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PubMed1985

Serological cross-reactions between Brucella abortus and Yersinia enterocolitica 0:9.

Yersinia enterocolitica (Ye) 0:9 is an organism of great significance in veterinary medicine largely as a result of its cross-reaction with Brucella abortus (Ba). Boty Ye 0:9 and Ba possess somatic antigens in common; as a result of which animals exposed to Ye 0:9 have an immune response which is distinguishable only with difficulty from that induced by Ba. Cattle were exposed to Ye 0:9 by the oral or intramammary routes. Oral exposure failed to generate significant serologic response. In contrast, intramammary inoculation produced a marked response. Serum antibodies provoked in this manner reacted strongly with Ba. The anti-Brucella response provoked by inoculation of Yersinia was sufficient to render milk and serum Brucella-seropositive as measured by the standard milk ring and serum agglutination tests. While both Ba and Ye 0:9 have 9 antigens in common, they differ significantly with respect to motility. Thus Ba is always non motile while Ye is motile when grown at room temperature. The presence of Yersinia H agglutinins in serum were shown to be evidence of previous exposure to Ye. The H agglutinins were not generated by Brucella infection. A rapid H agglutination test was shown to provide this differentiation without interference from cross-reacting O antigens. Results of Ba O and Ye O and OH antigens used in the agglutination test were found useful to differentiate antibodies against Ba from those induced by Ye 0:9 in cattle sera. The existence of enterobacterial common antigen (ECA) in Ye and its absence in Ba were utilized in an attempt to provide a method to distinguish Brucella infections from those with cross-reacting Yersinia.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1980

Lectin receptors as markers for Trypanosoma cruzi. Developmental stages and a study of the interaction of wheat germ agglutinin with sialic acid residues on epimastigote cells.

Trypanosoma cruzi at various stages of maturation and differentiation have been isolated by conventional cellular fractionation procedures and characterized by cell surface markers using 30 highly purified lectins encompassing all known sugar specificities. Cell surface carbohydrates of the various T. cruzi stages were analyzed by agglutination and lectin-binding assays. Specific receptors for wheat germ agglutinin (WGA), Helix pomatia, Sophora japonica, and Bandeiraea simplicifolia lectin II were found only in culture epimastigotes, whereas peanut agglutinin (PNA) sites were present exclusively in amastigotes, those for Phaseolus vulgaris in bloodstream trypomastigotes and amastigotes, and for Wistaria floribunda hemagglutinin predominantly in culture forms of T. cruzi. The N-acetylgalactosamine (DGalNAc)-binding lectin from Bauhinia purpurea agglutinated and inhibited the movement of epimastigotes and bloodstream trypomastigotes, but it only inhibited--without agglutinating--culture trypomastigotes. Because both the agglutination and inhibition of movement were reversed by specific sugar haptens, Bauhinia purpurea sites were present in all the flagellated parasites. On the other hand, PNA sites were detectable on epimastigotes after the cells were treated with sialidase, whereas, at the same time, WGA receptors were completely removed and those for the other sialic acid-binding proteins, Aaptos papillata lectin II and Limulus polyphemus, were partially eliminated; moreover, the activity of Wistaria floribunda hemagglutinin, a DGalNAc-binding lectin, increased 4,000 times. Trypsinization and lyzozyme treatment of epimastigote cells did not significantly affect lectin agglutination or lectin binding. WGA reacted solely with sialic acid residues on epimastigote cell surface with an apparent association constant of 2 x 10(6) M-1, each epimastigote having an estimated average of 3 x 10(6) WGA sites, as determined by binding experiments and a minimum of 7.7 x 10(6) sialic acid residues, as calculated by colorimetric method after sialidase digestion. Evidences are presented that the sialyl residues are rapidly regenerated (in approximately 4 h) and that they, at least for the most part, are not adsorbed from the culture medium. The receptor for the D-mannose-binding lectins (concanavalin A [Con A] and Lens culinaris) must either be on the same carbohydrate moiety having the WGA site, or, if in a distinct molecule, both carrier molecules of Con A and WGA sites must be located close to each other in the plasma membrane of the parasite.

Animals↗
PubMed1980

An example of auto-anti-A1 agglutinins.

The serum of an elderly man, group A, Le(a+b-), contained an IgM antibody that agglutinated his own cells and the cells of random group A1 donors. Over a period of 5 months, the titre of these auto-anti-A1 agglutinins was 4 at 22 degrees C.

ABO Blood-Group System↗
PubMed1985

Mannose-resistant hemagglutination and P receptor recognition of uropathogenic Escherichia coli isolated from adult patients.

Adhesions of 211 strains of uropathogenic Escherichia coli and 19 strains of normal fecal E. coli were characterized by patterns of agglutination with human erythrocytes, Saccharomyces cerevisiae, and horse erythrocytes coated with the P blood-group receptor (P). Mannose-resistant (MR) hemagglutination was significantly associated with P agglutination (P less than .001). E. coli expressing MR and/or P (MR/P) agglutinins concurrently with mannose-sensitive (MS) agglutinins predominated in all clinical categories. The highest percentage of E. coli demonstrating MR/P agglutinins, in the absence of MS agglutinins, was recovered from patients with acute pyelonephritis (35%) compared with percentages of patients with chronic pyelonephritis (13%), asymptomatic bacteriuria (16%), cystitis (11%), and normal fecal control E. coli (11%). Sixty-nine percent of E. coli isolates causing acute pyelonephritis agglutinated P-coated horse erythrocytes compared with only 11% of the fecal isolates. Strains expressing MR/P agglutinins (in the absence of MS agglutinins) isolated from patients with acute pyelonephritis, chronic pyelonephritis, and asymptomatic bacteriuria were significantly associated with the presence of antibody-coated bacteria in patients' urine sediments (P less than .010), an observation indicative of an immune response associated with bacterial invasion of host tissues.

Adhesins, Escherichia coli↗
PubMed1985

Alpha mating type-specific expression of mutations leading to constitutive agglutinability in Saccharomyces cerevisiae.

Two mutants of Saccharomyces cerevisiae have been isolated and characterized. The mutants were constitutively agglutinable at 36 degrees C, the temperature at which wild-type cells agglutinate only after induction by mating pheromone. The mutant cells had other properties specific for the normal alpha cell type, i.e., conjugation with a cells, response to a mating pheromone, and production of alpha mating pheromone. The two mutations, cag1 and cag2, were recessive and expressed only in alpha cells. cag1 is linked very closely to the MAT locus, but cag2 is unlinked to the MAT locus. These cag mutations complemented ste3-1. These results indicate that CAG genes are novel alpha-specific genes involved in the regulation of sex agglutinin synthesis.

Agglutination↗
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↗
PubMed1980

Immunochemical characteristics of human anti-T antibodies.

A specific and sensitive radioimmunoassay was developed to investigate the immunochemical properties of serum anti-T antibodies. Evidence was presented that the radioimmunoassay can measure non-agglutinating as well as agglutinating anti-T antibodies, while the hemagglutination method can detect only the latter type. Although the hemagglutination method failed to detect anti-T agglutinins in cord sera, the radioimmunoassay results demonstrated the presence of non-agglutinating antibodies. Presence of 1% polyethylene glycol potentiated some of the originally nonagglutinating antibodies to produce a hemagglutination reaction. Immunochemical characteristics associated with the human anti-T antibodies are discussed.

Agglutinins↗
PubMed1990

Cold agglutinins in cats with haemobartonellosis.

Coombs-positive anemia developed in cats inoculated with Haemobartonella felis. Cold agglutinins were detected in serum during the acute stage of the disease when anemia was present. The cold agglutinating activity was associated with IgM, was demonstrated at 4 C, and was abolished by treatment of sera with 2-mercaptoethanol. At 4 C, the sera from infected cats agglutinated or lysed parasitized autologous erythrocytes or normal erythrocytes pretreated with neuraminidase. These data indicate that cold agglutinins are associated with haemobartonellosis and suggest that immunologic responses to erythrocytic antigens have a role in the anemia.

Agglutination Tests↗
PubMed1976

The passive transfer of humoral immunity from sows infected with Hyostrongylus rubidus (Hassal and Stiles, 1892), the red stomach worm, to their offspring and its significance in the conferring of protective immunity.

Sows repeatedly infected with large single doses of third stage infective Hyostrongylus rubidus larvae show an anamnestic circulating agglutinin response to the parasite as detected by the passive haemagglutination reaction. At farrowing the circulating antibody level dropped, whereas the colostral agglutinating antibody level increased for a period of a few hours. The predominant class of immunoglobulin which had agglutinating activity against H. rubidus was IgG. Offspring which had suckled the infected mothers had a demonstrable agglutinin titre 4 days after birth, whereas offspring which suckled non-infected mothers had no demonstable agglutinins. On infection of the offspring, those which suckled infected mothers showed a more rapid and pronounced increase and duration of circulating agglutinins than those which had suckled noninfected mothers. The parasitic burden, as determined by the duration of egg laying and total egg output, was considerably lower for the group reared on the infected mothers. These experiments show that passively transferred agglutinating antibodies, mainly of the IgG class, were associated with protection.

Agglutinins↗
PubMed1984

[Blood groups A and O with a weaker serological reactivity to agglutinins in the serum].

In normal conditions anti-A and anti-B agglutinins are seldom weak and very seldom they are completely absent. Agglutination reaction depends on temperature. It is intensified by treatment of erythrocytes with enzymes (papain) and is also dependent on genotype of the person investigated. Alterations are more frequently observed in anti-B agglutinin. Two cases with defective A and O blood groups are presented, with anti-B agglutinin missing at routine investigation. Treatment of erythrocytes at 4 degrees C with papain indicated the presence of anti-B agglutinin which has a weaker serological expression. Assessment of immunoglobulin concentration by laser nephelometry before and after adsorption and elution, also indicated the presence of this agglutinin.

ABO Blood-Group System↗
PubMed1976

Human agglutinins to rabbit erythrocytes. Characterization of an antigen.

Crude preparations inhibiting the agglutination of rabbit erythrocytes by pooled human serum were obtained by extraction of erythrocyte stromata with various solvents (chloroform/methanol, trichloroacetic acid, and so forth). Highest inhibiting activity was found in a preparation containing sphingoglycolipid; 0.8 mug inhibited 2 agglutinating units of serum. The active preparations retained their activity after 5 min of incubation in a boiling water bath and after treatment with proteolytic enzymes or neuraminidase. Treatment with periodate abolished the activity. The antigenic site is therefore probably determined by the sugars of the sphingoglycolipid.

Agglutination Tests↗