin addition and was maximal by 1 h. Maximal inhibition ranged from 50 to 70% of control values. Studies of the kinetics of the uptake demonstrated that wheat germ agglutinin decreased the V of the uptake by 70% without affecting the apparent Km. Ovomucoid, a haptene inhibitor of wheat germ agglutinin-binding to cell surface receptors, prevented the wheat germ agglutinin-induced inhibition of alpha-aminoisobutyric acid transport. Three other lectins (Concanavalin A, Phaseolus vulgaris E-phytohemagglutinin and L-phytohemagglutinin) inhibited the uptake by 20% or less at doses up to 50 microgram/ml. (3) We propose that the cytotoxicity of wheat germ agglutinin probably results in part, if not totally, from membrane alterations which impair multiple membrane transport systems.

Aminoisobutyric Acids↗
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↗
PubMed1985

Ultraviolet difference spectroscopic analysis of the saccharide-binding properties of Ricinus communis agglutinin.

The nature of the binding of saccharides to Ricinus communis agglutinin was studied by ultraviolet difference spectroscopy. Upon binding of galactose and galactose-containing saccharides, R. communis agglutinin displayed difference spectra with an extreme maximum at 291-293 nm and a smaller maximum at 284-285 nm. Such difference spectra suggest that the environment of a tryptophan residue located at or near the saccharide-binding site of R. communis agglutinin is being changed by an interaction between a tryptophan residue and the bound saccharides. The value of the difference spectra (delta epsilon) increased upon progressive addition of saccharide until the saccharide binding site was saturated with ligand. From the increase in delta epsilon at 291-293 nm, the association constants were obtained for the R. communis agglutinin-saccharide interaction over the temperature range 5-35 degrees C and various pH values. The results clearly demonstrate that the association constants are nearly equal in the range of pH 5-8, but decrease beyond the above pH range and with elevation of temperature. From the thermodynamic parameters for the binding of various saccharides to R. communis agglutinin, we suggest that there exists a subsite structure in the saccharide-binding site of the R. communis agglutinin molecule.

Binding Sites↗
PubMed1986

Organization of genes expressing the blood-group-M-specific hemagglutinin of Escherichia coli: identification and nucleotide sequence of the M-agglutinin subunit gene.

The organization of genes encoding the blood group M-specific hemagglutinin (M-agglutinin) of Escherichia coli strain IH11165 was studied with a cloned 6.5-kb DNA segment. This DNA segment contains at least five genes which code for the polypeptides of 12.5, 30, 80, 18.5 and 21 kDa. The 30-, 80- and 21-kDa polypeptides are synthesized as precursors that are approximately 2 kDa larger. The 21-kDa polypeptide was identified as the M-agglutinin subunit by its reactivity with anti-M-agglutinin serum. Nucleotide sequence analysis of the corresponding gene showed that the M-agglutinin precursor had a 24-amino acid (aa) signal sequence, while the mature protein is 146 aa residues long. Although the organization of the M-agglutinin gene cluster resembles those of other E. coli adhesins, there is no significant sequence homology between the M-agglutinin subunit and the subunits of the other potentially related proteins in E. coli.

Amino Acid Sequence↗
PubMed2006

Effects of purified soybean agglutinin on growth and immune function in rats.

The objective of this study was to investigate the effect of purified soybean agglutinin on growth and immune function in rats. Thirty male Sprague-Dawley rats (77.8 +/- 2.6 g) were individually fed casein-cornstarch based diets containing 0, 0.05, 0.10, 0.15 or 0.20% soybean agglutinin (w/w) during a 20-day experiment. Growth declined linearly with increasing the concentration of soybean agglutinin (p < 0.05). The proliferation of lymphocytes in spleen, lymph nodes and blood decreased with an increase in dietary soybean agglutinin (p < 0.05). The concentrations of interleukin-2, interferon-gamma and tumor necrosis factor-alpha in plasma, spleen, and mesenteric lymph nodes as well as plasma concentrations of IgA, IgG and IgM also declined with increasing dose of soybean agglutinin (p < 0.05). The results show that dietary soybean agglutinin has negative effects on growth as well as both cell-mediated and humoral immune function of rats and appears to function in a dose-dependent manner.

Animal Feed↗