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PubMedDate not supplied

Modification of the slide agglutination test for the detection of sperm-agglutinins.

We have modified the slide agglutination test (SAT) in order to make it available for the routine detection and titration of sperm agglutinins. Serum and seminal plasma samples of 156 subfertile patients were tested by the modified slide agglutination test (MSAT) in two trials. Fifteen per cent of serum and 7.5% of siminal plasma samples gave positive results and MSAT showed excellent reproducibility: a highly significant statistical correlation between the positive titres in the two determinations was observed. One hundred and ten samples were tested simultaneously by the MSAT and the tray agglutination test (TAT). The two tests showed a similar sensitivity with a significant statistical correlation between the positive titres. Using the MSAT the reading of results was easier and more precise. Therefore we propose the MSAT for the routine detection and titration of sperm-agglutinins.

Humans↗
PubMed1988

Purification and characterization of an agglutinin from mucus of the snail Achatina fulica.

The mucus of the snail Achatina fulica shows the presence of an agglutinin that nonspecifically agglutinates human erythrocytes. The agglutinin has been purified by affinity chromatography using Sepharose 4B-hog gastric mucin as the affinity matrix. Homogeneity was checked by polyacrylamide gel electrophoresis, immunodiffusion, immunoelectrophoresis, and gel filtration. The agglutinin is a glycoprotein of native molecular weight 70,000. The isoelectric point of the protein was found to be 8.0. The predominant amino acids are aspartic acid and glutamic acid (or amides) and serine, which account for 32% of the total amino acid residues. The agglutinin has 10% carbohydrate (wt/wt) and the most abundant sugar is N-acetylglucosamine. The cd spectra of the agglutinin show the presence of random coil conformation. The inhibition of hemagglutination data indicates that the agglutinin is specific for beta glycosides of D-Gal and D-GalNAc.

Agglutinins↗
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

Serological diversity in Haemophilus somnus.

Serological interrelations among 46 strains of Haemophilus somnus of various geographical and pathological origins were studied by agglutination and agglutinin adsorption procedures. Sera prepared against nine representative American and Swiss isolates agglutinated all other strains to various titers. Adsorption of antisera to American strains by Swiss cultures tended to remove mainly the reactivity with Swiss antigens, whereas adsorption of such antisera to American strains in most instances abolished all agglutinating activity. Analogous observations were made when sera against Swiss cultures were adsorbed with cells of American and Swiss origin, respectively. Results of tests involving unadsorbed and adsorbed sera suggest the existence of at least three sets of antigen in H. somnus: American, Swiss, and common, which appear to exist in various combinations, accounting for four agglutination groups. These reflect to a considerable degree the geographical, although not the pathological or anatomical, origin of the respective strains.

Agglutination Tests↗
PubMedDate not supplied

Metacyclogenesis of Leishmania (Viannia) braziliensis in vitro: evidence that lentil lectin is a marker of complement resistance and enhanced infectivity.

Axenic culture in modified Grace's medium was used to induce metacyclogenesis of Leishmania (Viannia) braziliensis in vitro. Morphological characteristics, lectin agglutination profiles, susceptibility to complement lysis, and infectivity in vivo were compared between metacyclic promastigotes and promastigotes in mid-log phase growth. Short, arrow-like promastigotes and round, oval promastigotes were defined as putative metacyclic forms on the basis of being highly motile and free swimming, with a small cell body and long flagellum. These forms increased during metacyclogenesis to > 80% whereas long-bodied, slender promastigotes and intermediate slender promastigotes declined progressively. Lentil lectin selectively agglutinated L. braziliensis after the induction of metacyclogenesis, whereas concanavalin A, wheat germ agglutinin and peanut agglutinin similarly agglutinated metacyclic promastigotes and mid-log phase promastigotes. Metacyclic promastigotes survived in 7.5%-20% human serum whereas mid-log phase promastigotes did not. Five hundred metacyclic promastigotes were highly infective to hamsters whereas 500 mid-log phase promastigotes rarely caused any lesion. Specific agglutination by lentil lectin should allow purification of metacyclic organisms for standardization of immunoprotection and challenge experiments.

Agglutination↗
PubMed1992

A hemagglutinating substance in chitin.

Chitin from crustacean shells has often been used to isolate and purify plant lectins that have an affinity for poly-N-acetylglucosamine (poly-GlcNAc). When we used washed chitin from crab shells as an affinity medium to isolate a lectin from Pinus strobus L. (eastern white pine) ovules, we found that a substance having a strong capacity to agglutinate red blood cells was eluted from the chitin during a weak acid desorption step. The chitin agglutinin is a complex structure containing protein and poly-GlcNAc. Chitin samples from four biochemical suppliers were tested; all contained the elutable agglutinin. Acid (0.05 N HCl or 0.1 N acetic acid) appears to hydrolyze the material from the solid chitin. NaOH at 0.5 N does not remove the agglutinin. Since agglutination is the assay used to monitor lectin purification, care must be taken to avoid the native agglutinin if chitin is used as an affinity matrix.

Acetylglucosamine↗
PubMed1994

Conversion of egg-white lysozyme to a lectin-like protein with agglutinating activity analogous to wheat germ agglutinin.

Oligomers made of Asp-52-esterified lysozyme or native one showed agglutination for human, mouse, rat and chicken erythrocytes, and also for Hep G2 cells (liver carcinoma-derived cell line) [1] not weaker than wheat germ agglutinin (WGA). Oligomers of Asp-52-esterified lysozyme have about 4-fold stronger agglutinating activity than those of the native one. These results indicate that some enzymes can be converted to lectin-like proteins (neolectin) with binding characteristics similar to their substrate specificity.

Animals↗
PubMed1982

Differentiation of coagulase-positive and coagulase-negative staphylococci by lectins and plant agglutinins.

The screening of staphylococci with a panel of 14 lectins and extracts demonstrating lectin-like activity led to the development of a rapid agglutination slide test for the differentiation of certain coagulase-negative staphylococci and human strains of Staphylococcus aureus. The coagulase-negative staphylococci were agglutinated by agglutinins from Mangifera indica, Triticum vulgaris, and crude Limulus polyphemus. The test is rapid, requiring only 5 to 15 min to identify an unknown strain of staphylococci, as opposed to the 4 to 16 h required to perform the conventional tube coagulase test.

Agglutination Tests↗