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PubMed1980

Lectin-mediated induction of human neutrophil chemotaxis, chemokinesis, and cap formation.

Six lectins, including concanavalin A, phytohemagglutinin P, castor bean I, wheat germ agglutinin, peanut agglutinin, and pokeweed mitogen, were studied for their ability to stimulate human neutrophil locomotion and cap formation. Five of these lectins with known monosaccharide specificities, including concanavalin A, phytohemagglutinin, P, castor bean I, wheat germ agglutinin, and peanut agglutinin, were found to stimulate human neutrophil migration in a modified Boyden assay. Pokeweed mitogen showed negligible activity in the locomotion assay as compared with other lectins. Tests were performed to determine if the observed neutrophil migration in response to lectins was directional, and it was found that concanavalin A, phytohemagglutinin P, and peanut agglutinin were both chemokinetic and chemotactic, whereas castor bean I was only chemokinetic. Wheat germ agglutinin could not be declared chemotactic or chemokinetic due to its tendency to agglutinate neutrophils. Studies with fluoresceinated lectins demonstrated that lectins which stimulate neutrophil migration also bind to neutrophil surfaces. Preincubation with specific monosaccharide ligands blocked both stimulated locomotion and fluorescence, suggesting that an available lectin-binding site was required both for lectin binding and the stimulation of migration. Additional experiments indicated that fluoresceinated concanavalin A, phytohemagglutinin P, castor bean I, wheat germ agglutinin, and peanut agglutinin all induce cap formation on the neutrophil.

Binding Sites↗
PubMedDate not supplied

Antityphoid agglutinins in African school aged children with malaria.

BACKGROUND: Salmonella antibodies are known to cross-react with other antigens including those from Escherichia coli. Malaria antigens may also have similar characteristics. OBJECTIVES: To establish antibody levels in malaria patients and controls and to decipher (if any), relationship(s) between significant agglutinin responses to the various antigens as outcome factor and malaria parasitaemia as exposure factor. STUDY SETTING: University of Benin Teaching Hospital and Egor Local Government Area of Edo state, Nigeria, between July and August, 1999. STUDY DESIGN: Prospective and a case control study. PATIENTS AND METHODS: Agglutinins against H and O antigens of Salmonella typhi, Salmonella paratyphi A, B and C were determined using the Widal test in 189 school aged children(5-16 years) with malaria (males, 54.0%; females, 46.0%) and 175 apparently healthy children,(52.0% males, and 48.0 %) of comparable age and gender distributions. Agglutination reaction at >1.80 were significantly more in malaria patients (52/189 or 27.5%) than in controls (28/175 or 16.0%) (x2 = 7.07; p<0.05). Agglutination reaction to various antigens were significantly higher in controls with malaria parasitaemia (10/36 or 27.8%) than those without parasitaemia (18/139 or 12.9%) (x2 = 4.57; p<0.02) (OR=2.59). Significant titres were also more in subjects and controls with malaria parasitaemia (62/235 or 26.38%) than in those without (18/139 or 12.94%) (x2=9.32; p< 0.05) (OR=2.41). At dilution of > or =1.80 children aged 9 -14 years (as compared to those < or =8 years of age) and more males (subjects and controls) had demonstrable agglutinins. At most serum dilutions, antibodies to H antigens were more commonly found in subjects and controls than agglutinins against O antigen of Salmonella typhi. Fifty percent of subjects and controls had demonstrable agglutination at approximate dilutions of 1:60 and 1:40 respectively. The number of subjects and controls that showed demonstrable agglutinins against Salmonella paratyphi antigens were less than 10.0% CONCLUSION: Enhanced agglutinin to DO and DH may be a phenomenon associated with childhood malaria.

Adolescent↗
PubMed1978

Differential agglutination of particulate Vi and O antigens by the IgM and IgG class antibodies.

The IgG and IgM immunoglobulins were fractionated from pooled sera of typhoid patients and typhoid carriers and the agglutinin titres and weights of Vi and O antibodies in these immunoglobulin fractions determined. The O antigen particles were more effectively agglutinated than the Vi antigen particles by their corresponding antibodies of the IgM class. There was no such difference between IgG class Vi and O antibodies. Similar behaviour was found on indirect estimation of the agglutination capacity of the IgG and IgM class Vi and O antibodies in the sera of individual typhoid patients or carriers. The significance of such differential agglutinating capacity of the Vi and O antibodies of the IgM class is discussed.

Agglutination↗
PubMed1981

Improved serodiagnosis of Salmonella enteric fevers by an enzyme-linked immunosorbent assay.

The value of the enzyme-linked immunosorbent assay (ELISA) for the serological diagnosis of typhoid or paratyphoid fevers was tested with a collection of five sets of sera from 23 individuals who had no history of Salmonella infection from a nonendemic area (set 1) and from 143 patients from a highly endemic area (sets 2 to 5). The test was performed with a crude cell envelope fraction derived from Salmonella typhi. On the basis of results with sera in set 1, titers >160 (inverse of serum dilution) for immunoglobulin M (IgM) or >500 for IgG were regarded as signifying a specific antibody response. These titers were occasionally exceeded in sera in set 2, derived from patients with no clinical or laboratory evidence of Salmonella infection. In presumptive cases of typhoid or paratyphoid fevers (culture positive and agglutination negative or vice versa; 13 patients, set 3, and 26 patients, set 4, respectively), IgG antibodies were encountered more frequently than IgM, but some sera were negative in each group. In 81 confirmed cases (culture and agglutination positive, set 5) IgG antibodies were detected in at least one of the paired sera from all patients, and the IgG titers were higher (median 3,500) than those of the IgM antibodies (median 600). There was no evidence of a significant difference in IgM or IgG titers between acute- and convalescent-phase sera. The titers of 10 paired sera from patients from whom S. enteritidis, bioserotype paratyphi A, was isolated were somewhat lower than those of 84 patients with S. typhi isolation (serogroup D). There was some correlation between O antigen agglutination and IgM enzyme-linked immunosorbent assay, but otherwise the titers in the two serological tests varied independently. Of 11 patients in set 3 (2 patients with serogroup B agglutinins omitted), 1 belonged to blood group O, in contrast to 54 group O among 107 agglutination-positive patients, a distribution not necessarily reflected by the enzyme-linked immuno-sorbent assay. This study has provided good evidence that the enzyme-linked immunosorbent assay can serve as a valuable aid to the diagnosis of Salmonella infection in an endemic area, as a substitute for the agglutination test.

ABO Blood-Group System↗
PubMed1980

Comparative study between microscopic agglutination and complement fixation tests in experimental canine leptospirosis.

In order to evaluate the antibody response to pathologic leptospira from both serovars icterohaemorrhagiae and canicola, dogs were experimentally inoculated with these leptospiras. Each of the serovar were inoculated in 15 dogs and the antibody response in the acute phase of infected was followed by microscopic agglutination and complement fixation tests. Complement fixing antibodies were detected in both groups at the 4th day post infection and agglutinins appeared in circulation at the 7th day post infection when homologous antigens were used. On the 63rd day post infection with serovar canicola and on 56th day post infection with serovar icterohaemorrhagiae, complement fixing antibodies could no longer be detected but, in both experimental groups, specific agglutinins were presented in significant titers.

Agglutination Tests↗
PubMed1957

Agglutinating efficiency and combining capacity of Shigella and Vibrio antisera from rabbits at different stages of immunization.

Studies of the relative combining capacities of different antisera to Vibrio cholerae and Shigella flexneri were carried out using the Talmage test. In this test the absorption of an I(131) labelled antibody preparation by antigen is blocked by the addition of unlabelled unknown serum. Sera from rabbits in the early stages of immunization ("early antisera") had a high agglutinin titer, but low combining capacity. Sera from hyperimmune rabbits ("late antisera") had higher combining capacities than early antisera, but similar or lower agglutinin titers. More antigen was needed to absorb the agglutinins from late antisera than from early ones of the same agglutinin titer, indicating that late antisera contained relatively more antibody. At high concentrations, sera from hyperimmune rabbits agglutinated the homologous antigen more rapidly than did early antisera, even though early sera had similar or higher agglutinin titers. Sera drawn after the anamnestic response to bacterial antigen had the characteristics of late sera; i.e., their combining capacities were high. The possible significance of these findings for the in vitro estimation of protective antibody is discussed.

Animals↗
PubMed1985

Lectin-binding to hemocytes of Mytilus edulis.

Lectin receptors for WGA, Ricinus 60, Ricinus 120, and for the agglutinin from the albumin gland of Helix pomatia were detected on the surface of Mytilus hemocytes by an agglutination assay. When hemocyte monolayers on slides were incubated with these lectins, strong rosette formation was obtained after addition of human erythrocytes. The lowest lectin concentration which caused formation of rosettes was determined to be 5 micrograms/ml of WGA or of Helix agglutinin, and 20 micrograms/ml of Ricinus 60 or 40 micrograms/ml of Ricinus 120, respectively. In contrast to these results, no binding of indicator cells to Mytilus hemocytes occurred with various other lectins, including Con A.

Agglutination Tests↗
PubMed1991

Saccharomyces cerevisiae a- and alpha-agglutinin: characterization of their molecular interaction.

An O-glycosylated protein of approximately 18 kDa responsible for mating type specific agglutination has been isolated from Saccharomyces cerevisiae a cells, purified to homogeneity and via peptide sequences the gene was cloned by PCR. An open reading frame codes for a protein of 69 amino acids. A minimum of five serine and five threonine residues of the mature protein are glycosylated. alpha-Agglutinin is a highly N-glycosylated protein of approximately 250 kDa. Both purified agglutinins form a specific 1:1 complex in vitro. Pretreatment of alpha-agglutinin, but not of alpha-agglutinin, with diethylpyrocarbonate (DEPC) prevents formation of the complex; treatment of alpha-agglutinin in the presence of alpha-agglutinin protects the former from DEPC inactivation. By carboxy terminal shortening of the alpha-agglutinin gene and by replacing three of its eight histidyl residues by arginine, the active region of alpha-agglutinin for interaction with alpha-agglutinin has been defined. Neither the N- nor the O-linked saccharides of the two agglutinins seem to be essential for their interaction.

Base Sequence↗
PubMed1984

Glycoproteins of bovine epididymal spermatozoa--a cytochemical study.

Modifications in bull sperm plasmamembrane during epididymal passage were investigated by the use of four different lectins: Concanavalin A (Con A); Ricinus communis I (RCA1); Wheat germ agglutinin (WGA); Ulex europaeus agglutinin I (UEA1). During sperm passage from caput to cauda epididymidis agglutination by RCA1 and WGA distinctly increased. Similar but somewhat less pronounced difference in the agglutinability was found for Con A. No agglutination was observed with UEA1. Ultrastructural examination of Con A binding sites on sperm plasma membrane with a Con A-horseradish peroxidase-gold technique (Con A-HRP-G) revealed a significant increase in the number of gold granules on the sperm tails during the epididymal passage of spermatozoa. No change in WGA-binding sites was observed between caput and cauda spermatozoa using a WGA-peroxidase method.

Agglutination↗