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PubMed1979

Serotyping of Serratia marcescens: simplified tube O-agglutination test and comparison with other serological procedures.

A simplified tube O-agglutination test was developed and evaluated for the determination of somatic serogroup (O) antigens of Serratia marcescens. Use was made of Tryptic Soy broth (TSB)-grown O-cells that had been boiled for 1 hour; 0.145 M NaCl proved a satisfactory diluent. Various technical parameters of this test were examined as well. Rabbit anti-O immune sera, that had been elicited with 5 x concentrated, TSB-grown, 1 hour-boiled O-cells of all 15 currently employed O-antigen reference strains of S. marcescens yielded satisfactory O-agglutinin titers. The tube O-agglutination test compared favorably with the indirect hemagglutination technic, although the latter technic yielded significantly higher O-agglutinin titers with merely 7 of the 15 O-antigens of S. marcescens. The tube O-agglutination test permitted detection of higher O-agglutinin titers than a microtiter O-agglutination test utilizing O-cells that had been stained with safranin O. Conversely, titers obtained with TTC-stained O-cells in a microtiter agglutination procedure approximated those yielded by the tube O-agglutination test, but O-cells of the various S. marcescens strains were stained nonuniformly by triphenyltetrazolium chloride (TTC). As before, there existed marked serologic cross-reactivity between O-antigens O6 and O14. A new O6 candidate strain, S. marcescens isolate S 1i, serotype O6:H20, was proposed. Contrary to O-agglutinins of human control serum, the O-agglutinins of rabbit anti-O immune sera proved refractory to treatment with 0.1 M of 2-mercaptoethanol (2-ME) and 0.01 M dithiothreitol (DTT) respectively. Dual absorptions of rabbit anti-O immune sera with killed cells of Staphylococcus aureus Cowan I (protein A), failed to significantly reduce O-agglutinin titers, although human IgG and IgM was bound by protein A. It was tentatively concluded that the 2-ME- and DTT-refractory rabbit anti-S. marcescens O-agglutinins resided in the IgM immunoglobulin class.

Agglutination Tests↗
PubMed1992

Maturation-dependent goat epididymal sperm autoagglutination and its inhibition by a glycoprotein factor.

The maturing goat epididymal spermatozoa were isolated from different segments of epididymis and these cells dispersed in a modified Ringer's solution, were incubated at 37 degrees C for 60 min to evaluate their autoagglutination efficacy. Distal corpus-epididymal spermatozoa specifically showed high order of head-to-head autoagglutination property whereas all other sperm cells did not show any detectable aggregation. The goat epididymal plasma has been shown to possess an anti-agglutinin that markedly inhibits sperm agglutination phenomenon and also dissociates the cells from the sperm clusters. Epididymal plasma is the most potent source of the anti-agglutinin which is a heat-stable specific glycoprotein. Like the autoagglutination phenomenon, the initiation of sperm forward progression also starts in the distal-corpus epididymis. The temporal correlation of these two events suggests that sperm autoagglutination may be a prerequisite for the induction of flagellar motility during the epididymal maturity of male gametes.

Agglutination↗
PubMed1976

Surface morphology and agglutination of lectin-treated human lymphocytes and lymphoblasts.

Two human lymphoblasts (Raji and EB3) and normal human peripheral lymphocytes were exposed to different concentrations of Concanavalin A and wheat germ agglutinin. The lectin-induced agglutination was determined and correlated with lectin-induced changes in the surface morphology of these cells as studied in a scanning electron microscope. Whenever the lectin induced high agglutinability in a cell type, it also invariably had a smoothing effect on the cell surface. In contrast, when cells did not agglutinate well with a certain lectin, their cell surface remained essentially rough (villous) after addition of the lectin. The correlation found between increased agglutinability and altered cell surface morphology upon treatment with certain lectins suggests that both phenomena result from one and the same process. Additional evidence for this postulate is presented.

Agglutination↗
PubMed1965

TAXONOMY OF CLOSTRIDIUM BIFERMENTANS AND CLOSTRIDIUM SORDELLII. 3. AGGLUTINABILITY OF HEAT-RESISTANT SUBSTRAINS OFCLOSTRIDIUM SORDELLII.

Huang, C. T. (Kanazawa University, Kanazawa, Japan), Kenzo Tamai, and Shoki Nishida. Taxonomy of Clostridium bifermentans and Clostridium sordellii, III. Agglutinability of heat-resistant substrains of Clostridium sordellii. J. Bacteriol. 90:391-394. 1965.-By cross-agglutination tests with Clostridium bifermentans and C. sordellii antisera, the heat-resistant substrains from each pathogenic strain of C. sordellii were found to possess antigens of C. bifermentans in addition to displaying changes in biological activities. The agglutinability and biological activities varied with the sporulating potency acquired. Agglutinin-absorption tests further proved that heat-resistant substrains of C. sordellii were immunologically identical to C. bifermentans.

Agglutination↗
PubMed1983

Pseudothrombocytopenia with cold-type platelet agglutinins.

Pseudothrombocytopenia is an in vitro phenomenon of platelet agglutination and clumping in the presence of EDTA on the electronical measurement of platelet count. Agglutinins reacting with platelet antigens belong to one heavy and one light chain of immunoglobulins with or without complement by immunofluorescence. The platelets are markedly agglutinated in EDTA, but scarcely in the presence of other anticoagulants. Agglutinations seem to occur more readily at cold temperature rather than at 37 degrees C.

Agglutinins↗
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↗
PubMed1990

[Apropos of 2 cases of hemolytic anemia in mycoplasma pneumonia].

The authors present 2 cases of mycoplasmal pneumonia associated with severe haemolysis. Haemolytic anaemia is a well-known and habitually mild complication of the disease. It is related to a peak of cold agglutinins, which are antibodies that agglutinate red blood cells usually at low temperatures but sometimes at 37 degrees C when they are present in high concentrations. The pathogenesis of cold agglutinins is thought to involve the secretion of peroxides by Mycoplasma pneumoniae with alteration of ed cell antigens which become immunogenic.

Adult↗
PubMed1980

Induction and separation of mouse helper T cells by lectins.

The capability of Lens culinaris agglutinin (LcA) to induce selectively the helper T cell activity affecting primary antibody response was demonstrated. In the presence of mouse spleen cells, activated with LcA at a concentration of 12 . 5 microgram/ml, optimal augmentation of the humoral immune response to sheep erythrocytes (SRBC) was observed. It was also demonstrated that Limulus polyphemus agglutinin (LPA), which was shown to possess carbohydrate-binding specificity directed to sialic acid residues, preferentially agglutinated helper T cells. Conversely, peanut agglutinin (PNA), which binds preferentially to the sugar sequence beta-D-Gal-(1 leads to 3)-D-GalNAc, did not agglutinate the helper cells. Furthermore, the stimulatory effect of LPA-agglutinated cells on the antibody response was abolished by treatment of the cells with anti-Thy-1 . 2 and complement. These results suggested that the helper cells induced by LcA were T cells and that they have abundant sialic acid residues exposed on the cell surface.

Animals↗
PubMed1979

Studies on anti-B specificity and heterogeneity of some invertebrate hemagglutinins.

Hemolymph from Charybdis japonica and Lymantria dispar, and saline extract from Eunice kobiensis agglutinated human group B erythrocytes specifically. Multiple agglutinins were identified, and independent agglutinins were separated from hemolymph of Charybdis japonica (anti-Bcj+anti-Xcj) and Lymantria dispar (anti-BLD+RLD) by absorption experiments. By the agglutination and agglutination-inhibition experiments with simple sugars, the specificities of the anti-B agglutinins in these invertebrates were found to differ from each other.

ABO Blood-Group System↗
PubMed1976

The cell surface of Trypanosoma musculi bloodstream forms. II. Lectin and immunologic studies.

Living Trypanosoma musculi bloodstream trypomastigotes were agglutinated specifically with concanavalin A (ConA), wheat germ agglutinin (WGA), soybean agglutinin (SBA), and fucose-binding protein (FBP). The agglutination with these lectins of living cells from which the coat was removed by trypsinization was the same as with intact trypanosomes. Glutaraldehyde or formalin fixation did not affect the results with regard to agglutination with WGA, SBA, and FBP, but lower agglutination with ConA was observed upon fixation. By using a dense iron-dextran marker many fewer ConA marker particles were localized at the fine structural level in the intact than in trypsin-treated trypanosomes. On the basis of the results obtained by agglutination and electron microscopy, it is likely that fixation cross-links intact surface-coat components associated with the ConA binding sites. It is evident from the studies in which lectins were employed that ligands containing alpha-D-mannose, N-acetylglucosamine, N-acetylgalactosamine, and alpha-L-fucose are randomly distributed in the outer surface of the pellicular and flagellar membranes of T. musculi trypomastigotes. Results obtained with alpha-amylase- and dextranase-treated trypanosomes suggested that lectin-binding sugar ligands in the cell surface were not directly associated with alpha-1,4 or repetitive alpha-1,6 glucan-bonded polysaccharide moieties. Similar conclusions can be drawn on the basis of neuraminidase treatment with regard to N-acetylated neuraminic acids. After thorough washing, intact, but not trypsin-treated trypomastigotes were agglutinated specifically with antisera against whole mouse serum and against mouse IgG. Evidently, adsorbed constituents of mouse serum are regular components of the T. musculi surface coat. After incubation in dilute whole mouse serum or in mouse IgG solutions, also the trypsinized cells were agglutinated by the 2 antisera. No such results were obtained with trypsinized cells incubated in serum-free buffers. It was concluded that mouse serum proteins were readily readsorbed on, and firmly bound to the trypsinized cells' surfaces. Specific agglutinations were obtained with trypsinized cells after incubation in dilute rat, rabbit, bovine, and human sera and in solutions of rat and rabbit IgG in reactions with the corresponding antisera. It seems, therefore, that the host serum proteins are adsorbed nonspecifically to the cell surface of trypsinized T. musculi bloodstream forms. When examined by electron microscopy, the intact trypomastigotes were covered by an ununiform, slightly granular, fibrillar extracellular coat, applied to the entire outer lamina of the pellicular and flagellar membranes. No indication of such a coat was noted in the trypsinized organisms. Flocculent surface coat-like matrix could, however, be discerned in cells which, after trypsinization, were incubated in various sera.

Agglutination↗
PubMed1987

Lectin agglutination of thermophilic Campylobacter species.

Agglutination tests with lectins indicated differences in the surface composition of strains of the thermophilic (optimum temperature 42 degrees C) Campylobacter species C. coli, C. faecalis, C. hyointestinalis, C. jejuni and C. laridis. All strains examined were agglutinated by the protein-reactive agglutinins of Mangifera indica (mango) and Persea americana (avocado) and a large proportion was also agglutinated by the carbohydrate-reactive lectins of Canavalia ensiformis (Jack bean) and Triticum vulgaris (wheat germ). Reactions with other lectins varied widely between strains, even of the same species and serotype. Lectin agglutination may be useful as a supplementary procedure for characterizing individual Campylobacter isolates for epidemiological purposes.

Agglutination Tests↗
PubMed1983

Characterization of a salivary agglutinin reacting with a serotype c strain of Streptococcus mutans.

A protein, which can agglutinate a Streptococcus mutans serotype c strain, was isolated from parotid saliva by affinity adsorption of the salivary agglutinin to the microorganism followed by a desorption with a 10 mM phosphate buffer. The agglutinin was subjected to preparative ultracentrifugation, gel filtration, and ultrafiltration. The native purified agglutinin is active only in the presence of Ca. Polyacrylamide gel electrophoresis, analytical centrifugation, and analyses of amino acids and carbohydrates showed that the native agglutinin was a fucose-rich glycoprotein with a carbohydrate content of 45% and with a molecular weight of at least 5 X 10(6). After sodium dodecyl sulphate treatment the molecular weight was 4.4 X 10(5). There was a low content of proline and a high content of aspartic acid, serine and threonine. The concentration of agglutinin in parotid saliva is less than 0.5% of total protein. It has high biological activity: 0.1 microgram agglutinin causes a rapid aggregation of approximately 10(8) bacteria.

Agglutination Tests↗
PubMed1995

Properties of a blood-meal-induced midgut lectin from the tsetse fly Glossina morsitans.

The properties of a blood-meal-induced lectin (agglutinin) from the midgut of Glossina morsitans capable of agglutinating Trypanosoma brucei were studied in vitro. The midgut homogenate from flies that had been fed twice had the highest agglutination activity, followed by that from the once-fed flies and that from the unfed insects. As compared with the bloodstream-form trypanosomes, a much lower concentration of the midgut homogenate was required for agglutination of the procyclic parasites. Furthermore, the agglutination process was specifically inhibited by D-glucosamine. Soybean trypsin inhibitor abrogated agglutination of the bloodstream-form parasites, whereas the procyclics were unaffected. The agglutination process was temperature-sensitive, with little activity being evident between 4 degrees and 15 degrees C. Similarly, heating the midguts to 60 degrees-100 degrees C led to loss of activity. When the midgut homogenate was separated by anion-exchange chromatography, the agglutination activity co-eluted with trypsin activity at approximately 50% NaCl. These results suggest a very close relationship between midgut trypsin-like enzyme and the agglutinin. Since successful agglutination of bloodstream-form trypanosomes requires protease activity, it may be that the enzyme cleaves off some surface molecules on the parasite surface, thus exposing the lectin-binding sites.

Agglutination Tests↗
PubMed1976

Leptospiral agglutinins in dogs in Sydney.

From June 1971 to June 1972, sera from 600 dogs in Sydney were tested for leptospiral agglutinins by a rapid slide agglutination method. The end-point titre was taken at 50 percent agglutination of the live organisms. Forty-one samples (6.8 percent) had a significant leptospiral titres (100 or greater) and 5 of these reacted to 2 serotypes. Thirty serums (5 percent) contained agglutinins against L. copenhageni, and 6 (1 percent) against L. pomona, while a few samples reacted against hardjo, tarassovi, australis, grippotyphosa or pyrogenes serotypes. No significant titres were found to L. canicola, L. hebdomadis, L. autumnalis or L. bataviae.

Agglutinins↗
PubMed1973

Salmonella dublin abortion in cattle. I. Observations on the serum agglutination test.

The somatic and flagellar serum agglutinin titre were determined in paired samples obtained from seventy-seven cases of bovine abortion associated with Salmonella dublin infection. The cases could be divided into four serological groups with an active infection being demonstrated in most cases. The serum agglutination test was shown to be a relatively specific diagnostic test but was of more limited value in the retrospective identification of convalescent cases.

Abortion, Veterinary↗
PubMed1955

Specific agglutination of Treponema pallidum by sera from rabbits and human beings with treponemal infections.

A method has been described for the preparation of Treponema pallidum suspensions that are suitable for specific agglutination studies and can be stored at 4 degrees C. for months without loss of agglutinability. Such suspensions have been shown to react with two distinct antibodies in the serum of syphilitic animals and man: Wassermann antibody and a specific treponeme agglutinin. It has been demonstrated that the agglutination of treponemes by specific treponeme agglutinin is enhanced by heat treatment or aging of the suspension, and inhibited by a divalent cation, probably Ca(++), normally present in serum. This inhibition has been overcome by the use of a chelating agent, ethylene-diamine tetracetate. These findings have been utilized to devise a simple agglutination test for the diagnosis of treponeme infections that is very sensitive and highly specific. This test has been carried out with 430 human sera, and a comparison has been made of the results of the agglutination, treponemal immobilization, and standard serological tests on these sera. The agglutination test appears to have a specificity comparable to the treponemal immobilization test and considerably greater than the standard serological tests.

Agglutination↗