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PubMed1990

Hemagglutinating and binding properties of botulinum C2 toxin.

To characterize the binding substance(s) for botulinum C2 toxin, the hemagglutinating activity of component II of botulinum C2 toxin (C2II) was studied by hemagglutination and hemagglutination inhibition. Human and animal erythrocytes were agglutinated by trypsinized C2II much more strongly than by untreated C2II. Trypsinized C2II agglutinated neuraminidase-treated erythrocytes more strongly than intact, trypsin- and pronase-treated ones. On the other hand, trypsin- and pronase-treated erythrocytes were more weakly hemolyzed by trypsinized C2II than intact and neuraminidase-treated ones, and trypsinized C2II showed both hemagglutinating and hemolytic activities to these erythrocytes. Hemagglutination of trypsin-treated human type B erythrocytes was inhibited by galactose, N-acetylgalactosamine, N-acetylglucosamine, L-fucose and mannose. Thyroglobulin and bovine salivary mucin were much stronger inhibitors. From these findings, the binding substance(s) for botulinum C2 toxin on erythrocytes is(are) suggested to be glycoprotein(s).

Acetylgalactosamine↗
PubMed2005

Properties of hemagglutination by Prevotella melaninogenica.

Although Prevotella melaninogenica belongs to the commensal oral microbiota, some strains possess putative virulence factors. For example, we have previously described fimbriated, hemagglutinating strains of P. melaninogenica, isolated from patients with periodontal disease. The aim of this investigation was to compare some chemical and physical properties of hemagglutination (HA) of P. melaninogenica with those of other pigmented gram-negative anaerobes. HA of 13 P. melaninogenica strains proved to be considerably weaker than that of the major periodontal pathogen, Porphyromonas gingivalis. Vigorous shaking reduced HA of shaken cells but the shaken supernatant had the same hemagglutinating activity as non-shaken cells. The hemagglutinating agent on P. melaninogenica seemed to be a protein, which can be separated from the cell and binds to lactose-, galactose-, and raffinose-containing carbohydrates on the erythrocytes. Adherence to epithelial cells did not differ significantly between the hemagglutinating and non-hemagglutinating strains of P. melaninogenica. Although P. melaninogenica is able to agglutinate erythrocytes, this potential virulence factor is of a considerably lower magnitude than that of major periodontal pathogens.

Journal Article↗
PubMed1964

A SYNTHETIC ACYL POLYSACCHARIDE AND THE HEMAGGLUTINATION ACTIVITY.

From Mycobacterium tuberculosis, a serologically specific polysaccharide was purified. It contained mannose, arabinose, and a trace of glucose. It was not active in hemagglutination (HA) reaction. Partial acylation of the polysaccharide was carried out with palmitoylchloride, and the synthetic lipopolysaccharide contained 15.1 per cent of esterified palmitic acid. The synthetic lipopolysaccharide had hemagglutination activity and 0.5 microg was able to sensitize 1 ml of 2 per cent erythrocyte suspension; it had the same activity as the natural antigenic lipopolysaccharide. The same antibody in the antiserum was involved in the hemagglutination reaction with both the synthetic and natural lipopolysaccharides. The sensitizing activity of the synthetic lipopolysaccharide was completely neutralized by cholesterol. Model experiments showed that the lipid moiety of hemagglutination antigen was essential for the sensitization of erythrocytes. The mechanism of the hemagglutination reaction is discussed.

Animals↗
PubMed1985

Simple hemagglutination inhibition test for the diagnosis of toxoplasmosis.

A simple hemagglutination inhibition (HI) test for the serological diagnosis of toxoplasmosis has been developed and evaluated. A total of 84 human and 120 mouse serum samples were tested by the newly developed HI test and compared with an immunoglobulin G-indirect fluorescent antibody test. Statistical analysis of serum titers obtained by using the HI test and the immunoglobulin G-indirect fluorescent antibody test showed a correlation coefficient of 0.89. The diagnostic efficacy of HI when compared with the immunoglobulin G-indirect fluorescent antibody diagnostic test results was 96.43% for human sera and 100% for mouse sera. The unique hemagglutination antigen, derived from Toxoplasma gondii (Rh strain) exotoxin, spontaneously binds with mouse or rat erythrocytes, causing the hemagglutination reaction. In this study, 2, 4, or 8 hemagglutinating units of T. gondii exotoxin was used with Swiss/Webster mouse erythrocytes as an indicator for the HI assay. The results indicate that 8 hemagglutinating units is optimal because this concentration has the least unexplained variability. T. gondii exotoxin was stable for at least 18 months at -70 degrees C. The Toxoplasma HI test we report in this paper is shown to be a fast, easy, highly specific, and sensitive test for the diagnosis of toxoplasmosis.

Animals↗
PubMed2006

First report of a xylose-specific lectin with potent hemagglutinating, antiproliferative and anti-mitogenic activities from a wild ascomycete mushroom.

From fresh fruiting bodies of the wild ascomycete mushroom (Xylaria hypoxylon) a lectin with N-terminal sequence resemblance to a part of Aspergillus oryzae genome and only slight similarity to fungal immunomodulatory protein from the mushroom Flammulina velutipes was isolated. The protocol comprised extraction with water, precipitation from the aqueous extract using 80% saturated (NH(4))(2)SO(4), ion exchange chromatography on DEAE-cellulose and CM-cellulose, and then gel filtration by fast protein liquid chromatography on Superdex 75. Lectin activity was adsorbed on DEAE-cellulose and unadsorbed on CM-cellulose. The lectin appeared as a single band with a molecular mass of 14.4 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a single 28.8-kDa peak in gel filtration on Superdex 75. The lectin exhibited highly potent antiproliferative activity toward tumor cell lines, and exerted a potent anti-mitogenic action on mouse splenocytes. The hemagglutinating activity of the lectin was inhibited by inulin and xylose. It was stable up to 35 degrees C. At 40 degrees C its hemagglutinating activity was reduced by 50%, and it dwindled to 12.5% of the original activity at 50 degrees C. The hemagglutinating activity was also sensitive to NaOH and HCl solutions. The hemagglutinating activity was unaffected by CaCl(2) and ZnCl(2), and was potentiated substantially in the presence of AlCl(3) and FeCl(3). The distinctive features of this lectin comprise a unique sugar specificity, and highly potent hemagglutinating, antiproliferative and anti-mitogenic activities. X. hypoxylon lectin differs in molecular mass, N-terminal sequence and sugar specificity from previously reported ascomycete mushroom lectins.

Amino Acid Sequence↗
PubMed1984

Localization of the hemagglutinating activity of platelet thrombospondin to a 140 000-dalton thermolytic fragment.

The platelet protein thrombospondin (TSP) which is secreted from alpha-granules upon platelet activation agglutinates trypsinized, glutaraldehyde-fixed human erythrocytes. Optimal conditions for the hemagglutinating activity require that both Ca2+ and Mg2+ be present in final concentrations of 2 mM. In the presence of dithiothreitol (i.e., reduction of disulfide bonds), the lectin-like activity decreases in a manner proportional to the extent of reduction of the molecule from its native trimeric configuration into its Mr 180 000 subunits. Proteolysis of purified TSP with thermolysin, which produces discrete domains with the capacity to bind fibrinogen and heparin, also diminishes, but does not abolish, the hemagglutinating activity. Fibrinogen was without effect on hemagglutinating activity while heparin was found to be a potent inhibitor. Other proteoglycans such as hyaluronic acid, chondroitin sulfate, keratan sulfate, dermatan sulfate, and heparan sulfate had no effect. That portion of the TSP molecule apparently responsible for the hemagglutinating activity was identified by incubating a thermolytic digest of TSP with red blood cells and then determining which fragment was bound to the cell surface. The binding site resides within a peptide fragment of 140 000 daltons but is absent from an Mr 120 000 fragment derived from the Mr 140 000 fragment. Under the conditions for optimal expression of hemagglutinating activity (i.e., 2 mM MgCl2 and 2 mM CaCl2), this Mr 140 000 fragment was also shown to have heparin binding activity.

Blood Platelets↗
PubMed1984

Hemagglutination-inhibiting antibody in hemorrhagic fever with renal syndrome.

Hemagglutination activity was demonstrated in a Hantaan virus antigen prepared from infected suckling mouse brain by sucrose-acetone extraction. Hemagglutination of goose erythrocytes was pH dependent and was optimal at pH 6.0-6.2. Immunofluorescent and hemagglutination-inhibiting antibodies were significantly correlated in 80 human and 13 animal sera. Hemagglutination-inhibiting antibody was present in some patients 20 years after the onset of hemorrhagic fever with renal syndrome. The hemagglutination inhibition test was useful for confirming that an insectivore, Suncus murinus, may be an animal reservoir host of a Hantaan-like virus.

Animals↗
PubMed1998

A hemagglutinating variant of Prevotella melaninogenica isolated from the oral cavity.

Strains resembling Prevotella melaninogenica were isolated from healthy subjects and patients with periodontal disease and were identified using: a 5-test phenotypic screen; commercial identification kits; and a 16S rRNA-based polymerase chain reaction (PCR) method. Eleven clinical isolates closely resembling P. melaninogenica, and all from patients with periodontitis, were able to agglutinate erythrocytes. In the electron microscope, hemagglutinating isolates showed fimbria-like structures, that were not seen on non-hemagglutinating isolates. Some strains were further classified with PCR-restriction fragment-length polymorphism (RFLP) of 16S rRNA genes. Amplified 16S rDNA was digested using five different endonucleases, separated with agarose gel electrophoresis, stained and photographed. Photographs were then scanned, digitized and a distance matrix calculated using Dice coefficient, where the presence or absence of a band was used as a character. The distance matrix was plotted as a phenogram. At 70% similarity six clusters were seen. Type strains of separate Prevotella species did not fall into any cluster. Hemagglutinating isolates fell into three clusters: four clustered with the type strains of P. melaninogenica and Prevotella veroralis; four with other P. melaninogenica isolates and two hemagglutinating isolates clustered together Prevotella loescheii. The PCR-RFLP results showed that the hemagglutinating strains did not form a homogenous group inside the Prevotella genus.

Adult↗
PubMedDate not supplied

Comparison of latex agglutination, indirect hemagglutination, and ELISA techniques for the detection of Toxoplasma gondii-specific antibodies in the serum of cats.

The primary purpose of this study was to determine whether commercially available latex agglutination and indirect hemagglutination kits for the detection of Toxoplasma gondii-specific antibodies were capable of detecting T. gondii-specific immunoglobulin M (IgM) in the serum of cats. Serum samples from 35 cats containing either T. gondii-specific IgM, T. gondii-specific immunoglobulin G (IgG), or both were collected. Each serum sample was assayed using a latex agglutination kit, an indirect hemagglutination kit, an enzyme-linked immunosorbent assay (ELISA) for the detection of T. gondii-specific IgG, and an ELISA for the detection of T. gondii-specific IgM. When serum samples containing only T. gondii-specific IgM as determined by ELISA were assayed, the latex agglutination kit and the indirect hemagglutination kit detected antibodies in 33.3% and 13.3%, respectively. When T. gondii-specific IgG was present in a serum sample, the results from the latex agglutination kit, the indirect hemagglutination kit, and the IgG-ELISA were similar; however, there was a wide variation in titer magnitude results between the three assays. It was concluded that the latex agglutination kit and the indirect hemagglutination kit did not adequately detect T. gondii-specific IgM in feline serum.

Animals↗
PubMed1997

Hemagglutination is a novel biological function of lipopolysaccharide (LPS), as seen with the Vibrio cholerae O139 LPS.

It has been generally thought that the polysaccharide moiety of lipopolysaccharide (LPS) maintains only serological specificity, while the lipid A portion determines various biological functions. However, we found that hemagglutination was a common function of the polysaccharide moiety of LPSs from important human enteropathogenic bacteria. Of the LPSs examined, Vibrio cholerae O139 LPS showed the highest hemagglutinating activity. Glycoproteins, such as mucin and fetuin, showed efficient inhibition of the hemagglutinating ability. Since cell-mediated hemagglutination is known to be correlated with bacterial adherence, hemagglutination induced by the polysaccharide moiety is interpreted to indicate that cell-surface LPS is a potential adhesin.

Bacterial Adhesion↗
PubMed1980

Hemagglutination properties and adherence ability of Aeromonas hydrophila.

Human diarrheal isolates and enterotoxigenic strains of Aeromonas hydrophila are strong hemagglutinators with human blood cells. Sugar inhibition studies and yeast coagglutination tests with 11 selected strains revealed six different hemagglutination mechanisms for this species. These were characterized by inhibition by L-fucose, inhibition by D-galactose, inhibition by D-mannose, and two distinguishable mechanisms which were inhibited by either L-fucose or D-mannose, one being pilus mediated. Inhibition of hemagglutination by another strain required a combination of D-galactose and D-mannose. The hemagglutinating strains also attached well to human blood cells and buccal epithelial cells, with as many as 55% of the cells of a culture attaching successfully. In some cases the attachment to buccal epithelial cells appeared to involve mechanisms different from those used for hemagglutination.

Aeromonas↗
PubMed1982

Pilus production, hemagglutination, and adhesion by porcine strains of enterotoxigenic Escherichia coli lacking K88, K99, and 987P antigens.

Three strains of enterotoxigenic Escherichia coli which adhered, colonized intensively, and caused disease in pig intestine, but which did not produce pili of the K88, K99, or 987P antigen types were designated 3P(-) ETEC. The 3P(-) ETEC caused mannose-resistant hemagglutination, adhered to porcine intestinal epithelial cells in vitro, and produced pili. However, most bacteria taken directly from the intestine of pigs infected with 3P(-) ETEC appeared to be nonpiliated. Two preparations were isolated from the 3P(-) ETEC. One (material A) contained pili, caused mannose-sensitive hemagglutination, and did not inhibit adhesion of whole bacteria to epithelial cells in vitro. The other (material B) had no demonstrable pili, caused mannose-resistant hemagglutination, and blocked ahesion of bacteria to epithelial cells in vitro. Antiserum against an acapsular mutant (K(-)) of one 3P(-) ETEC strain was absorbed to remove antibodies directed against somatic (O) antigen. The absorbed antiserum agglutinated all three 3P(-) ETEC strains grown in the K(-) form at 37 degrees C, but not when they were grown at 18 degrees C. The absorbed antiserum blocked the hemagglutinating activity of material B, but not of material A. It also reacted (via indirect immunofluorescence) with all of the 3P(-) ETEC when they were grown in pig intestine. The results were interpreted to indicate that: (i) the epithelial adhesive and mannose-resistant hemagglutinating activities of the 3P(-) ETEC strains may be mediated by an antigen contained in material B; (ii) this antigen either is not pilus associated or is associated with pili that are not demonstrable by the methods used here; (iii) the 3P(-) ETEC strains produce type 1 pili which do not mediate their adhesion to intestinal epithelium of pigs.

Adhesiveness↗
PubMed1982

Failure to detect hemagglutination-inhibiting antibodies with intact avian influenza virions.

Avian influenza viruses replicate in a variety of mammals and birds, yet hemagglutination inhibition tests show that postinfection sera from these animals (e.g., ferrets and ducks) have insignificant levels of antibodies (Hinshaw et al., Infect. Immun. 34:354-361, 1981). This suggested that avian influenza viruses, in contrast to mammalian viruses, may not induce a significant humoral response. Studies reported here indicate that avian influenza viruses do induce high levels of antibodies in ferrets, ducks, and mice and produce long-lived memory for cytotoxic T-cells in mice. The failure to detect hemagglutination-inhibiting antibodies to avian viruses was explained by the finding that antibodies to avian influenza viruses were not detectable in hemagglutination inhibition tests with intact virus yet were readily demonstrable when hemagglutinin subunits were used. In addition, these sera contained high levels of neutralizing antibodies to the avian virus. These findings suggest that the hemagglutinins of avian and mammalian influenza viruses may differ in their accessibility to antibodies or the biological consequence of antibody attachment or both. The practical consequence of these studies is that hemagglutination inhibition tests with intact avian viruses fail to detect antibody and do not correlate with virus neutralization. The avian virus used in these studies, A/Mallard/NY/6870/78 (H2N2), replicated and caused mortality in BALB/c mice, emphasizing that the host range and virulence of avian viruses extends to mammals. The above findings suggest that avian viruses could infect mammals in nature, yet seroepidemiological studies with conventional hemagglutination inhibition tests could give misleading results.

Animals↗
PubMed1992

Hemagglutination and adherence to plastic by Staphylococcus epidermidis.

Staphylococcus epidermidis is an important nosocomial pathogen responsible for intravenous catheter-related bacteremia and infections of other prosthetic medical devices. We found that the ability of S. epidermidis to hemagglutinate erythrocytes correlated with the adherence of bacteria to plastic and to intravenous catheters. S. epidermidis isolates responsible for prosthetic-valve endocarditis (n = 61) and isolates from intravenous catheters (n = 59) were significantly more likely to cause hemagglutination than isolates from the skin of preoperative cardiac surgery patients (n = 19) (P = 0.027). S. epidermidis isolates (n = 23) recovered from the skin of patients 7 to 10 days after cardiac surgery were significantly more likely to exhibit hemagglutination than the preoperative isolates (P = 0.015). By a quantitative adherence assay, we also observed that the hemagglutination titer and number of species of erythrocytes agglutinated correlated directly with adherence to polystyrene (P less than 0.001). In addition, hemagglutinating isolates were significantly more likely to be recovered in high number from intravenous catheters when semiquantitative catheter culture techniques were used (P less than 0.001). We speculate that hemagglutinin(s) either plays a direct role in adherence to polymers and thus prosthetic-device infection or serves as an easily demonstrable marker for adherence-prone isolates.

Animals↗
PubMed1995

Antigenic, structural, and functional relationships between fimbriae and the hemagglutinating adhesin HA-Ag2 of Porphyromonas gingivalis.

While the adhesive properties of Porphyromonas gingivalis are known to allow colonization of the subgingival tissues, the roles of fimbriae and adhesin molecules in hemagglutination remain unclear. The purpose of this study was to analyze the antigenic, structural, and functional relationships of these two components. Five populations of monoclonal antibodies were produced against (i) the hemagglutinating adhesin HA-Ag2 resolved by crossed immunoelectrophoresis (CIE), (ii) native fimbriae, and (iii) each of the three immunoprecipitates, Ag8a, Ag8b, and Ag8c, that define fimbriae by CIE. The tests used for characterization of the monoclonal antibodies included immunoblot reactivity, inhibition of hemagglutination, capacity to dissociate immunoprecipitates by CIE, localization of recognized epitopes by immunoelectron microscopy, and epitope mapping by competition enzyme-linked immunosorbent assay. The results from the different immunochemical tests clearly showed a close antigenic relationship between fimbriae and the hemagglutinating adhesin HA-Ag2. We were able to establish that the epitopic domain H1 of HA-Ag2 is hemagglutinin specific and that domain F2 is fimbria specific. Our data indicate that the polymeric structural unit of fimbriae must be complexed to HA-Ag2, the adhesin, to confer hemagglutination activity to the bacterial cells.

Animals↗
PubMed1997

A specific cell surface antigen of Streptococcus gordonii is associated with bacterial hemagglutination and adhesion to alpha2-3-linked sialic acid-containing receptors.

A Ca2+-independent lectin activity for alpha2-3-linked sialic acid-containing receptors is associated with Streptococcus gordonii DL1 (Challis) but not with a spontaneous mutant, strain D102, that specifically lacks hemagglutinating activity. Comparison of crossed-immunoelectrophoresis patterns of parent and mutant sonicated cell extracts identified a unique antigen (Hs antigen) in the parent cell extract that was purified by DEAE Sephacel column chromatography and by a wheat germ agglutinin (WGA) lectin affinity column. The purified antigen formed a single arc in crossed immunoelectrophoresis with anti-DL1 serum and migrated as a diffuse band above the 200-kDa marker in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy with specific anti-Hs antibody revealed labeling of structures in the fibrillar layer of strain DL1 and no labeling of fibrillar structures on strain D102. Rabbit anti-DL1 serum and anti-Hs Fab inhibited the hemagglutinating activity of strain DL1, and the inhibition was specifically neutralized by purified Hs antigen. Anti-Hs Fab did not inhibit the hemagglutinating activities of several heterologous S. gordonii strains; however, these bacteria were agglutinated by anti-Hs immunoglobulin G and also by WGA. In contrast, two S. gordonii strains that lacked hemagglutinating activity did not react with anti-Hs antibody or with WGA. These findings associate the sialic acid-binding lectin activity of S. gordonii DL1 with a specific fibrillar antigen, which is composed of protein and WGA reactive carbohydrate, and indicate that cross-reactive antigens occur on other strains of this species that possess hemagglutinating activity.

Animals↗
PubMed2003

Norwalk virus-like particle hemagglutination by binding to h histo-blood group antigens.

Noroviruses are a major cause of epidemic acute nonbacterial gastroenteritis worldwide. Here we report our discovery that recombinant Norwalk virus virus-like particles (rNV VLPs) agglutinate red blood cells (RBCs). Since histo-blood group antigens are expressed on gut mucosa as well as RBCs, we used rNV VLP hemagglutination (HA) as a model system for studying NV attachment to cells in order to help identify a potential NV receptor(s). rNV VLP HA is dependent on low temperature (4 degrees C) and acidic pH. Of the 13 species of RBCs tested, rNV VLPs hemagglutinated only chimpanzee and human RBCs. The rNV VLPs hemagglutinated all human type O (11 of 11), A (9 of 9), and AB (4 of 4) RBCs; however, few human type B RBC samples (4 of 14) were hemagglutinated. HA with periodate- and neuraminidase-treated RBCs indicated that rNV VLP binding was carbohydrate dependent and did not require sialic acid. The rNV VLPs did not hemagglutinate Bombay RBCs (zero of seven) that lack H type 2 antigen, and an anti-H type 2 antibody inhibited rNV VLP HA of human type O RBCs. These data indicated that the H type 2 antigen functions as the rNV VLP HA receptor on human type O RBCs. The rNV VLP HA was also inhibited by rNV VLP-specific monoclonal antibody 8812, an antibody that inhibits VLP binding to Caco-2 cells. Convalescent-phase sera from NV-infected individuals showed increased rNV VLP HA inhibition titers compared to prechallenge sera. In carbohydrate binding assays, the rNV VLPs bound to synthetic Lewis d (Le(d)), Le(b), H type 2, and Le(y) antigens, and these antigens also inhibited rNV VLP HA of human type O RBCs. Overall, our results indicate that carbohydrate antigens in the gut are a previously unrecognized factor in NV pathogenesis.

ABO Blood-Group System↗
PubMed1990

Studies on the binding and hemagglutinating properties of cholera toxin to human erythrocytes.

The binding and hemagglutinating properties of cholera toxin (CT) were studied by competitive binding assays and hemagglutination inhibition. The binding of 125I-labeled CT to neuraminidase-treated human type B erythrocytes was most effectively inhibited by ganglioside GM1 among different inhibitors used. Other mono-, di-, and polysaccharides and glycoproteins were at least 10(5) times less potent inhibitors. On the other hand, hemagglutination of neuraminidase-treated human type B erythrocytes by CT was inhibited by lactose, galactose, hog A + H, bovine salivary mucin, porcine thyroglobulin, and fetuin, whereas that was not effectively inhibited by ganglioside GM1 at the highest concentration. These findings suggest that the predominant binding substance for CT on human type B erythrocytes is ganglioside GM1 and that hemagglutination requires some additional process since the interaction of CT with ganglioside GM1 is somehow different in hemagglutination.

ABO Blood-Group System↗