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PubMed1981

Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins.

Glycopeptides and oligosaccharides of either the N-acetyllactosaminic or the oligomannosidic type derived from glycoproteins containing the N-glycosylamine linkage were used to define the specificity of different lectins (concanavalin A, Lens culinaris agglutinin, Vicia faba agglutinin, Pisum sativum agglutinin, Ricinus communis agglutinins, soybean agglutinin, wheat germ agglutinin, Solanum tuberosum agglutinin, Datura stramonium agglutinin, Lotus tetragonolobus agglutinin, Ulex europeus agglutinin) by studying the inhibition of human red blood cell agglutination by these structures. The results obtained show that lectins considered 'identical' in terms of monosaccharide specificity, possess the ability to recognize fine differences in more complex structures. In fact, different lectins are able to recognize different saccharidic sequences on the same glycan structure. As these sequences are likely to be common to numerous glycoproteins, including cell membrane glycoproteins, the results obtained with lectins in the study of cell surface carbohydrates have to be very carefully interpreted. Moreover, our results confirm previous data on the spatial configuration of the glycan moiety of glycoproteins deduced from the construction of molecular models: the fact that oligosaccharides bearing an alpha-NeuAc-(2 leads to 6)-Gal unit are more powerful inhibitors than oligosaccharides bearing an alpha-NeuAc-(2 leads to 3)-Gal unit could be related to the high rotational freedom of alpha-2,6 linkage; the observation that glycoasparagines, glycopeptides and glycoproteins possess a higher affinity for lectins than the related oligosaccharides could be explained by the fact that the glycan--amino acid linkage leads to structures more rigid than those of the oligosaccharides themselves.

Acetylgalactosamine↗
PubMed1986

Are cross-reacting natural antibodies multispecific?

Human natural antibodies to antigens of Escherichia coli and Serratia marcescens were studied for cross-reactivity. The organisms were grown on synthetic media and extracted at 100 degrees C. The extracts were precipitated three times at 71% ethanol concentration and redissolved at the desired concentration. These preparations were referred to as Escherichia antigen (Ea) and Serratia antigen (Sa). They readily coated red blood cells (RBC), which then could be used for passive agglutination tests. Human serum selected for this study had strong agglutinins combining with both antigens (cross-reacting antibody) and rather weak agglutinins combining with Ea only or Sa only, a property that became obvious from absorption experiments. Absorption of the serum with RBC coated by Ea removed all activity for Ea and most of the activity for Sa, and the opposite effect was noted after absorption of the serum by RBC coated by Sa. The activity against both antigens could be recovered by elution of antibodies at 56 degrees C from RBC coated by either Ea or Sa. Significantly, inhibition of the serum or the eluate with soluble antigens gave strictly specific results in that Ea abolished only the reaction with RBC coated by Ea and did not influence the reaction of RBC coated by Sa, and the opposite result was obtained upon inhibition of the serum with Sa. These results strongly indicated to us that the cross-reacting antibodies under study were multispecific, i.e., had different antigen-reactive sites (haptophore groups) for Ea and Sa. Further evidence supporting this contention was obtained from a study in which the cross-reacting antibody was 'labelled' by a bacterial antigen. To this end, the tested serum was neutralized with Sa and then reacted with RBC coated by Ea. From these RBC, antibodies were eluted from which Sa was recovered. A 'mirror image' experiment was also conducted in which Ea was recovered from antibodies that were blocked by Ea and reacted with RBC coated by Sa.

Antibodies, Bacterial↗
PubMed1979

A simple technique to differentiate between animals infected with Yersinia enterocolitica IX and those infected with Brucella abortus.

While both Brucella abortus and Yersinia enterocolitica IX have O antigens in common, they differ significantly with respect to motility. Thus Br abortus is always non-motile while Y enterocolitica is motile when grown at room temperature. The presence of yersinia H agglutinins in serum can be shown to be evidence of previous exposure to Y enterocolitica. These agglutinins are not generated by brucella infection. A rapid H agglutination test will serve to provide this differentiation without interference from cross-reacting O antigens.

Agglutination Tests↗
PubMed1965

Protective antigens from El Tor vibrios. 1. The preparation and properties of a purified protective antigen from an El Tor vibrio (Ogawa subtype).

A biochemically and immunologically homogeneous antigenic fraction having the properties of a lipopolysaccharide has been isolated from the culture supernatant of an El Tor vibrio (Ogawa subtype). This antigen was very specifically protective for mice challenged with Ogawa strains of either El Tor vibrios or Vibrio cholerae. Rabbit antisera prepared against the antigen were passively protective for mice and highly vibriocidal but had little agglutinating activity. However, the antigen was able specifically to absorb agglutinins, as well as mouse-protective and vibriocidal antibody from serum prepared against whole bacterial cells. The specific protective activity of this lipopolysaccharide was much greater than that of vaccines made from whole bacterial cells, and its toxicity in animals was about equivalent to that of whole cells. The relationship of activity to toxicity therefore represented an improvement over the vaccines that were studied.

Animals↗
PubMed1984

Defects in specific associations between astroglia and neurons occur in microcultures of weaver mouse cerebellar cells.

The neurological mutation weaver is characterized by defects in granule cell migration along Bergmann glial processes and by subsequent death and disposition of granule cells. Immunocytochemical localization of antisera raised against purified glial filament protein (AbGF) and transmission electron microscopy were used to visualize specific associations between granule neurons and astroglia in microcultures of cerebellar cells dissociated from normal (+/+), heterozygous (+/wv), and homozygous (wv/wv) B6CBA-w mouse cerebella. In microcultures of cells dissociated from normal B6CBA-Aw-J-wv (+/+) cerebella, staining with AbGF closely resembled results previously reported for cells taken from C57BL/6J (+/+) tissue. Two forms of stained astroglia were seen, one with a larger perikaryon and shorter processes, among which 12 to 20 unstained cells nestled; and another with a smaller cell soma and longer processes, along which a few unstained cells were seen. The first resembled astrocytes of the internal granular layer and white matter, the second Bergmann astroglia. In microcultures of heterozygous animals (+/wv), the number of granule cells was reduced slightly. Many stained astroglia resembled those from +/+ cerebella, but others had thickened processes and enlarged terminal "endfeet." Granule cells associated with both forms of stained astroglia. Cultures from homozygous weaver (wv/wv) cerebella contained very few, if any, granule cells and did not exhibit specific neuronal/glial interactions characteristic of +/+ cells. Both forms of stained wv/wv glial cells had enlarged cell somata giving rise to stunted processes, suggesting that both Bergmann glia and astrocytes are affected by the weaver gene. By both immunocytochemical staining and electron microscopy, accumulation and tangling of glial filaments were seen. Immunocytochemical staining of weaver cerebellar tissue with AbGF also revealed abnormalities in astrocytes of the internal granular layer and white matter in addition to previously reported defects in Bergmann glia. Agglutination with five plant lectins, each with a different carbohydrate-binding specificity, revealed that postnatal weaver cerebellar cells agglutinate with the lectins concanavalin A and the wheat germ agglutinin, suggesting the persistence postnatally of embryonic cell surface elements on postnatal weaver cells.

Animals↗
PubMed1997

[False positive FDP test associated with malignant lymphoma].

We present a man with non-Hodgkin's lymphoma who had false positive FDP test results and who had monoclonal IgM and IgG. At admission, laboratory examinations showed elevated FDP levels and prolonged PT and APTT, which did not improve by anti-coagulation therapy. Although coagulation system data returned to normal levels after steroid pulse therapy, the FDP level increased. Positive pregnancy test and results of dilution analyses on FDP assay yielded a diagnosis of false positive FDP test results due to serum latex agglutinin. The addition of anti-immunoglobulin antibody inhibited latex agglutination by serum. FDP levels positively correlated with serum IgM concentrations. These data suggest that the false positive FDP test in this case was due to latex agglutination by monoclonal IgM.

Connectin↗
PubMed1976

[Study of the action of phytohemagglutinin on continuous human cells].

A study was made of the agglutinating and growth-stimulating properties of phitohemaagglutinin (PHA) preparations in experiments on continuous human cells (clone line HeLa k-41 and CaVe). PHA and PHA gamma-globulin fraction possessed poor hemagglutination properties against human erythrocytes of A, B and O groups, but expressed marked cytoagglutination properties against HeLa k-41 and CaVe cells. With high PHA doses (100 and 500 microng/ml) proliferation and mitotic indx of the culture cells was lower and the percentage of dead cells and the agglutinin titre in the preparations was greater (1 : 256). With lower PHA doses (5 and 25 microng/ml) the growth was much stronger and the percentage of dead cells lower. The agglutinin titre in the preparations decreased to 1 : 16-1 : 32. PHA gamma-globulin fraction produced the strongest growth-stimulating action with the least amount of dead cells. However, the agglutinin titre in the preparations remained high (1 : 128). A conclusion was drawn that the action of PHA preparations stimulating and inhibiting the growth of continuous human cells proved to be directly connected with the agglutinin content in the preparations, since gamma-globulin PHA fraction expressed the greatest cytoagglutinating and growth-stimulating action.

Agglutination Tests↗
PubMed1976

Saccharides on teratocarcinoma cell plasma membranes. Their investigation with radioactively labelled lectins.

We have studied the interaction of five lectins differing in their sugar specificity, with the surface of clonal cell lines derived from transplantable murine teratocarcinoma. The results show that the differentiation from primitive embryonal carcinoma cells into parietal yolk sac cells is accompanied by changes in cell surface saccharides. These changes consist of a marked decrease in the total number of binding sites for the L-fucose-specific lectin of Lotus tetragonolobus and a large increase in the total number of binding sites for wax bean agglutinin. It is suggested that these differences can be used as markers in the study of this early embryonic differentiation. No agglutination of primitive embryonal carcinoma cells or of parietal yolk sac cells by low concentrations (10mug/ml) of concanavalin A, soybean agglutinin or the fucose binding proteins was observed.

Binding Sites↗
PubMed2003

Seroepidemiology of Toxoplasma gondii in dogs in Trinidad and Tobago.

A cross-sectional study was conducted to determine the seroprevalence of Toxoplasma gondii agglutinins and to investigate the relationship between various risk factors and occurrence of toxoplasmosis in dogs in Trinidad. Of a total 250 dogs, comprising domestic, hunting and stray dogs, 80 (32.0%) were positive for T. gondii agglutinins at a titre of > or =1:32 using a latex agglutination test. Stray dogs (60.5%) had statistically significantly higher (P<0.001) seroprevalence for toxoplasmosis than hunting dogs (30.5%) and domestic dogs (25.5%). Amongst dogs whose ages were known, the prevalence of toxoplasmosis was significantly highest (P=0.037) in dogs in the >2-3 years age group compared with other age groups. Dogs that consumed home-cooked foods had a seroprevalence of 32.9% compared with those fed commercial dog foods (17.2%) and dogs fed both home-cooked and commercial foods (21.0%). However, the difference was not statistically significant (P>0.05; chi(2)). The rather high prevalence of toxoplasmosis in stray dogs is a good indication of the extent of the infection in the environment.

Age Factors↗
PubMed1983

Purification of peanut agglutinin by affinity chromatography on asialoglycophorin from human erythrocytes.

A simple and efficient method of purification of peanut agglutinin is described. This method involves affinity chromatography on human asialoglycophorin linked to Affi-Gel. One milliliter of the packed adsorbent contained 1.7 mg of covalently linked asialoglycophorin and bound about 6 mg of the peanut agglutinin. From 250 g of row peanuts 510 mg of the electrophoretically homogeneous lectin with high agglutinating activity was obtained.

Asialoglycoproteins↗
PubMed1997

Inverse correlation between IgG-antihinge region and antierythrocyte autoantibody in chronic benign and malignant cold agglutination.

Previous reports provided evidence of an immunosuppressive role of natural anti-F(ab')2 antibodies. If suppressive anti-F(ab')2 antibodies also regulated the autoantibody production in cold agglutination, one would expect high titers of anti-F(ab')2 to be associated with low titers of cold agglutinins. Indeed, our previous studies revealed an inverse correlation between IgG-anti-F(ab')2 and cold agglutinins. Many previous experiments focused on anti-F(ab')2 of an antiidiotypic nature. Recent epitope mapping showed that anti-F(ab')2 of healthy persons is not an antiidiotype but recognizes a hinge region sequence. We attempted to answer the question whether this IgG-antihinge antibody is responsible for the previously described association between anti-F(ab')2 and cold agglutinins. IgG-antihinge and IgG-anti-F(ab')2 antibody was determined and statistically analyzed in the serum of 334 patients with cold agglutination. Our experiments revealed a strong correlation between the concentrations of antihinge and the previously described anti-F(ab')2 antibody. The anti-F(ab')2 activity was competitively inhibited by a synthetic hinge peptide. Moreover, patients with high antihinge titers had low cold agglutinin titers, and vice versa. A stratification according to cold agglutinin specificity and disease etiology showed that the inverse correlation is present only in anti-I and anti-i patients suffering from monoclonal B-lymphocyte proliferation. In conclusion, our results confirm the correlation previously described for anti-F(ab')2 antibody and antierythrocyte autoantibody and define for the first time an association between an idiotype-independent anti-IgG autoantibody and cold agglutinin.

Adult↗
PubMedDate not supplied

Anti-Sdx: a "new" auto-agglutinin related to the Sda blood group.

Two examples of a "new" IgM saline-agglutinating auto-antibody are described. The antibodies bind complement, have the ability to cause in vivo hemolysis, and are most active at room temperature at a pH of about 6.5. Despite tests on more than 5,000 people, no nonreactive cell sample has been found. The reactive antigen is not denatured by neuraminidase, papain, or ficin, and is present on i adult red blood cells. The antibodies appear to be slightly inhibited by human saliva and milk, and more convincingly inhibited by urine from Sd(a+) persons. They are not inhibited by urine from Sd(a-) persons, but are strongly inhibited by guinea pig urine. The serologic characteristics indicate a relationship to the Sda blood group and the auto-antibody has been named antiSdx. Sdx antigen is present on red blood cells from some higher primates and is absent from rabbit, rhesus monkey, dog and sheep cells.

ABO Blood-Group System↗
PubMed1981

Participation of pili and cell wall adhesion in the yeast agglutination activity of Escherichia coli.

Escherichia coli strain 2699 (O6:K13) which had been isolated from a case of urinary tract infection exhibited pili during the stationary phase (24 to 40 h), but not during the exponential phase (4 h), when grown in static broth culture. The bacteria were also piliated when grown for 24 h on agar. They agglutinated Saccharomyces cerevisiae (baker's yeast) in the piliated as well as in the nonpiliated state. The agglutinations were mannose sensitive, i.e., they could be inhibited with 50 mM methyl-alpha-mannoside. The bacteria were first depiliated by shearing and then used for the isolation of outer membrane vesicles with an Omnimixer. Purified pili and outer membranes were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electron microscopy. The pili could be demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis only after treatment at low pH or in saturated guanidine hydrochloride which is typical of the common type 1 pili. Depiliated bacteria, purified pili, and purified outer membranes gave mannose-sensitive agglutination of S. cerevisiae. The findings are discussed with respect to possible mechanisms of cell agglutination.

Agglutinins↗
PubMed1975

Sperm antibodies in serum and seminal plasma.

The relation between sperm antibodies (agglutinins and IF-antibodies) in serum and seminal plasma was studied in three selected groups of male partners in infertile couples with respect to specificity, concentrations and immunoglobulin classes. Agglutinins were found in seminal plasma only when they were also present in serum, but there was no strict correlation between the titres in seminal plasma and serum although serum titres were always the higher ones. However, in cases with tail-to-tail agglutinins a difference of more than 2 fourfold steps between the titres was never found; spontaneous agglutination in the ejaculate generally occurred when the seminal plasma titre was 64 or more, and in 6 patients with high seminal plasma titres IgA was detected in the midpiece region of ejaculated spermatozoa. In contrast, head-to-head agglutinins were found in seminal plasma in only one of 3 patients with these agglutinins in serum, and only in a low titre. Absorption of IgG of IgG with protein-A-producing Staphylococcus aureus showed that tail-to-tail agglutinins in serum were IgG antibodies, whereas they could be characterized as "non-IgA-in seminal plasma, suggesting a local production of these antibodies. IF-antibodies were rarely found in seminal plasma and seemed to be of little significance in relation to infertility in men.

Adult↗
PubMed1986

Lectin binding by eosinophils.

Lectins which identify carbohydrates and glycoproteins have been used to characterize specific components of the surface of guinea pig peritoneal exudate eosinophils. Agglutination of eosinophils purified by discontinuous metrizamide gradients was scored microscopically. Wheat germ agglutinin (WGA) was most effective (0.05 micrograms/ml). However, higher concentrations of soybean lectin and concanavalin A (Con A) were also effective. No differences in lectin binding were noted between eosinophils harvested from uninfected animals, Trichinella spiralis-infected animals, or animals receiving weekly intraperitoneal injections of polymyxin B. Neuraminidase pretreatment to remove surface sialic acid reduced agglutination by WGA. Eosinophils did not adhere to WGA-coated Sepharose beads; however, they did adhere to Con A-coated beads. Pretreatment with neuraminidase did not affect the adherence of eosinophils to plastic surfaces, suggesting that sialic acid does not play an important role in adherence. Formation of lectin-inhibitor complexes within the incubation mixture complicated interpretation of studies of binding to plastic surfaces. These studies demonstrate that lectin binding sites are present on the surface of eosinophils. Lectin-type binding may be important in interactions between eosinophils and noningestible parasites.

Agglutination↗
PubMed1975

[Immunization experiments for producing antibody-like substances in caterpillars of Mamestra brassicae L. (Insecta, Lepid., Noct.)].

The agglutinins against human blood cells described in caterpillars of Mamestra brassicae L. were not demonstrable when feeding the animals with a semisynthetic food. After injection or oral intake of certain bacteria (E. coli or streptococci of group C) or even Pope's broth the "antibody-like substances" known from feeding with natural food are being formed, and they agglutinated all human blood cells. The individual animals showed differences regarding the strength of agglutinin formation. The immune reactions observed possibly indicate the existence of a primitive immune system in these species (arthropods).

Agglutination↗
PubMed1988

The identification of membrane glycoconjugates in Leishmania species.

The membrane glycoconjugates of 8 different species of Leishmania were compared by lectin blotting. Five different lectins with various sugar specificities were examined: concanavalin A, Lens culinaris, Ricinus communis, soybean agglutinin, and peanut agglutinin. Concanavalin A and Lens culinaris reacted with every Leishmania tested. The patterns observed for these 2 lectins, as well as the various species of parasites, were different. However, a common 41,000-52,000 and a 160,000-185,000 Mr component was present in almost all the parasite isolates examined. Ricinus communis only recognized a nondiscrete galactose-containing glycoconjugate similar to Leishmania-excreted factor. Soybean and peanut agglutinins reacted with a few low molecular weight parasite components. Soybean agglutinin reacted with all the Leishmania species tested, whereas peanut lectin only recognized 3 isolates. The latter lectin bound to discrete components migrating with the dye front and with Mr's of 35,000 and 52,000. Increased glycosylation was noted on avirulent L. major promastigotes and was associated with the appearance of several new peanut agglutinin-binding glycoproteins.

Agglutination↗