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PubMed1983

Comparison of passive hemagglutination with Turkey erythrocyte assay, enzyme-linked immunosorbent assay, and counterimmunoelectrophoresis assay for serological evaluation of tetanus immunity.

Antibody titers to tetanus toxin in human sera were assayed by passive hemagglutination with turkey erythrocytes, enzyme-linked immunosorbent assay, and counterimmunoelectrophoresis. The first two of these tests were shown to be the most sensitive for antibody detection, having the same range of sensitivity and reproducibility. The antibody levels determined by these assays were up to 400-fold higher than those determined by counterimmunoelectrophoresis. The turkey erythrocyte hemagglutination assay requires only 40 min, whereas the immunosorbent assay method requires 24 h. These results suggest that the hemagglutination assay is the more appropriate method for rapid and sensitive determination of tetanus antibody levels.

Journal Article↗
PubMed1976

Local and systemic opsonic adherent, hemagglutinating and rosette forming activity in mice induced by respiratory immunization with sheep red blood cells.

The humoral response in mice after intranasal (IN) instillation of sheep red blood cells (SRBC) was compared to that produced by intraperitoneal route of immunization. Study of opsonic adherent (passive indirect cytophilic) and hemagglutinating antibody levels in serum and bronchial washings after repeated challenge with SRBC showed that serum antibody titers following respiratory immunization does not differ from the general pattern of a humoral antibody response. The bronchial wash antibody titer was higher than the serum titer as calculated per globulin unit. In contrast, the appearance of measurable antibodies in the bronchial washings after repeated intraperitoneal immunization was delayed and in low titer. B. pertussis vaccine administered in conjunction with SRBC was found to be an excellent adjuvant in the intranasal route of immunization. A single administration of SRBC-Pertussis evoked a considerable adjuvant effect as measured by hemagglutinating and opsonic adherent tests. Monospecific anti-mouse IgG nullified the hemagglutinating and opsonic adherent activity of the bronchial washings, while monospecific anti-mouse IgM had no effect in either activity. Lung and spleen cells capable of forming rosettes with SRBC of intranasally immunized and control mice were counted. Mean response on day 14 was 6 X 10(3) rosetes per million lung lymphoid cells in comparison with less than 10(3) in control mice. No difference was found in the number of rosette-forming cells in the spleen of control and intranasally immunized mice.

Adjuvants, Immunologic↗
PubMed1988

Hemagglutinating activity of Dolichos lablab seed protein.

The hemagglutinating activity of a crude extract and partially purified protein fractions from seeds of Dolichos lablab grown in the state of Bahia, Brazil, has been examined. The crude extract agglutinates rabbit erythrocytes non-specifically with respect to blood groups. The hemagglutination of rabbit erythrocytes induced by the crude extract of D. lablab was inhibited most effectively by N-acetyl-D-glucosamine (3 mM) and alpha-methyl-D-mannoside (3 mM) followed by D-glucosamine (6 mM), D-mannose (6 mM) and D-glucose (12 mM). The spectrum of sugar inhibition of the hemagglutinating activity of the Brazilian seeds combines the characteristics of seeds coming from Turkey and India as indicated by the preferential inhibitory effect exerted by N-acetyl-D-glucosamine and the inhibition by D-mannose and D-glucose. These data suggest that the Brazilian seeds may belong to a different variety of Dolichos lablab.

Acetylglucosamine↗
PubMed1984

Persistence of passively acquired antibodies to hemagglutinating encephalomyelitis virus in swine.

The persistence of passively acquired antibodies to hemagglutinating encephalomyelitis virus (HEV) was determined in 4 pigs in each of the litters of 10 sows. At time of delivery by the sows, the colostrum and serum samples (from the 10 sows) had hemagglutination-inhibiting antibodies to HEV. All of the pigs also had hemagglutination-inhibiting antibodies to HEV at 2 days of age. The level of circulating antibodies to HEV decreased at a nonlinear rate and persisted for about 4 to 18 (mean 10.5) weeks in the circulation of pigs. All 40 pigs were seronegative at 20 weeks of age.

Animals↗
PubMed1997

[Use of a phage peptide library in mapping the group-specific hemagglutinating domain of alpha-virus glycoprotein E2].

Phage display peptide library f88-4/15 (G. P. Smith, USA) was used for mapping the hemagglutination activity domain of glycoprotein E2 of alphaviruses. Using affinity selection and ELISA, we selected the clones binding monoclonal antibody 4H5 to Venezuelan equine encephalomyelitis virus and inhibiting alphavirus hemagglutinating activity. Analysis of the similarity between the peptides amino acid sequences with the alphavirus glycoprotein E2 sequences revealed a structural motive of 4 amino acid residues (HTSR) which was identified in the 85-88 region. Bacteriophages F36 and F19 contained motives corresponding to 102-SXXM-105 and 109-AXXP-112 regions in alphavirus proteins E2. These data permit us to propose that the detected regions are fragments of a group-specific alphavirus hemagglutination domain.

Amino Acid Sequence↗
PubMed1978

Relationship of human adenoviruses 12, 18, and 31 as determined by hemagglutination inhibition.

Adenoviruses 12 and 31, but not Ad18, agglutinate rat blood cells at high titer, providing suitable blood cells be available and a prolonged contact period of virus with the erythrocytes is allowed. Purified virus particles show direct, and virus-free supernatants show direct and indirect, hemagglutination, ie, enhancement of HA by heterologous antiserum. Hemagglutination inhibition with rabbit antisera shows cross-reactions between Ad12 and Ad31 with titers 4--32 times lower than with homologous antigens; Ad18 antisera react with antigens from both of the other serotypes. No cross-reactions were seen with antisera from other adenoviruses. This suggests an antigenic relationship of the three viruses of subgroup IV in their fiber antigen gamma, in addition to the known relation in the hexon (epsilon), which is apparent in cross-neutralization.

Adenoviruses, Human↗
PubMed1979

Clinical evaluation of a rubella passive hemagglutination test system.

A recently marketed passive hemagglutination (PHA) test (Rubacell, Abbott Laboratories) was compared to the hemagglutination inhibition (HI) test for the detection of antibody to rubella virus. The performance of the PHA system in determining immunity to rubella was evaluated by comparing the PHA results and HI results on 1, 086 randomly selected sera submitted for routine premarital and prenatal testing. Of the 1, 079 specimens assayable by both procedures, 1, 053 of the results (97.6%) were in agreement on initial testing. When the 26 initially discrepant specimens were retested for clarification, there was final agreement in 1, 067 of the specimens (98.9%). Twelve specimens were classified as persistently discrepant (five were not retested by PHA) and seven were unassayable by HI. Seven of the specimens with discrepant results were PHA positive and HI negative, and five were PHA negative and HI positive. Discussion of the two tests with respect to technical difficulty, cost, and controls is also included.

Antibodies, Viral↗
PubMed1990

Chemical modification studies on a blood group A-specific lectin, crotalarin (Crotalaria striata) and its effect on hemagglutinating activity.

Crotalarin, the N-acetyl-D-galactosamine-binding blood group A-specific lectin from the seeds of Crotalaria striata was subjected to various chemical modifications in order to ascertain the amino acid residues responsible for its carbohydrate-binding property. Modification of lysine, cysteine and arginine residues did not affect the carbohydrate-binding activity of the lectin. However, modification of tyrosine residue and carboxy group of the acidic amino acids led to a complete loss of its activity, indicating the involvement of tyrosine and aspartic and glutamic acid in the saccharide-binding respectively. The hemagglutinating activity of the lectin was completely/almost completely lost by modification of tryptophan residues. The relative loss in hemagglutinating activity on modification of tryptophan residues indicate that one residue/molecule is required for the carbohydrate-binding activity of the lectin. Modification was not effective in the presence of D-galactose (0.2 M). A marked decrease in the fluorescence emission was found as the tryptophan residues of crotalarin were modified. The c.d. spectra showed the presence of an identical pattern of conformation in the native and modified lectins which confirms that the loss in activity was due to modification only. The effect of periodate oxidation on crotalarin showed loss of activity whereas action of enzymes retained most of the activity.

ABO Blood-Group System↗
PubMed1977

Variables of the rubella hemagglutination tests employing freeze-dried erythrocytes.

The variables which affect the interaction between freeze-dried one-day-old chick erythrocytes and rubella hemagglutinin prepared from rubella-infected porcine kidney cells were defined and evaluated. The sensitivity of the hemagglutination (HA) reaction is much greater at pH 6.0 to 6.2 than at pH 7.0 to 7.5 HEPES (N-2-hydroxyethylpiperazine-N'-2'-ethanesulfonic acid) diluent with added Ca+ or Mg2+ ion gave four- to eightfold higher HA titers than one without divalent cations. The development of agglutinated and non-agglutinated erythrocyte patterns depended much upon the concentrations of gelatin and albumin in the HEPES diluent. Gelatin especially was essential to obtain stable and clearly distinguishable patterns. Optimal conditions for the agglutination of freeze-dried erythrocytes by rubella hemagglutinin were provided when a HEPES-buffered saline at pH 6.2, containing 10(-3) M CaCl2, 0.2 per cent bovine serum albumin, and 0.0025 per cent gelatin was employed throughout as a diluent for serum, hemagglutinin, and freeze-dried erythrocyte suspension. This diluent gave maximally sensitive and reproducible results in rubella HA and hemagglutination-inhibition (HI) tests employing freeze-dried erythrocytes.

Animals↗
PubMed1977

An inhibitor to rubella hemagglutination present in bovine albumin preparations: its removal by treatment with kaolin.

Certain commercial preparations of bovine albumin, fraction V, show inhibitory activity in the rubella hemagglutination (HA) and hemagglutination-inhibition (HI) tests. This does not appear to be due to albumin per se, but instead to a contaminant (or contaminants) with the properties of a lipoprotein. All inhibitory activity can be removed from albumin preparations by treatment with kaolin, gel filtration, or flotation ultracentrifugation. We have found that, even when there was no inhibition of HA titers, kaolin treatment of the albumins prior to their incorporation into the test diluent resulted in more clearly defined agglutination patterns. Reasons for and against including albumin in the test diluent are discussed. It is concluded that, although not essential, it is a worthwhile additive. Our data suggest, however, that each batch of albumin used for this purpose should be checked for the presence of inhibitor, and that treatment with kaolin might be considered as a routine step prior to its incorporation into the test diluent.

Hemagglutination Inhibition Tests↗
PubMed1985

A mixed hemagglutination test for binding of glycosylated cytochemical markers.

A sensitive hemagglutination test which uses simultaneously erythrocytes from two different species was developed to test the ability of glycosylated cytochemical markers to interact with membrane-bound lectins. The interaction between galactose-terminated glycoconjugates and Ricinus communis agglutinin 120 was chosen for exemplification. The lectin was covalently attached to the surface of sheep red blood cells, thus rendering them highly agglutinating for human erythrocytes. Small amounts of a large variety of terminal galactose-containing molecules inhibited the hemagglutination. The assay proved to be particularly useful for testing colloidal gold-adsorbed glycoconjugates of low protein concentration.

Animals↗
PubMed1983

Identification of the rotaviral gene that codes for hemagglutination and protease-enhanced plaque formation.

Temperature-sensitive mutants of bovine rotavirus, UK Compton strain, and rhesus monkey rotavirus, MMU18006 strain, were used to derive 16 reassortants by coinfection of MA104 cells. The parental viruses differed phenotypically in their neutralization specificity, their ability to hemagglutinate, and their requirement for exogenous trypsin for infectivity. When the reassortants were assayed for neutralization specificity and hemagglutination, four phenotypes were observed, indicating that these two rotaviral functions segregated independently. Protease-enhanced infectivity phenotype segregated with the HA phenotype indicating that these two functions were manifestations of the same gene product. In order to determine the gene responsible for these rotaviral functions, the reassortants were genotyped by hybridizing 32P-labeled parental transcripts and denatured reassortant genomic RNAs and analyzing the resulting hybrids by gel electrophoresis. The fourth RNA segment was clearly shown to code for HA and protease enhanced plaque formation in MA104 cells. The neutralization antigen was linked to the eighth and ninth RNA segments that comigrated during gel electrophoresis and thus could not be differentiated.

Animals↗
PubMed1990

Purification and characterization from human parotid secretion of a peptide which inhibits hemagglutination of Bacteroides gingivalis 381.

A peptide from human parotid secretion which inhibited hemagglutination of Bacteroides gingivalis 381 was purified by ultrafiltration followed by DEAE-Sephadex A-25 column chromatography and by gel filtration on Sephadex G-25, and then by reversed-phase HPLC. The complete amino acid sequence of the peptide, determined by automated Edman degradation was as follows; Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr. The peptide contained 12 residues and the charged amino acids predominated with 4 histidine, 2 lysine, 1 arginine and 1 glutamic acid residues, thus being a histidine-rich peptide. The peptide was an active inhibitor of the hemagglutinating activity of B. gingivalis. Specific binding of tritium-labeled peptide to B. gingivalis cells was demonstrated. These results suggest that the histidine-rich peptide may function as a binding domain for the hemagglutinins of B. gingivalis during agglutination.

Amino Acid Sequence↗
PubMed2006

Chemoenzymatic synthesis and application of a sialoglycopolymer with a chitosan backbone as a potent inhibitor of human influenza virus hemagglutination.

Sialoglycopeptide (SGP) is referred as the glycopeptide in hen's egg yolk, which has an N-linked, complex-type, disialyl biantennary oligosaccharide with an alpha-(2-->6)-sialyl N-acetyllactosamine residue. The residue is known as a binding ligand of type-A human influenza virus hemagglutinin. We describe herein a simple synthesis of a sialoglycopolymer with a chitosan backbone as a potent inhibitor of human influenza virus hemagglutination that makes use of the natural source ingredient, SGP, and the transglycosylation activity of endo-beta-N-acetylglucosaminidase from Mucor hiemalis (Endo-M). Its inhibitiory activity for influenza virus hemagglutination is 40 times higher than that of SGP, and its competitive inhibition is determined to be over 300 times higher than that of fetuin. These results indicate that a sialoglycopolymer having a multivalent sialo-oligosaccharide could potentially be used for the prevention of influenza virus infection.

Acetylglucosamine↗
PubMed1987

Hemagglutination patterns of Pseudomonas aeruginosa strains of different serogroups, Habs and Fisher types.

Pseudomonas aeruginosa strains of sixteen Habs and three Fisher types were examined for their hemagglutination activity using vertebrate erythrocytes including human ones. Their carbohydrate-binding specificity as determined by hemagglutination-inhibition suggests a possible method of their purification. This study also indicates the possibility of an occurrence of multiple lectins of different specificity.

Hemagglutination Inhibition Tests↗
PubMed1951

The adsorption of proteins on erythrocytes treated with tannic acid and subsequent hemagglutination by antiprotein sera.

Treatment of sheep erythrocytes with suitable concentrations of tannic acid render them capable of adsorbing certain protein molecules from solution in saline. Red cells which have adsorbed proteins in this way are agglutinated after washing by the homologous antiprotein sera, even by high dilutions. Through hemagglutination sera can be titrated for antibodies against antigens adsorbed on the cells exposed to tannic acid. Furthermore, small amounts of the antigens can be detected through their power to inhibit hemagglutination of the treated cells.

Adsorption↗
PubMed1982

Evaluation of a passive hemagglutination test kit for the detection of rubella antibodies.

RUBACELL (Abbott Laboratories), a commercial test kit for the detection of rubella antibodies that utilizes the principle of passive hemagglutination (PHA), was compared with a standard hemagglutination-inhibition (HI) assay procedure. The PHA test gives a qualitative yes/no result suitable for pregravidic determination of immune status. The procedure is technically simple and requires less than half the time needed for the HI assay. Four of 61 sera that were negative with HI assay tested as indeterminate or as falsely positive using the RUBACELL procedure.

Antibodies, Viral↗
PubMed1983

Identification of a protein having hemagglutinating activity in the hemolymph of the silkworm, Bombyx mori.

Hemolymph of Bombyx mori larvae was found to contain activity to agglutinate trypsinized and glutaraldehyde-fixed sheep red blood cells (fixed SRBC). The specific activity of the hemagglutinin changed during development from the fifth instar to the adult with a transient increase just before pupation. This activity was specifically inhibited by glucuronic acid and heparin. The material with hemagglutinating activity was partially purified by gel filtration on Sephacryl S-300. A protein with molecular weight of 260,000 that preferentially binds to fixed SRBC was identified using radioiodinated hemagglutinin. Antibody raised against this protein specifically inhibited the activity of partially purified hemagglutinin, indicating that this protein is essential for hemagglutination.

Animals↗