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PubMed2001

Cervical secretory immunoglobulin A to human papillomavirus type 16 (HPV16) from HPV16-infected women inhibit HPV16 virus-like particles-induced hemagglutination of mouse red blood cells.

Secretory immunoglobulin A (sIgA) antibodies are the first line of defence at the genital mucosa, and are thought to hinder viral infections by binding to conformational epitopes on the viral capsid. To investigate if cervical sIgA binds to conformational epitopes of the Human papillomavirus type 16 (HPV16), cervical mucus samples from 109 HPV16-infected patients were examined in a HPV16 virus-like particles-induced hemagglutination inhibition assay. 48 (44.1%) patients were able to inhibit hemagglutination. Inhibition of hemagglutination was associated with the presence of sIgA (P=0.001). In conclusion, naturally occurring cervical anti-HPV16 sIgA binds to and hinders conformational epitopes on the viral capsid, suggesting that these antibodies might have a neutralizing capacity.

Capsid↗
PubMed1978

Leptotrichia buccalis hemagglutination in cell binding and salivary inhibition studies.

The characteristic hemagglutination (HA) of Leptotrichia buccalis was used for measuring its attachment to various human cells and for determining if saliva contained hemagglutination inhibition (HI) factors. The microbial strain utilized displayed the characteristic EM morphology of L. buccalis. Sonicated preparations of the organism were tested for HA activity before and after adsorption with human cells. Buccal epithelial cells, red blood cells (RBC), HeLa and embryonic kidney cells all bound the HA fragments of the organisms. The bacterial fragments on the cells could be observed by fluorescent antibody testing. The fragments were released from the cells used for adsorption with chelators and upon addition of CaCl2 the HA activity returned. Whole saliva displayed hemagglutination inhibition activity in a manner suggesting a binding site interaction. The similarity of the HA activity of F. nucleatum is discussed as are the relationships of cell binding to colonization of the organisms and immunopathology to host cells.

Adsorption↗
PubMed1970

Detection of foot-and-mouth disease virus antibodies. I. "Passive" hemagglutination test.

A passive hemagglutination test has been developed to detect and measure foot-and-mouth disease virus (FMDV) antibody by using glutaraldehyde as a coupling reagent. An optimal concentration of 10 to 40 mug of virus per ml with 0.25% glutaraldehyde at 25 C for 1 hr was established for the sensitization of sheep erythrocytes. A reaction time of 18 hr at 4 C or 2 hr at 37 C induced good agglutination in the presence of specific antibody. Sensitization was carried out in phosphate buffer, whereas agglutination and preadsorption of nonspecific agglutinins from sera were performed in gelatin (0.1%, w/v)-stabilized, phosphate-buffered saline. An optimal pH of 7.2 was also established for all reactions. Antibodies derived from guinea pigs hyperimmunized by infecting with FMDV, types A, O, and C were both virus-and type-specific. Preliminary experiments showed that strain A-119 and strain A-24 Cruzeiro could also be distinguished by hemagglutination. Parallel hemagglutination and complement-fixation tests showed the former to be two to four times more sensitive than the latter.

Aldehydes↗
PubMed1976

Hemagglutination by equine infectious anemia virus.

Equine infectious anemia (EIA) virus which was propagated on an equine dermal cell line agglutinated guinea pig erythrocytes. Viral fluids containing about 10(7.5) mean tissue culture infective doses/ml showed hemagglutinating (HA) titers ranging from 16 to 32 units/0.05 ml. Results of cesium chloride equilibrium density gradient centrifugation revealed that the hemagglutinin was inseparable from the virus particles. The hemagglutination reaction persisted over a wide range of temperature and pH, and the absence of divalent cations did not decrease its activity. The HA activity was stable at 4 degrees C but not at 56 degreesC. The activity was destroyed by virus-disrupting lipid solvents and moderately sensitive to a proteolytic enzyme. Neuraminidase enhanced HA activity slightly. Phospholipase C had no effect on HA titer, although it completely inactivated infectivity. It was relatively stable to ultraviolet irradiation. Thus, the hemagglutinin appears to be closely associated with virus particles, and its activity is dependent on the presence of its lipids and proteins. Hemagglutination was inhibited by sera from horses infected with EIA virus. Hemagglutinin receptors on the erythrocytes were inactivated by a proteolytic enzyme and formaldehyde but were not influenced by neuraminidase, sodium deoxycholate, or KIO4.

Animals↗
PubMed1982

New passive hemagglutination assay kit that uses hemagglutinin-sensitized erythrocytes for detection of rubella antibodies.

A new passive hemagglutination assay for the detection of antibodies to rubella virus hemagglutinin (PHAST-Rubella) was compared with the hemagglutination inhibition (HI) test and another passive hemagglutination test that uses a soluble rubella virus antigen (SA-PHA). When the immune responses of vaccinated individuals were monitored, similar rises in antibody titer were detected by HI or PHAST-Rubella, whereas the rise in titer detected by SA-PHA was delayed. Early-phase vaccine-induced immunoglobulin M antibody analyzed by sucrose gradient fractionation was detected to the same degree by HI and PHAST-Rubella, but early-phase immunoglobulin G antibody reacted more strongly in the HI test. When acute and convalescent serum pairs from rubella-infected individuals were evaluated, a fourfold rise in titer was detected by PHAST-Rubella and HI in 15 of 15 pairs, whereas SA-PHA, which is not intended for detecting antibody titer rises in acute infections, detected a rise in titer in only 3 of 15 pairs. In studies to determine rubella immune status, testing of 1,078 premarital and random serum specimens resulted in 98.6% agreement among the three methods in identifying rubella antibody-positive and -negative individuals. For the quantitative PHAST-Rubella procedure, a coefficient of correlation of 0.93 was obtained, in comparison with HI, when a panel of 40 characterized sera were tested. These results indicate that PHAST-Rubella reagents can detect rubella antibodies as well as HI reagents and thus may be used as a fast and accurate means of determining rubella immune status and for the quantitation of rubella antibodies.

Antibodies, Viral↗
PubMed1967

Envelope protein of influenza virus. I. Hemagglutinating activity of reassociated subunits.

The hemagglutinating properties of influenza virus envelope protein, prepared by reassociation of polypeptide subunits, have been defined and compared with those of virus and ether-split hemagglutinin. In general, the characteristics of the intact and ether-split virus were found to be similar, whereas those of the envelope protein were distinctly different. The use of chicken, pigeon, and guinea pig erythrocytes both at 23 and 4 C disclosed that the hemagglutinating titers of envelope protein preparations were particularly dependent on the system employed. Under optimal conditions, with guinea pig cells at 4 C, the titers of envelope protein preparations were equivalent to those of the original virus concentrates. The hemagglutinating activity of envelope protein was particularly sensitive to elevated temperature, concentrated urea, sulfhydryl-reducing reagents, and tryptic digestion at high salt concentrations. In all these respects, the intact virus was more resistant than the envelope protein. Interpretation of the data indicates that the hemagglutinin is stabilized when associated with the lipid micelle at the surface of the virus.

Animals↗
PubMed2003

Hemagglutination and antigenic comparison of rabbit hemorrhagic disease virus.

The hemagglutinating activity and serological properties of three strains of rabbit hemorrhagic disease virus, Chinese, Korean and Shizuoka, which was first isolated in Japan, were examined by hemagglutination (HA) and cross hemagglutination inhibition (HI) test with human erythrocytes. Similar results were observed between the Chinese and Korean strains, both of which gave positive HA at 4 degrees C with O, A, B and AB, and at 22 degrees C with B and AB blood groups. In the Shizuoka strain, positive HA was observed at 4 degrees C with O, A, B and AB, at 22 degrees C with A, B And AB, and at 37 degrees C with B blood group. In experimentally infected rabbits, HI antibody in these animals showed a titer of 16,384 or 32,768 at 4 weeks after inoculation. No serological difference was observed in three strains by cross HI test.

Animals↗
PubMed2006

The hemagglutinating activity of Pseudomonas aeruginosa strains isolated from humans and animals.

The presence and type of adhesins occurring in Pseudomonas aeruginosa strains were determined by hemagglutination test with a 3% suspension of normal and trypsin-treated human group A erythrocytes, with or without the addition of sugar inhibitors (D-mannose, D-glucose, L-fucose, D-galactose, D-fructose, lactose, N-acetylneuraminic acid, N-acetylglucosamine and N-acetylgalactosamine). This study showed that a low percentage of Pseudomonas aeruginosa strains caused the agglutination of normal erythrocytes. Trypsin treatment of erythrocytes did not affect the hemagglutinating properties, indicating that hemagglutination was not dependent upon a trypsin-sensitive protein on the erythrocytes surface. Most of the studied strains agglutinated RBCs at 37 degrees C. A great variability in the inhibiting activity on studied strains was observed among the carbohydrates tested. These results demonstrated the predominant role of N-acetylglucosamine, N-acetylgalactosamine and N-acetylneuraminic acid for Pseudomonas aeruginosa adhesion to RBCs.

Animals↗
PubMedDate not supplied

[A method for detecting the hemagglutinating activity of enteroviruses].

Optimal conditions to reveal the hemagglutinating activity in the Coxsackie viruses of group B and hemagglutination test (HAT) performed by the micromethod are studied and determined. The titre of hemagglutinins revealed in HAT is established to depend on pH of the phosphate-buffer solution, concentration of human erythrocytes and their group attribution. The viruses passaged at the suboptimal temperature 33 degrees C are shown to possess the maximal hemagglutinating activity.

Enterovirus B, Human↗
PubMed1971

A micro-passive hemagglutination test for the rapid detection of antibodies to infectious bovine rhinotracheitis virus.

Serum antibodies to infectious bovine rhinotracheitis virus are most commonly detected using the serum-virus-neutralization test, a time-consuming and expensive procedure. A passive hemagglutination test was developed for the rapid detection of antibodies using the Microtiter System. Two cloned strains of the virus were used in the investigation, namely the BF strain and the Los Angeles strain. Erythrocytes from several species were used. The best results were obtained using the Los Angeles strain of virus adsorbed to sheep cells treated with formalin and tannic acid. Sera from field cases of the disease as well as hyperimmune bovine and rabbit sera were tested using both the micro-passive hemagglutination test and the standard plaque-neutralization procedures. Comparable titers were obtained in the two tests. The micro-passive hemagglutination test is rapid, accurate and economical.

Animals↗
PubMed1984

[Trials to obtain conjugates for the passive hemagglutination test with chromium chloride and their use in studying foot-and-mouth disease viruses].

Experiments were carried out to produce conjugates for the hemagglutination-inhibition reaction with the aid of chromic chloride. Studies with reference F.M.D. viruses and with CFT revealed that the antibody erythrocyte diagnostic agents were highly specific, and were stable in storage at +4 degrees C and in freeze-drying. It was found that the conjugates obtained with F.M.D. antigens possessed high specificity, however, were not stable and 7 to 10 days later lost their activity. Tests with the hemagglutination-reaction showed that immunity itself could be studied in cattle treated with F.M.D. vaccines. A correlation was found between the results obtained via the hemagglutination reaction and those obtained with the aid of the virus-neutralization test.

Animals↗
PubMed1983

[Laboratory procedures with adenoviruses. X. Hemagglutination with glutaraldehyde-fixed erythrocytes].

Erythrocyte preparations from man, rat, and monkey, fixed by glutaraldehyde (0.06%, final concentration, 30 min room temperature), remained agglutinable by various human adenoviruses. While incomplete adenovirus hemagglutinins from species of subgenera A, C, and E did not react with fixed blood cells, the numerous species of subgenera B and D, in which hemagglutination and hemagglutination-inhibition are essential for identification, did so. Fixed blood cells were also agglutinable by indirect hemagglutinins of adenovirus 9 and 11; hence, hemagglutination-enhancement tests with fixed blood cells are feasible. Fixed blood cells remained stable and agglutinable up to one year; they could also be lyophilized.

Adenoviruses, Human↗
PubMed1984

[D-mannose-resistant hemagglutination in opportunistic enterobacteria in infantile diarrhea].

D-mannose-resistant hemagglutination with human and bovine red blood cells was determined in 284 cultures of opportunistis enterobacteria isolated from 99 patients with acute intestinal infections and in 55 cultures isolated from 27 practically healthy children aged up to 1 year. In 16 sick children (16.16%) opportunistic enterobacteria, positive when tested in D-mannose-resistant hemagglutination, were detected. In no case were such cultures isolated from practically healthy children. In 9 out of 12 species of opportunistic bacteria belonging to the family Enterobacteriaceae strains showing the positive reaction in the D-mannose-resistant hemagglutination test were found.

Diarrhea, Infantile↗
PubMed1981

Coagglutination and indirect hemagglutination in the detection of an excreted immunologically active substance from Leishmania.

The methods of coagglutination and indirect hemagglutination were used to detect the production of the immunologically active excreted factor (EF) of Leishmania. Staphylococci, rich in protein A and sensitized with specific anti-Leishmania antibodies, coagglutinated with supernatant fractions of cultures, thus enabling continuous monitoring of the excretion of EF by multiplying parasites. Papain-treated human red blood cells, sensitized with crude or purified EF, also agglutinated with the coagglutination reagent. The sensitized papain-treated red blood cells may be employed in indirect hemagglutination to detect specific antibodies to Leishmania in rabbit and human sera. As the EF is specific for each Leishmania serotype group, coagglutination and indirect hemagglutination offer the possibility of rapid, easy, sensitive and specific diagnostic tools in the determinations of both antigen and antibody in specimens from suspected cases of leishmaniasis.

Animals↗
PubMed1975

Estimation of hemagglutination-inhibition titers.

In the hemagglutination-inhibition test, simple relationships exist between units of hemagglutinating virus and hemagglutination-inhibition antibody titers. Equations have worked out which allow estimating antibody titers for different virus doses, provided all other parameters are kept constant. They are applicable when the isofixation lines in log-log plots as obtained in box titrations either are positioned at angles of 45degree or deviate from this value. Using lower or higher doses of hemagglutinin in the test, the coefficient of variation of the estimated antibody titers was found to be approximately 4 per cent. This procedure is useful in a number of virus-cell-serum systems and allows comparisons of antibody titers obtained in different laboratories.

Antibodies, Viral↗
PubMed1981

[Determination of O-agglutinins against Yersinia enterocolitica by the indirect hemagglutination test (author's transl)].

O-agglutinins against Yersinia enterocolitica serovar 03 and serovar 09 in serum specimens were determined by the indirect (passive) hemagglutination test and the Widal technique. The hemagglutination test was carried out in microtitre plates with formalized and sensitized turkey erythrocytes. Cell wall antigens (lipopolysaccharides) were prepared by the phenol-water method. The indirect hemagglutination test had a high sensitivity and specificity. Moreover, this test has the advantage of being easier to set up and read than the bacteria agglutination. No unspecific reactions were observed.

Agglutinins↗
PubMed1991

Deantigenation of human erythrocytes by bacterial glycosidases--evidence for the noninvolvement of medium-sized glycosphingolipids in the Dolichos biflorus lectin hemagglutination.

Fresh human A1 erythrocytes, washed and pretreated in phosphate buffer with or without papain, were incubated at 37 degrees C with blood group-degrading enzymes from the human fecal Ruminococcus torques strain IX-70. The effects were assayed as changes in hemagglutination patterns, and blood group activities of alkali stable glycolipid extracts from the enzyme-treated cells using Dolichos biflorus anti-A1 lectin, Ulex europaeus type 1 anti-H lectin, and various monoclonal anti-A antibodies. Hemolysis was negligible (less than or equal to 1% after 6 h), and the osmotic fragility increased slightly only after papain treatment. The papain-untreated A1 erythrocytes lost D. biflorus agglutinability within minutes at room temperature with the unfractionated bacterial enzyme mixture IX-70 (42 mU 1,3-alpha-N-acetylgalactosaminidase (alpha-GalNAc'ase)/ml), but remained A active by strong agglutination with BioClone anti-A antibody even after 6 h of incubation. Thin layer chromatographic (TLC) immunostaining of extracted lipids showed hydrolysis of D. biflorus binding glycosphingolipids with more than six monosaccharides after 1 h, i.e., at a slower rate than the loss of D. biflorus agglutinability. Disappearance of these glycosphingolipids after 1 h paralleled the appearance of U. europaeus agglutinability and the strong binding of this lectin to glycolipid extracts in TLC immunoassays. A partly purified 1,3-alpha-GalNAc'ase (XI-117) (100 mU/ml) and a 1,2-alpha-fucosidase fraction (XI-50) containing alpha-GalNAc'ase (10 mU/ml) did not degrade blood group A active glycosphingolipids but completely abolished the D. biflorus agglutinability within 6 h. Papain pretreatment exposed U. europaeus receptors on the cell surface without changing the A1 hemagglutination pattern. It also facilitated a complete degradation of D. biflorus and U. europaeus reactive glycolipids with the IX-70 enzyme mixture within 6 h. The D. biflorus lectin was a good discriminator of A1/A2 subjects using erythrocyte lipid extracts but had a low affinity for the blood group A type 3 and type 4 glycosphingolipids in the TLC-overlay technique. In conclusion this study shows that (i) loss of D. biflorus A1 hemagglutination does not correlate with a loss of D. biflorus binding glycosphingolipids and (ii) loss of D. biflorus binding glycosphingolipids does not correlate with a loss of D. biflorus agglutinability. The results indicate that the serological D. biflorus agglutinability of A1 erythrocytes is not dependent on medium-sized glycosphingolipids (hexa- to dodecaglycosylceramides).

ABO Blood-Group System↗
PubMed1983

C1q has albumin binding activity but does not interfere in the hemagglutination test for anti-albumin antibodies.

Two factors in the sera of patients with liver disease interact with polymerized human serum albumin (HSAP). These are anti-albumin antibodies (AAA) and receptors for polymerized albumin on HBsAg. Recently it was demonstrated by radioimmunoassay that purified human C1q also binds HSAP. Our data confirm the reaction between purified human C1q and HSAP by passive hemagglutination and by indirect immunofluorescence of HSAP-coated erythrocytes (E-HSAP). It is shown that although purified C1q binds HSAP, in the serum, the AAA and not C1q are responsible for the albumin binding activity in HBsAg-negative sera of patients with liver disease and of normal individuals, as detected by passive hemagglutination of E-HSAP, AAA were found to inhibit the binding of serum C1q to polymerized albumin, and hence the E-HSAP hemagglutination test for AAA titration in human sera proved valid.

Antibodies↗