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PubMed1996

Purification, physicochemical characterization and biological properties of a lectin from Erythrina velutina forma aurantiaca seeds.

A lectin was purified from seeds of Erythrina velutina forma aurantiaca by affinity chromatography on cross-linked guar gum. The lectin is a potent agglutinin for human (minimal concentration of protein able to cause visible agglutination of a 2% erythrocyte suspension varying from 1 to 4 micrograms/ml), rabbit (4 micrograms/ml) and chicken erythrocytes (8 micrograms/ml) but presented low activity against cow (250 micrograms/ml) or sheep (333 micrograms/ml) blood cells. Hemagglutination of human O+ erythrocytes was inhibited by D-lactose (0.2 mM) > D-galactose (0.8 mM) > D-raffinose (2.1 mM). At pH 7.5, chromatography on a Superose 12 HR 10/30 column showed that the lectin was primarily a dimer (56.0 kDa) composed of two identical subunits (31.6 kDa each). A small amount of a tetrameric form was also apparently present. The lectin is a glycoprotein (7.3% carbohydrate), has a pI of 4.5, contains high levels of acidic (Asp and Glu, 64.2 and 51.6 residues/mol, respectively) and hydroxy amino acids (Ser and Thr, 42.9 and 38.5 residues/mol, respectively) but relatively low amounts of sulfur amino acids (Cys and Met, 1.0 and 5.0 residues/mol, respectively) and has an N-terminal sequence of Val-Glu-Thr-Ile/Leu-Pro-Phe-Ser. Its hemagglutinating activity was abolished by heating at 70 degrees C for 10 min. The activation energy (delta G') required for denaturation measured by loss of hemagglutination activity was 24.87 kcal/mol. In rats, the purified lectin (100 micrograms) induced neutrophil migration into the peritoneal cavity (3.7 +/- 0.6 x 10(6) neutrophils/ml) or into the air pouch (2.75 +/- 0.25 x 10(6) neutrophils/ml), 8 and 10 times greater than the negative control, respectively.

Animals↗

PubMed1977

Agglutinins to Coxiella burnetii and Brucella spp, with particular reference to Brucella canis, in wild animals of southern Texas.

The prevalence of agglutinins to Coxiella burnetii and Brucella spp, particularly Brucella canis, was determined in 269 wild animals (14 species) in southern Texas. Serologic evidence of coxiellosis and brucellosis, including B canis infection, was shown for coyotes, raccoons, opossums, badgers, jackrabbits, and feral hogs. Using the microagglutination test, the seroprevalence of C burnetii, phases I and II (titer greater than or equal to 4) was 4.1 and 27.9%, respectively. For brucella agglutinins, prevalence rates were 7.1, 8.9, and 6.7%, as determined by the brucellosis card test, the rapid slide agglutination test, and the salt 2-mercaptoethanol tube agglutination (titer greater than or equal to 50) test, respectively.

Agglutinins↗

PubMed1994

Identification of anti-agglutinin for spermatozoa in epididymal boar plasma.

The present report identifies epididymal boar anti-agglutinin and examines its effect on sperm motility. Boar spermatozoa from the cauda epididymidis were washed and incubated in modified Krebs-Ringer bicarbonate at 37 degrees C (5% CO2 in air). In the samples washed three or five times and then incubated for 3-5 h, higher rates (72-79%) of spermatozoa were associated with one another at the acrosomal region, mainly in groups of 2-5 cells (head-to-head agglutination), and many cells exhibited intensively flagellant and/or circular types of movement but rarely progressive motility. The addition of epididymal plasma or 25 kDa protein purified from it markedly inhibited the occurrence of head-to-head agglutination in washed spermatozoa, whereas heat treatment and subsequent removal of insoluble materials reduced the anti-agglutination activity of epididymal plasma. The percentages of progressively motile cells in the samples incubated with epididymal plasma or 25 kDa epididymal protein rose coincident with the reduction of sperm agglutination. These findings demonstrate that the 25 kDa epididymal protein is an anti-agglutinin for the cauda spermatozoa and that it effectively functions to maintain progressive motility of the cells in vitro.

Animals↗

PubMed1987

Ethanol-induced alterations in human erythrocyte shape and surface properties: modulatory role of prostaglandin E1.

Exposure of human erythrocytes to ethanol (1 to 20% by vol) in Ca2+ and Mg2+-free phosphate-buffered saline, pH 7.4, transformed biconcave discs into spiculated echinocytes within 3 min at 25 degrees C. The effects of ethanol were concentration-and time-dependent, but reversible by washing in the incubation buffer system within 60 min of initial exposure to ethanol. After prolonged ethanol exposure (180 min), washing of cells resulted in the formation of stomatocytes (cup-forms). Ethanol-induced echinocytosis was also accompanied by a 30% enhancement in the agglutinability of erythrocytes by ligands with high affinity for negative surface charge (poly-L-lysine and wheat germ agglutinin, 20 microliters/ml) without any alterations in surface charge topography. Concomitant exposure of erythrocytes to prostaglandin E1 (100 nM) selectively prevented the enhancement of ligand-mediated agglutinability, but did not modify cell shape. These data indicate that certain erythrocyte surface properties may not be directly influenced by cell shape and suggest a unique modulatory action of prostaglandin E1 on shape-transformed cells.

Alprostadil↗

PubMed1987

Isolation and composition of the constitutive agglutinins from haploid Saccharomyces cerevisiae cells.

Sex-specific agglutinins from the cell surface of haploid cells of Saccharomyces cerevisiae (X2180, mta and mt alpha) were purified and analysed. The constitutive agglutinin from mta cells was extractable with 3 mM dithiothreitol. It was shown to be a glycoprotein (3% mannose) with an apparent Mr of 43,000 based on gel filtration, but in SDS-PAGE it behaved as a much smaller molecule (Mr between 18,000 and 26,000). About one in three amino acids was a hydroxyamino acid. Its biological activity was resistant to boiling for 1 h, but sensitive to pronase. Intact mt alpha cells retained their agglutinability in the presence of dithiothreitol but limited trypsinizing released a biologically active agglutinin fragment. It had an apparent Mr of 320,000 (gel filtration). When analysed by SDS-PAGE, a single diffuse band with an apparent Mr of 225,000 was observed. The protein was 94% (w/w) mannose with a trace of N-acetyl glucosamine. Its biological activity was almost completely lost after boiling for 1 h. Both agglutinins behaved as monovalent molecules and specifically inhibited the biological activity of both noninduced and pheromone-induced cells. Pheromone treatment of mta cells resulted in an apparent 32-fold increase in agglutinin activity at the cell surface, whereas pheromone treatment of mt alpha cells only doubled the apparent agglutinin activity.

Agglutinins↗

PubMed1983

Acquired B antigen: further studies using synthetic oligosaccharides.

The reactivity of acquired-B red cells with various antisera has been investigated by agglutination inhibition assays using four trisaccharides obtained by chemical synthesis. Two of these had the structure GalNAc alpha 1-3 (LFuc alpha 1-2). Gal and Gal alpha 1-3 (LFuc alpha 1-2) Gal which are characteristic of the A and B determinants respectively and were indeed strong inhibitors of human anti-A and -B antibodies. The other two sugars denoted B-OAc and B-NH2 are derivatives of the B-trisaccharide by substitution of the hydroxyl group on carbon-2 of the alpha-galactose residue with the O-acetyl group (B-OAc) or the amino group (B-NH2) respectively. We have shown that both B and B-NH2 trisaccharides inhibited strongly the agglutination of acquired B red cells by the anti-B reagents (crude or affinity purified) whereas sera containing "anti-acquired B" agglutinins were specifically inhibited by B-NH2 but not by the A, B or B-OAc structures. We have also shown that the agglutination of Tk-activated erythrocytes by the BS-II lectin is specifically inhibited by N-acetylglucosamine but not by B, B-OAc or B-NH2 structures. These results and the observation that anti-acquired B agglutinins cannot be adsorbed on Tk red cells suggest that (i) the "B-like" and the "acquired-B" determinants share a common structure best represented by B-NH2 and (ii) Tk and "acquired-B" antigens are not identical.

ABO Blood-Group System↗

PubMed1976

[A further case of albumin auto-agglutination in a blood donor].

A blood donor is described whose serum contains an albumin active agglutinin reacting with autologous as well as normal donors red cells. Natrium caprylate present in some commercial albumin preparations is show to be co-responsible for this unusual reaction which cause difficulties or errors in Rh grouping.

Adult↗

PubMed1988

Molecular Studies on the Role of a Root Surface Agglutinin in Adherence and Colonization by Pseudomonas putida.

Pseudomonas putida aggressively colonizes root surfaces and is agglutinated by a root surface glycoprotein. Mutants of P. putida derived chemically or by Tn5 insertion demonstrated enhanced or decreased agglutinability. Two nonagglutinable Tn5 mutants (Agg) and two mutants with enhanced agglutinability (Agg) possessed Tn5 in unique restriction sites. Agg mutants colonized root surfaces of seedlings grown from inoculated seeds, but at levels lower than those observed with the Agg parent. In short-term binding studies, Agg cells adhered at levels that were 20- to 30-fold less than those for Agg parental cells. These data suggest that the agglutination interaction plays a role in the attachment of P. putida to root surfaces.

Journal Article↗

PubMedDate not supplied

The isolation of a possible antagglutinin from human semen.

A substance, proteinaceous in nature, with an anti-agglutinic action on clumped sperm has been extracted from human semen. It appears to exist in two forms: an active reduced form and an inactive oxidised form. The protein was extracted from oxidised seminal plasma by salting with saturated ammonium sulphate. The extract was purified by preferential adsorption on a calcium carbonate column, the eluate being collected as fractions. The antagglutinin gave an extinction curve, as determined by ultraviolet spectrophotometry, similar to that as reported for the bull. Extraction recoveries, from semen stored frozen at different temperatures, indicate that the substance is possibly enzyme labile. An effect of the antagglutinin on clumped human sperm is illustrated.

Agglutinins↗

PubMed1975

Microtechnique for simultaneous determination of immobilizing and cytotoxic sperm antibodies. Methodological and clinical studies.

A microtechnique for simultaneous detection of immobilizing and cyctotoxic sperm antibodies was elaborated according to the principles of Terasaki and McClelland. The technique was found reproducible, easy to perform and thus suitable for large scale examinations. The test includes determination of titres for immobilizing and cytotoxic effects and provides at the same time an opportunity to observe both complement-dependent and independent activities. Furthermore, agglutination patterns can easily be recorded. The requirement of only small volumes of test samples makes the test suitable also in testing secretions from the genital tract. In these cases, inclusion of a control for anticomplementary activity of the sample is advisable. In serum from 288 men from infertile couples simultaneous occurence of immobilizing and cytotoxic antibodies was observed in eight cases; all of them also had sperm-agglutinins in serum. In two of these cases, immobilizing and, in one case, cytotoxic activity was revealed in seminal plasma using undiluted samples. Patients with negative findings in serum also revealed negative findings in seminal plasma. Immobilizing and cytotoxic antibodies were not disclosed in serum from 247 women from infertile couples.

Agglutination Tests↗

PubMedDate not supplied

Management of cold agglutination syndrome.

Cold haemagglutination syndrome is difficult to treat. Fortunately it seldom needs treating. In most cases cold agglutinins are an incidental finding representing either normality or a benign chronic monoclonal gammopathy that does not cause ill health. Two sorts of symptoms are likely in the more severe cases. Acrocyanosis is usually treated by keeping the patient warm and if necessary removing him or her to Florida or the Canary Islands. In the rare cases of haemolytic anaemia, an underlying lymphoid tumour should be sought and treated. If none exists, then it is unlikely that the treatments that are useful in warm antibody haemolytic anaemia will be helpful. Plasma exchange ought to work but in practice there are frequently problems of red cell agglutination within the cell separator or the plastic tubes. For this reason plasma exchange within a heated room is advocated. When cardiac surgery is contemplated pre-operative plasma exchange is sometimes helpful, or the heart may be stopped by potassium solutions and the operation is carried out in the warm.

Anemia, Hemolytic↗

PubMed1992

Agglutinins in the hemolymph of the hard clam, Mercenaria mercenaria.

Lectins in the serum of the clam Mercenaria mercenaria agglutinate some red blood cells, bacteria, and yeast. The interaction of these substances with particles is affected by sugars, ions, temperature, and alteration of particle surfaces. Lectins are not needed for phagocytosis of foreign particles in vitro. In M. mercenaria these recognition molecules do not enhance defense mechanisms.

Agglutinins↗

PubMed1978

Standardization of the agglutination test in the diagnosis of Yersinia enterocolitica infection.

For preparation of antigens standard strains of Yersinia enterocolitica representing serological groups I to VI (according to KNAPP and THAL) were used. The following antigens preparations were used: antigens autoclaved at 121 degrees C, antigens treated with formaline and living cells. The antigens were titrated against homologous immune sera, and their optical density was estimated spectrophotometrically. In the rabbit immune sera, and additionally, in the sera of blood donors and subjects suspected of Y. enterocolitica infection the levels of agglutinins were estimated against the antigens of all serotypes. The results from both groups of sera were analysed numerically with the use of the "Odra 1204" computer. Basing on the antigen titers frequency distribution critical and diagnostically doubtless values were established. The usefulness of living cells and antigens treated with formaline of the serotype IA and serotype V in the serological diagnosis of the Y. enterocolitica infections was demonstrated.

Agglutination Tests↗

PubMed1995

Elevated levels of serum antibodies to the lectin wheat germ agglutinin in celiac children lend support to the gluten-lectin theory of celiac disease.

Lectins recognize carbohydrate moities of glycoproteins and glycolipids, and can elicit several biological effects, including cell agglutination, cell activation and mitogenesis. According to the gluten-lectin theory, celiac lesions represent a response to a toxic lectin, putatively wheat germ agglutinin (WGA). In this study we compared the serum antibody levels IgA, IgG and IgM to WGA and to gliadin in children under investigation for celiac disease (CD), as compared to reference children. We found that the levels of IgA and IgG to WGA as well as gliadin were significantly higher in celiac children on a gluten-containing diet, compared to children on gluten-free diet and reference children. These findings lend support to the concept that WGA is a biologically significant component of gluten. Since WGA can mimic the effects of epidermal growth factor (EGF) at the cellular level, we hypothesize that the crypt hyperplasia seen in celiac children could be due to a mitogenic response induced by WGA.

Adolescent↗

PubMed1994

Cloning, sequencing, and viscometric adhesion analysis of heat-resistant agglutinin 1, an integral membrane hemagglutinin from Escherichia coli O9:H10:K99.

The gene encoding a mannose-resistant hemagglutinating protein was cloned from Escherichia coli O9:H10:K99. The hemagglutinin is different from two other mannose-resistant hemagglutinins in this strain, K99 and F41. The agglutinin, named heat-resistant agglutinin 1 (HRA1) since heating to 70 degrees C does not destroy its aggregative properties, strongly agglutinates human, pig, and dog erythrocytes, shows little or no affinity towards cow and chicken erythrocytes, but agglutinates human colon adenocarcinoma 201 (COLO 201) cells. The hra1 gene present on the recombinant plasmid pETE1 was localized by subcloning, and its nucleotide sequence was determined. The gene consists of a 792-bp open reading frame coding for a putative protein of 29 kDa with a predicted N-terminal secretory signal sequence. HRA1 shares no significant identity with data base protein sequences. HRA1 is strongly associated with the bacterial membrane, resisting sonication and isolation attempts based upon standard adhesin purification techniques. N-terminal sequencing of a unique 25-kDa band present in polyacrylamide gels of outer membrane preparations of bacteria harboring pETE1 correlated with the predicted N-terminal amino acid sequence of HRA1 after cleavage of the signal peptide. A viscometric agglutination assay sensitive to the strength of bacterial adhesion shows that the agglutination mediated by bacteria expressing HRA1 is weaker than that of bacteria bearing the F41 adhesin, probably because of the high-molecular-weight, multivalent nature of the latter adhesin. Our observations suggest that HRA1 is a monomeric outer membrane agglutinin.

Adhesins, Bacterial↗

PubMed1971

Effects of heterologous antineutrophil serum in guinea pigs. Hematologic and ultrastructural observations.

Two pools of rabbit anti-guinea pig neutrophil serum (ANS) were prepared using an intravenous (ANS I) or subcutaneous (ANS II) route of immunization with proteose peptone-stimulated peritoneal exudate neutrophils (PMNs) from albino guinea pigs. In vitro, both pools of ANS contained high titers of agglutinating antibodies to neutrophils and lower titers against lymphocytes and red cells. Agglutinins against all three cell types could be selectively removed by absorption. The in vivo hematologic effects of both the absorbed and unabsorbed antisera were examined after intraperitoneal administration, and the effects of ANS on neutrophils in blood, bone marrow, and peritoneal cavity were examined by light and electron microscopy of spleen, liver, lung, lymph node, buffy coat, bone marrow and pellets of peritoneal cells removed at various time intervals within 24 hours. Injection of either antisera caused a rapid decrease in circulating neutrophils and lymphocytes, which reached their lowest levels within 12 hours. Neutrophils that disappeared from the circulation were sequestered primarily in liver and spleen where they were phagocytized, as morphologically intact cells, by macrophages and then rapidly digested. Immature bone marrow neutrophils as young as early myelocytes were ingested by macrophages in the marrow at 6 hours or later after ANS. Neutrophils that were phagocytized were apparently opsonized by ANS since there was no ultrastructural evidence of neutrophil lysis in blood or bone marrow after ANS treatment. However, both lysed and ingested neutrophils were observed in the peritoneal cavity. Absorption of ANS with neutrophils removed the ability of the serum to produce neutropenia. However, absorption of ANS with lymphocytes did not alter the lymphopenia produced by the antiserum. The fate of lymphocytes leaving the peripheral circulation was not apparent. Lymphocytes did not accumulate in liver or spleen sinusoids and were not ingested by macrophages in these organs, as were the neutrophils. There was no evidence of paracortical depletion or extensive phagocytosis of lymphocytes in lymph nodes after ANS, as other investigators have reported after administration of antilymphocyte serum.

Agglutination↗

PubMed1988

Bacterial agglutinins in rat salivary glands: effect of glandular stimulation and calcium dependency.

The secretory pattern of salivary, bacterial agglutinins was studied in the rat. The three major salivary glands were cannulated bilaterally and their secretions collected separately after parasympathomimetic and sympathetic stimulation. The bacterial aggregating activity of the secretions was tested against four strains of bacteria indigenous to the rat. Agglutinin activity was demonstrated in both parasympathomimetic and sympathetic secretions. The parotid glands tended to show the highest total output of agglutinins, with the highest titers found in parotid saliva on sympathetic stimulation. In submandibular and, particularly, parotid saliva, titers tended to increase when stimulation with pilocarpine was followed by sympathetic stimulation. In contrast, titer in sublingual saliva tended to decrease on sympathetic stimulation. When expressed as titer output per minute, sympathetic parotid secretion showed the highest agglutinin activity. Agglutinin activity appeared unrelated to total protein or to duct-derived amidolytic activity. Titers of parotid or submandibular saliva were increased 5- to 10-fold by the presence of 3.3 mM CaCl2 in the reaction mixture. By contrast, the agglutinating activity of sublingual saliva on parasympathomimetic stimulation was unaffected by extraneous CaCl2. Measurements of Ca concentration in similarly obtained rat salivary secretions did not show patterns of Ca concentration that could be related to the varying sensitivity of the agglutinating activity to Ca.

Agglutinins↗

PubMed1984

Chlamydomonas agglutinin conjugated to agarose beads as an in vitro probe of adhesion.

Flagellar sexual agglutinins are responsible for the primary recognition and adhesion events of mating in Chlamydomonas reinhardi which culminate in zygotic union of plus and minus gametes. Recent studies in this laboratory have shown the plus agglutinin to be an extremely large (greater than 10(6) D) and asymmetric glycoprotein containing a high proportion of hydroxyproline and serine residues [14, 27, 28]. This paper reports an improved method for in vitro investigations of the adhesive nature of this molecule. Purified agglutinin is covalently attached to an insoluble (Affi-gel 15 agarose bead) support and shown to retain potent agglutination activity when presented to living minus gametes, which rapidly and extensively adhere to the coated bead surface by their flagella. The specificity of the response is documented by the lack of interaction of plus gametes with the immobilized plus agglutinin (IA+). Using this simple yet sensitive bioassay, we have subjected IA+ beads to various enzymatic, chemical and physical treatments and assessed the effects on agglutinin activity. These studies reveal that Chlamydomonas plus agglutinin is sensitive to thermolysin or trypsin digestion, alkaline borohydride reduction, periodate oxidation, thiol reduction and heating at 65 degrees C, but unaffected by treatment with chymotrypsin, endo- or exoglycosidases, or incubation with isolated minus agglutinin. The implications of these results for agglutinin structure and possible functional interactions in initial recognition/adhesion events are discussed.

Adhesiveness↗