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PubMed1987

Further characterization of the cold agglutinin from the snail Achatina fulica.

The cold agglutinin from the albumin gland of the snail Achatina fulica was purified to homogeneity by using sheep gastric mucin-Sepharose 4B as affinity column followed by gel filtration on Bio-Gel P-300. The homogeneity was checked by alkaline gel electrophoresis, immunodiffusion and immunoelectrophoresis. The purified cold agglutinin is a glycoprotein of native M2 220,000 consisting of three non-covalently bound subunits of Mr 84,000, 74,000 and 62,000 and having a pI value of 4.5. The predominant amino acids are aspartic acid and glutamic acid (or amides) and serine, which account for 39% of the residues. About 3% of the residues are half-cystine. The lectin is a glycoprotein with about 30.7% carbohydrate, the most abundant sugars being galactose, N-acetylgalactosamine and N-acetylglucosamine. Mannose, xylose and fucose are also present. The inhibition of agglutination of human umbilical-cord erythrocytes by the cold agglutinin is specific for methyl beta-D-galactoside and also for glycolipids present on cord erythrocytes. The c.d. data show only negative ellipticity values in the far-u.v. region for the protein at various concentrations and temperatures and also in the presence of the hapten lactose (at different concentrations), indicating the presence of a random-coil conformation in the agglutinin that varies according to temperature.

Agglutinins↗
PubMed2001

Wheat germ agglutinin-binding glycoproteins are decreased in Alzheimer's disease cerebrospinal fluid.

A number of biomarkers (e.g. Abeta, tau) has been identified in Alzheimer's disease CSF. However, none fulfils the criteria of sensitivity and specificity (> 80%) needed for the development of an accurate diagnostic test. The lack of a suitable marker has prompted the search for new CSF biomarkers. In this study, the glycosylation of CSF proteins was examined using lectin blotting. Lumbar CSF was collected ante mortem from 22 non-Alzheimer's disease and 12 probable Alzheimer's disease cases and ventricular CSF collected post mortem from 7 non-Alzheimer's disease and 16 Alzheimer's disease cases confirmed by pathologic examination. When CSF glycoproteins were stained with wheat germ agglutinin (WGA), the staining intensity was found to be significantly lower in the Alzheimer's disease group. No difference in staining was found using other lectins (Canavalia ensiformis agglutinin, Ricinus communis agglutinin, Lens culinaris agglutinin). The measurement of WGA-reactive glycoproteins in CSF may be a useful biomarker for diagnosis of Alzheimer's disease.

Aged↗
PubMed2001

Inhibitory effect of bovine milk lactoferrin on the interaction between a streptococcal surface protein antigen and human salivary agglutinin.

Human whole saliva induces aggregation of Streptococcus mutans cells via an interaction between a surface protein antigen (PAc) of the organism and salivary agglutinin. Bovine milk inhibits the saliva-induced aggregation of S. mutans. In this study, the milk component that possesses inhibitory activity against this aggregation was isolated and found to be lactoferrin. Surface plasmon resonance analysis indicated that bovine lactoferrin binds more strongly to salivary agglutinin, especially to high molecular mass glycoprotein, which is a component of the agglutinin, than to recombinant PAc. The binding of bovine lactoferrin to salivary agglutinin was thermostable, and the optimal pH for binding was 4.0. To identify the saliva-binding region of bovine lactoferrin, 11 truncated bovine lactoferrin fragments were constructed. A fragment corresponding to the C-terminal half of the lactoferrin molecule had a strong inhibitory effect on the saliva-induced aggregation of S. mutans, whereas a fragment corresponding to the N-terminal half had a weak inhibitory effect. Seven shorter fragments corresponding to lactoferrin residues 473-538 also showed a high ability to inhibit the aggregation of S. mutans. These results suggest that residues 473-538 of bovine lactoferrin are important in the inhibition of saliva-induced aggregation of S. mutans.

Agglutinins↗
PubMed1985

Spurious red blood cell parameters due to serum cold agglutinins: observations on Ortho ELT-8 cell counter.

The pattern of spurious red blood cell parameters caused by serum cold agglutinins has been well characterized for the Coulter counters but not the Ortho ELT-8. The pattern consists of a spurious increase in mean corpuscular volume (MCV), a discrepancy between the hemoglobin and the hematocrit, the latter falsely reduced and consequently a MCHC value greater than 36%. Since MCHC rarely exceeds 36% in health or disease, it is an important clue to the spurious nature of the macrocytosis caused by cold agglutinins. The authors have studied five examples of cold agglutinin induced artefact on the Ortho ELT-8 counter. Although a pattern similar to that for the Coulter counters was anticipated, three of the five patients failed to show the characteristics "internal discrepancy" and a MCHC value greater than 36%, despite a marked spurious elevation of MCV. In two of the three patients a classical pattern of cold agglutinin artefact was observed on a Coulter S Plus IV counter with only a modest elevation of MCV. Possible explanations for the observed pattern on the ELT-8 and its implications are discussed.

Adult↗
PubMed1984

Agglutinins to anaerobic bacteria in Crohn's disease and in Indian patients with diarrhoea.

Agglutinins to certain species of Eubacterium and Peptostreptococcus have been reported in sera from a high proportion of patients with Crohn's disease. Because this might be a non-specific finding common to patients with diarrhoea associated with damaged intestinal mucosa, we have compared the incidence of such agglutinins in patients with Crohn's disease with that seen in patients in North-East India with acute or chronic diarrhoea. The incidence of agglutinins in Crohn's disease was 44%, compared with 11% in acute and 17% in chronic diarrhoea. These figures suggest that mucosal damage alone does not explain the high incidence of agglutinins in Crohn's disease.

Adult↗
PubMed2005

Plus and minus sexual agglutinins from Chlamydomonas reinhardtii.

Gametes of the unicellular green alga Chlamydomonas reinhardtii undergo sexual adhesion via enormous chimeric Hyp-rich glycoproteins (HRGPs), the plus and minus sexual agglutinins, that are displayed on their flagellar membrane surfaces. We have previously purified the agglutinins and analyzed their structural organization using electron microscopy. We report here the cloning and sequencing of the Sag1 and Sad1 genes that encode the two agglutinins and relate their derived amino acid sequences and predicted secondary structure to the morphology of the purified proteins. Both agglutinin proteins are organized into three distinct domains: a head, a shaft in a polyproline II configuration, and an N-terminal domain. The plus and minus heads are related in overall organization but poorly conserved in sequence except for two regions of predicted hydrophobic alpha-helix. The shafts contain numerous repeats of the PPSPX motif previously identified in Gp1, a cell wall HRGP. We propose that the head domains engage in autolectin associations with the distal termini of their own shafts and suggest ways that adhesion may involve head-head interactions, exolectin interactions between the heads and shafts of opposite type, and antiparallel shaft-shaft interactions mediated by carbohydrates displayed in polyproline II configurations.

Agglutinins↗
PubMed1978

Inhibition of human anti-Gd cold agglutinins by sialyllactose.

Two examples of IgM kappa-monotopic cold agglutinins occurring in patients with non-Hodgkin lymphomas, reacted with erythrocyte autoantigens, which were protease-resistant but were inactivated by neuraminidase. The cold agglutinins were inhibited by the trisaccharide sialyllactose [NeuNAc(alpha,2 leads to 3) Gal (beta, 1 leads to 4)Glc], which is not related to oligosaccharides known to inhibit anti-I/-i cold agglutinins, Anti-Pr cold agglutinins are not inhibited by sialyllactose, although N-acetylneuraminic acid (NeuNAc) is an essential component not only of Gd but also of Pr determinants. Gd determinants are not bound to erythrocyte membrane glycoproteins, but are apparently bound to membrane glycolipids (gangliosides).

Agglutinins↗
PubMed1978

Variation of cold agglutinin levels.

Cold agglutinin levels were determined in 120 individuals ranging in age from 1 to 64 years using untreated and ficin-treated group O erythrocytes. The geometric mean titer for untreated cells was 5.7 +/- 1.1 SEM and for ficin-treated cells 18.7 +/- 1.1 SEM. The mean titers and scores for various blood groups were not significantly different. Titers and scores correlated significantly to total serum IgM concentration (p less than 0.001). Females had significantly higher cold agglutinin levels than males (p less than 0.001). A significant decrease of cold agglutinins occurred in the 26- to 64-year age group as compared to the 11- to 25-year age group (p less than 0.01). The data should contribute to a clearer understanding of the biological impact of cold agglutinins.

Adolescent↗
PubMed1985

A combination of IgG and IgM autoantibodies in chronic cold agglutinin disease: immunologic studies and response to splenectomy.

A patient with chronic cold agglutinin disease and anti-I antibody was studied. The titer of the patient's serum at 4 degrees C was 700 with adult I RBC, 256 with cord RBC, 256 with adult i RBC. At room temperature the titers were decreased and the serum also reacted at a titer of 4,000 with enzyme treated adult I RBC. Dithiothreitol treatment of the serum and purified antibody decreased reactivity only slightly, indicating that the antibody was IgG. The heat eluate contained 1.2 mg/ml IgG kappa, but only 80 micrograms/ml IgM kappa. A hybridoma made by fusing the patient's peripheral blood lymphocytes with a human myeloma cell line contained only IgM kappa (30 micrograms/ml) anti-I activity. The IgM fraction of the heat eluate reacted similarly to the hybridoma supernatant. The IgG fraction resembled the serum and heat eluate. In this case study, IgG kappa and IgM kappa immunoglobulins, both possessing cold agglutinin activity, were present in the patient's serum. This finding is unusual in idiopathic cold agglutinin disease and in view of the predominance of an IgG cold agglutinin, splenectomy was recommended for treatment.

Adult↗
PubMed1993

Identification of a salivary agglutinin-binding domain within cell surface adhesin P1 of Streptococcus mutans.

DNA encoding the alanine-rich region (A-region) of the cell surface adhesin, P1, from Streptococcus mutans was subcloned and expressed as a fusion protein with the maltose-binding protein (MBP) of Escherichia coli. The A-region fusion protein was shown to competitively inhibit both adherence of S. mutans to salivary agglutinin-coated hydroxyapatite and fluid-phase agglutinin-mediated aggregation of this organism. MBP alone or an MBP-paramyosin fusion protein was not inhibitory. Proteolytic cleavage of the fusion protein into its component moieties, MBP and A-region, resulted in breakdown of the A-region into three main fragments. Western immunoblot analysis of calcium-dependent agglutinin binding to this preparation revealed binding specificity for a 28-kDa fragment. Thus, the A-region of P1 is an important domain which interacts directly with salivary agglutinin, and this interaction interferes with both the aggregation and the adherence mechanisms in vitro.

Adhesins, Bacterial↗
PubMed1987

Interaction of alpha-agglutinin with Saccharomyces cerevisiae a cells.

Binding of Saccharomyces cerevisiae alpha-agglutinin to target a cells was assayed by agglutination inhibition and 125I-alpha-agglutinin binding. The assays showed characteristics of equilibrium binding, namely saturability, competability, and the establishment of a kinetic endpoint in the presence of free alpha-agglutinin and free receptor. The binding was heterogeneous, displaying strong binding (10(9) liters/mol) and a weaker interaction. There were about 2 X 10(4) strong binding sites per a cell. Denaturing gels displayed identical labeled species binding to the a cells in the weak and strong interactions. Furthermore, weakly bound material could subsequently bind tightly to fresh a cells, implying that the same species of alpha-agglutinin was bound in the two states.

Agglutination↗
PubMed1983

Pseudothrombocytopenia and IgA-related platelet agglutinin in a patient with IgA nephritis.

A 41-year-old female was evaluated for asymptomatic proteinuria and thrombocytopenia. The renal biopsy disclosed mild to moderate mesangial proliferation, and the immunohistology showed granular deposition of dominant IgA and C3 in the mesangium, which is consistent with IgA nephritis. Thrombocytopenia was EDTA-dependent pseudothrombocytopenia type 1. Heparinized blood restored the platelet count to normal. Serological examinations revealed that the platelet agglutinin was IgA, and the platelet clumping required both EDTA and IgA-related agglutinin. Thus, the present case adds the combination of IgA nephritis and pseudothrombocytopenia to the spectrum of the so-called thromborenal syndrome. In view of recent findings that platelet agglutinins belong to immunoglobulins or fractions, occurring frequently in a variety of immunologically abnormal situations, IgA-related agglutinin as seen in this patient may have more than a chance association with IgA nephritis.

Adult↗
PubMed1991

Cold agglutinin autoantibodies in psychiatric patients: their relation to diagnosis and pharmacological treatment.

BACKGROUND AND METHOD: The purpose of this study was to compare titers of cold agglutinins in schizophrenic patients with those in patients with major affective disorders and in normal healthy subjects. One hundred sixty-six psychiatric patients and 37 healthy comparison subjects were included in the study. Ninety of the patients suffered from schizophrenia, 54 from bipolar disorder, and 22 from major depression. Venous blood samples were obtained from all subjects between 8:00 and 10:00 a.m. and were immediately tested for cold agglutinin titers. RESULTS: A high frequency (42.2%) of positive cold agglutinin titers was detected in the schizophrenic patients, compared with the bipolar (11.1%) and unipolar (9.0%) patients and the comparison group (8.1%). The investigators did not find any pharmacological effect on these results. CONCLUSIONS: The findings suggest that, at least in this group, positive cold agglutinin titers are associated with schizophrenia. However, this observation cannot provide direct evidence for the involvement of viral or autoimmune factors in schizophrenia.

Adult↗
PubMed2001

Salivary non-immunoglobulin agglutinin inhibits human leukocyte elastase digestion of acidic proline-rich salivary proteins.

Saliva contains acidic proline-rich salivary proteins that are involved in the formation of the salivary pellicle coating supragingival tooth surfaces. However, human leukocyte elastase, arriving in gingival exudates from inflamed periodontal tissues, degrades the acidic proline-rich salivary proteins, preventing binding to hydroxylapatite surfaces. Here it is reported that high-molecular-weight non-immunoglobulin salivary agglutinin inhibited the proteolytic action of human leukocyte elastase on purified acidic proline-rich salivary proteins. Inhibition was eliminated with monoclonal antibody to a protein determinant on the salivary agglutinin. The addition of antibody against salivary agglutinin blocked the inhibitory effect of parotid saliva on exogenously applied human leukocyte elastase, allowing for the elastase-mediated digestion of the salivary acidic proline-rich salivary proteins. Salivary agglutinin, therefore, is a physiologically important inhibitor of human leukocyte elastase and is able to inhibit elastase-mediated digestion of salivary acidic proline-rich proteins.

Agglutinins↗
PubMed1980

The production of anti-A1 agglutinins in A-like rabbits injected with human group a1 secretor saliva.

A-like and non-A-like rabbits were injected with human group A1 and A2 secretor saliva. The sera were then examined for their agglutinative capacity against human group A1, A2, B and O erythrocytes before and after sequential adsorption with group O, B and A2 erythrocytes. The A-like rabbits produced specific anti-A1 agglutinins when injected with group A1 saliva but not when injected with group A2 saliva. The non-A-like rabbits produced anti-A and anti-A1 agglutinins in response to the A1 antigen but only anti-A agglutinins when group A2 saliva was injected. These experiments support the interpretation that a qualitative difference exists between subgroups A1 and A2. The non-A-like rabbits also formed cross-reacting antibodies as shown by the increase in the agglutinins reactive with human group B red cells.

ABO Blood-Group System↗
PubMed1983

Human lymphocyte agglutinins in Tursiops truncatus (bottlenose dolphin).

A naturally occurring heterophile agglutinin directed against human erythrocytes and lymphocytes is present in the serum of the marine mammal, Tursiops truncatus (Bottlenose dolphin). Differential specificity was demonstrated with the use of absorption techniques that showed at least 3 separate specificities directed against erythrocytes, T cells, and B cells, of which the B cell agglutinin was in the highest titer. Isolation techniques employing ion exchange and affinity chromatography have shown these agglutinins to be of the IgM class. Agglutinin activity is lost when lymphocytes are treated with pronase, suggesting that the surface receptor is protein or protein associated.

Agglutination Tests↗
PubMed1976

NDV-O agglutinins and heteroagglutinins in sera of blood donors.

In sera of healthy blood donors advancing age was accompanied by a decrease in the levels of agglutinins against human group O erythrocytes modified by Newcastle disease virus (NDV-O agglutinins) and of heteroagglutinins against sheep, guinea-pig and rabbit erythrocytes. Significant correlations of titres existed between the different heteroagglutinins, but not between these and the NDV-O agglutinins. The origins and interrelations of the natural agglutinins are discussed.

ABO Blood-Group System↗
PubMedDate not supplied

[Studies on the relation between the production of anti-O and anti-H agglutinins and the specific treatment of typhoid fever].

The AA, studied the behaviour of anti-O and anti-H agglutinins in patients with typhoid fever treated with CAF or with CAF+ corticosteroides. They have shown that, during the treatment with antibiotics, the O-agglutinins, which appeared extremely quickly, can be present at a high level and for a long time in the serum; on the other hand the H-agglutinins are usually present at a lower level and tend to decrease more rapidly. In patients treated with CAF+ corticosteroides the agglutinins behaviour was not substancially different from that in patients treated with antibiotic only. These modifications in humoral immunity are notable only when treatment is begun early. On the basis of the results and of data in the most recent literature, the AA. also discuss the problem of typhoid relapses, the pathogenesis of which cannot depend from the modifications of humoral immunity only.

Adolescent↗