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PubMed1983

A rapid and sensitive assay for neuraminidase using peanut lectin hemagglutination: application to Vibrio cholera and Trypanosoma cruzi.

A neuraminidase assay based on peanut lectin agglutination is described. Human red blood cells are used both as substrate for the enzyme and as probe for the lectin. The validity of the method is ascertained by measuring the enzyme and lectin activities on erythrocytes whose outer membrane sialic acid was labeled with tritium after oxidation with sodium periodate followed by reduction with sodium borotritiide. The neuraminidases of Trypanosoma cruzi and Vibrio cholera are used as examples; in both cases, a linear relationship is observed between the degree of erythrocyte desialylation and the peanut hemagglutination titer. For the hemagglutination assay, lectin in homogeneous form as well as in crude peanut extracts may be used, and free sialic acid need not be separated from substrate-bound sialic acid. The hemagglutinating activity of peanut lectin is not affected by pre-treatment of the erythrocytes with various proteases. The method is particularly useful in the neuraminidase analysis of multiple samples, such as in gel filtration chromatography and for screening of hybridoma antibodies against neuraminidase.

Chromatography, Gel↗
PubMed1981

Comparison of hemagglutination inhibition, serum neutralization and ELISA-PVM tests for the detection of antibodies to pneumonia virus of mice in rat sera.

Recently, the seroneutralization, hemagglutination inhibition, and the ELISA procedures were used to determine the presence of serum antibody to the pneumonia virus of mice in rat sera. This study was initiated to evaluate the reliability of these procedures to detect specific antibodies in our laboratory animal species. The results obtained indicate that: 1) the seroneutralization test is not reliable since numerous false-positive sera were detected; 2) the ELISA is more sensitive than both the seroneutralization and hemagglutination inhibition procedures, and 3) the presence of low hemagglutination inhibition titers should not be considered significant.

Animals↗
PubMed1984

Hemagglutinating factor in an extract of Sarcoptes scabiei var. suis (De Geer).

A naturally occurring hemagglutinating factor to tanned human O positive, ovine and porcine erythrocytes was found in extracts from Sarcoptes scabiei var. suis. This hemagglutinating factor did not react with bovine, equine or avian erythrocytes. This factor was demonstrated by microscopic examination of the tanned erythrocytes and by the passive hemagglutination assay.

Animals↗
PubMed1989

Incidence of hemagglutination activity among pathogenic and non-pathogenic Bacteroides fragilis strains and role of capsule and pili in HA and adherence.

We analyzed the ability of 120 encapsulated strains of B. fragilis to agglutinate guinea pig and human red blood cells. Sixteen strains showed a strong hemagglutination (HA) ability, 21 strains a moderate HA ability, 7 strains a weak HA ability and 74 strains did not agglutinate the tested red blood cells. Six strains tested from each HA group were able to adhere to cheek epithelial cells and to a cultured human intestinal cell line. Hemagglutinating strains were the most adhesive. By electron microscopy, pilus-like structures were found in three of the encapsulated adhesive strains. Treatment of the bacterial cells with pronase E reduced both HA ability and adherence of piliated encapsulated, and of piliated non-encapsulated strains. Glucosidase treatment of cells reduced HA activity and adherence of piliated encapsulated and of non-piliated encapsulated strains. Finally, it was found that hemagglutinating strains are more frequently isolated from clinical specimens (55%) than from feces of healthy donors (20%).

Bacterial Adhesion↗
PubMed1992

Biological role of an arginine residue present in a histidine-rich peptide which inhibits hemagglutination of Porphyromonas gingivalis.

Inhibitory effects of synthetic fragments in histatin 8, having the sequence Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr, on hemagglutination by Porphyromonas gingivalis 381 were examined. The hemagglutinating activity was reduced much more by the peptide Lys-His-His-Ser-His-Arg-Gly-Tyr than by the peptides Lys-His-His-Ser-His and/or Lys-Phe-His-Glu-Lys. These results suggest that the arginine residue may have an important role in the inhibition of hemagglutination by P. gingivalis.

Amino Acid Sequence↗
PubMed2005

Hemagglutinating and hemolytic activities of Enterococcus faecalis strains isolated from different human clinical sources.

A total of 95 Enterococcus faecalis strains isolated from different human clinical sources were investigated for hemagglutinating activities and hemolysin (Hly) production in the presence of erythrocytes from a wide range of species. MRHA (mannose-resistant hemagglutination) activity was found in all clinical strains tested in this study. MRHA of E. faecalis strains isolated from different sources was most frequently observed with human (both group O and A) and guinea pig erythrocytes. None of the strains agglutinated horse erythrocytes in the presence of 1% alpha-D-mannose. It should be emphasized that our data indicate the absence of a relationship between sources and MRHA. In contrast, all 95 strains investigated in this report were negative for MSHA (mannose-sensitive hemagglutination) activity. Regarding hemolysin production, it was seen that E. faecalis, and particularly urinary strains, preferably lysed horse erythrocytes. On the other hand, none of the 95 clinical strains tested in this study showed hemolytic activity against bovine and sheep erythrocytes. In general, these results show that E. faecalis strains isolated from different clinical sources possessed a diversity of hemagglutinins and a limited repertoire of hemolysin activities.

Animals↗
PubMed1986

Characterization of Escherichia coli wild-type strains by means of agglutination with antisera raised against cloned P-, S-, and MS-fimbriae antigens, hemagglutination, serotyping and hemolysin production.

E. coli strains isolated from patients with urinary tract infections (UTI) very often possess mannose-sensitive (MS) and mannose-resistant (MR) adherence factors (fimbriae). According to their receptor specificity the mannose-resistant adhesins can be divided into several types, P, S, M and X. We have cloned the determinants of three groups of UTI E. coli adhesins, MS, P and S, and prepared specific antisera against the fimbriae antigens. 189 hemagglutination (HA+)-positive strains, 96 fecal isolates and 93 strains isolated from UTI have been tested with these specific antisera and further characterized by receptor specific HA, HA patterns and further of the "common O serogroups" 01, 02, 04, 06, 07, 08, 018, 025, 075, most prevalent in UTI, and hemolysin production. 68 (73%) of the UTI strains and 50 (52%) of the fecal isolates showed P-receptor specificity; 16 (17%) of the uropathogenic bacteria and 33 (34%) of the fecal strains exhibited S, M or X-fimbriae antigens. 24% of the P-hemagglutinating (P+) strains reacted with P (F8)-specific antiserum. In contrast, more than three quarter of the S+-strains were agglutinated by S-specific antiserum. HA-pattern VI and 018 antigen were found to be associated with P-fimbriae strains, whereas HA-pattern V and VII and the O antigens 02 (M-type), 06 and 018 (S-type) occurred most frequently in P--strains. A high percentage of P-fimbriated strains showed mannose-sensitive hemagglutination and hemolysin production.

Adhesiveness↗
PubMed2004

Expression of recombinant envelope protein of Japanese encephalitis virus YL strain in Escherichia coli possesses hemagglutination activity.

The nucleotide sequence of glycoprotein E of YL vaccine strain was cloned, sequenced and expressed in E. coli. Phylogenetic analysis of envelope (E) amino acid sequences of 18 JEVs in GenBank showed that the vaccine strain YL closer to the virulent strain HVI which is a Taiwanese isolate. We found only two amino acid mutations (K-138 and G-389) of E protein might lead viral attenuation in YL. In this study, we used pRSET vector system to construct three recombinant plasmids (pRSET/F1R1, pRSET/F2R2 and pRSET/F1R2), which encoded and expressed different or overlapping amino acid region of E protein. The antigenicity and hemagglutination activity of these recombinant proteins were examined by western blotting and hemagglutination test, respectively. Our results demonstrated that the recombinant protein of pRSET/F1R2 possesses predominant antigenicity and hemagglutination activity.

Animals↗
PubMed2002

Lipoplex-induced hemagglutination: potential involvement in intravenous gene delivery.

We report a study aiming to characterize the interaction of blood and blood components with lipoplexes under conditions relevant to in vivo intravenous transfection. In this study we focus on the interaction of lipoplexes with red blood cells (RBC). It was found that no significant hemolysis occurred during several hours' incubation using lipoplex compositions and lipoplex/red blood cell ratios in the range commonly used for in vivo transfection. However, the interaction of RBC with lipoplexes resulted in massive agglutination, which occurs irrespective of the type of cationic lipid or helper lipid. Agglutination was also induced by polyplexes (such as dendrimer/DNA complexes) and lipoplexes in the presence of spermidine or protamine sulfate (the latter induced hemagglutination by itself). DSPE-PEG(2000) inserted into the lipoplexes inhibits hemagglutination somewhat. In order to understand the effect of serum on the agglutination better, plasma was separated into its high molecular weight components (HMWC, >14 kDa) and its low molecular weight components (LMWC, < or = 14 kDa). These fractions were characterized for their level of proteins, primary amino groups, osmotic pressure, and electrical conductivity, and compared with saline (0.15 M NaCl). It was found that both LMWC and HMWC inhibit agglutination by themselves, although whole serum demonstrates better hemagglutination inhibition than each fraction separately. The inhibitory effect of the serum (or plasma) is explained by its effect on the electrostatics of the lipoplexes, reducing their positive charge, as was demonstrated using fluorescein-phosphatidylethanolamine-labeled lipoplexes. The effect of LMWC was related to ionic strength and was equal to the effect of 0.15 M NaCl. The level of agglutination was reduced with increasing lipoplex DNA(-)/cationic lipid(+) (DNA(-)/L(+)) ratio. However, at the low DNA(-)/L(+) ratio needed to achieve significant in vivo transfection after i.v. administration, massive agglutination occurred. These data suggest that i.v. administration of lipoplexes and polyplexes may lead to RBC agglutination, and the agglutinates formed may explain the localization of lipoplexes and expression of their transgenes in the lungs.

Anticoagulants↗
PubMedDate not supplied

Hemagglutination enhancement by bovine serum albumin is affected by octanoate, Reactive Blue 2 (Cibacron Blue), and polymer.

An AutoAnalyzer system was used to study factors that influence the albumin enhancement of agglutination of Rh(D)-positive red cells by IgG anti-D. An albumin consisting of trimer and higher oligomer was more efficient than a preparation composed mainly of monomer and dimer. Modification of the hemagglutination-enhancing property of albumin was obtained by the addition of ligands (octanoate [caprylate] and Reactive Blue 2 [Cibacron Blue]). Irrespective of the polymer content, neither ligand alone had any effect on low-fatty-acid albumins. However, when mixtures of octanoate and Cibacron Blue were added to the same albumins, hemagglutination was initially increased, and then diminished with increasing concentrations of ligands. The enhancing property of high-fatty-acid, nonpolymerized albumin was markedly reduced by the addition of octanoate or Cibacron Blue. On the other hand, only Cibacron Blue could produce the same inhibitory effect on a polymerized albumin with high fatty acid content. The implication is that the total free fatty acids bound and polymer content are two independent variables that can affect the performance of an albumin as a hemagglutination enhancer.

Drug Synergism↗
PubMed1953

Inhibition of influenza virus multiplication by alkyl derivatives of benzimidazole. II. Measurement of inhibitory activity by hemagglutination titrations.

The activity of compounds which inhibit the multiplication of influenza virus can be measured in chorioallantoic membrane cultures in vitro by means of hemagglutination titrations on the medium. Studies on the reproducibility of virus reproduction in membrane cultures have revealed the major variables which affect the results and thus have led to the development of a precise technique. Under strictly controlled experimental conditions, the extent of reproduction of the virus in membrane cultures is predictable within narrow limits of variation. With 10(5.5) EID(50) of influenza B virus, Lee strain, and 5.75 cm.(2) of chorioallantoic membrane per ml., the ratio of infective virus particles to susceptible allantoic cells appears to be approximately 1:28. Under these conditions, the evidence indicates that two cycles of multiplication occur and nearly maximal hemagglutination titers are found with culture medium at 36 hours. The extent of the deviation in the absolute titer in different experiments was only 0.112 log unit. At a concentration of 0.0017 M, 2,5-dimethylbenzimidazole caused inhibition of the multiplication of influenza B virus, Lee strain, which persisted for at least 70 hours as measured by hemagglutination titrations on the culture medium. The degree of inhibition was closely comparable to that demonstrated by infectivity titrations on the membrane at the end of the first cycle of virus reproduction (1).

Benzimidazoles↗
PubMed2005

Effect of amino acid residue and oligosaccharide chain chemical modifications on spectral and hemagglutinating activity of Millettia dielsiana Harms. ex Diels. lectin.

The effects of modifying the carbohydrate chain and amino acids on the conformation and activity of Millettia dielsiana Harms. ex Diels. lectin (MDL) were studied by hemagglutination, fluorescence and circular dichroism analysis. The modification of tryptophan residues led to a compete loss of hemagglutinating activity; however, the addition of mannose was able to prevent this loss of activity. The results indicate that two tryptophan residues are involved in the carbohydrate-binding site. Modifications of the carboxyl group residues produced an 80% loss of activity, but the presence of mannose protected against the modification. The results suggest that the carboxyl groups of aspartic and glutamic acids are involved in the carbohydrate-binding site of the lectin. However, oxidation of the carbohydrate chain and modification of the histidine and arginine residues did not affect the hemagglutinating activity of MDL. Fluorescence studies of MDL indicate that tryptophan residues are present in a relatively hydrophobic region, and the binding of mannose to MDL could quench tryptophan fluorescence without any change in lambda(max). The circular dichroism spectrum showed that all of these modifications affected the conformation of the MDL molecule to different extents, except the modification of arginine residues. Fluorescence quenching showed that acrylamide and iodoacetic acids are able to quench 77% and 98% of the fluorescence of tryptophan in MDL, respectively. However, KI produced a barely perceptible effect on the fluorescence of MDL, even when the concentration of I(-) was 0.15 M. This demonstrates that most of tryptophan residues are located in relatively hydrophobic or negatively charged areas near the surface of the MDL molecule.

Acrylamide↗
PubMed1978

Detection of early "significant" antibody responses in paired sera by the use of an automated bovine parainfluenza-3 hemagglutination-inhibition system.

An automated bovine parainfluenza-3 hemagglutination-inhibition system was used to detect small increases (15--20%) in specific antibody titer between paired bovine sera collected three days apart. Automated and manual parainfluenza-3 hemagglutination-inhibition test procedures were compared as methods for the serologic diagnosis of parainfluenza-3 infection. Fifteen daily serum specimens from each of three animals were analyzed as various possible manual-test and automated-test serum pairs. With the sera from two of the animals, considered to be parainfluenza-3 hemagglutination-inhibition-positive, the manual microtiter test procedure made 18 (69%) false negative diagnoses when using the standard manual-test criteria for "evidence of infection." When a 20% titer increase between three-day serum pairs was considered "serologically significant," the automated system made three (17%) false-negative diagnoses. At a 15% "serologically significant" increase, no false-negative diagnosis was made. The utilization of automated serology for the routine diagnosis of disease should permit treatment and control measures to be initiated early, thereby reducing losses due to infectious disease.

Animals↗
PubMed1977

Comparison of the enzyme-linked immunosorbent assay and the indirect hemagglutination test for detection of antibody to cytomegalovirus.

Thirty samples of serum were tested for antibody to cytomegalovirus by enzyme-linked immunosorbent assay (ELISA) and indirect hemagglutination (IHA). The two tests were in extremely close agreement. Of the 30 sera evaluated by ELISA, 16 were considered to be positive and 14 were considered negative. In all 16 positive samples, the titers by ELISA were at least twofold to 10-fold higher than the indirect hemagglutination titers. Two of the 14 sera evaluated as negative by the ELISA test had low indirect hemagglutination titers (1:8 and 1:4). They were not detectable at the initial dilution (1:50) of the ELISA test. These two sera might have been classified as positive if the initial dilution in ELISA had been lower than 1:50.

Animals↗
PubMed1977

Restitution of hemagglutinating activity to spikeless particles of HVJ (Sendai virus) by glycoprotein components of Newcastle disease virus.

Spikeless particles of HVJ (Sendai virus) lacking in hemagglutinating (HA) activity were obtained by enzymatic digestion of virions with trypsin followed by centrifugation through a sucrose gradient. When they were mixed with glycoprotein components of Newcastle disease virus (NDV) obtained by treatment of purified virions with deoxycholate (DOC), the mixture showed hemagglutination reaction, which was inhibited by anti-NDV serum, but not by anti-HVJ serum. Sedimentation profile of the HA active agents was then examined by centrifugation of the mixture of spikeless particles of HVJ (labeled with 3H-uridine) and glycoproteins of NDV (labeled with 14C-amino acid mixture). The results showed that the peak of HA activity had both of the radioactivities, and that the sedimentation rate of the HA was faster than that of spikeless HVJ but slower than that of intact HVJ. Electron micrographs of such HA active structures showed that they were morphologically closely similar to intact virion of HVJ, although they had neither hemolytic activity nor infectivity. The mixture of spikeless HVJ and glycoproteins of HVJ or NDV which were removed from virions by proteolytic enzymes, on the other hand, did not show any detectable hemagglutinating activity.

Deoxycholic Acid↗
PubMed1993

Host-specific hemagglutination of influenza A (H1N1) virus.

H1N1 strains of influenza A virus isolated during the influenza season of 1991-92 were divided into two groups according to the property of host-specific hemagglutination. Group 1 viruses agglutinated human and chicken red blood cells. Group 2 viruses agglutinated human but not chicken red blood cells. The viruses of both groups, however, showed the same antigenic structure determined with ferret antisera. The virus clones which were plaque-purified twice from a group 2 virus retained the characteristic of host-specific hemagglutination after five successive passages in MDCK cells, indicating that this phenomenon is genetically determined. However, the amino acid sequences of the hemagglutinin (HA) polypeptides deduced from the nucleotide sequences of the HA gene of the two groups did not show any differences between them. This suggests a difference in amino acids in some other polypeptide(s), which affects the host-specific hemagglutination.

Amino Acid Sequence↗
PubMed1993

Participation of an arginyl residue of insulin chain B in the inhibition of hemagglutination by Porphyromonas gingivalis.

Insulin chain B, containing each one arginyl and lysyl residue in its peptide chain, inhibited hemagglutination by Porphyromonas gingivalis. To determine the further inhibitory profile, chain B was digested into 4 fragments by protease, which was contained in the preparation of hemagglutinin from P. gingivalis. Identification of each fragment by the amino acid analysis revealed that the chain was cleaved at the carboxyl site of arginyl and/or lysyl residues, but one fragment contained citrulline instead of arginine at its carboxyl terminal. This citrulline might have originated from arginine by an arginine deiminase-like enzyme of P. gingivalis. Only one fragment that contained the arginyl residue exhibited inhibitory activity on hemagglutination, but it was considerably weakened compared with that of the intact chain B. The difference in the inhibitory activity seemed to depend on the position of an arginyl residue in the peptide; this was also confirmed using several derivatives of bradykinin. The present result suggests that the internal arginyl residue in a peptide chain may be critical for the inhibition of the hemagglutination by P. gingivalis.

Amino Acid Sequence↗
PubMed1995

The cloning, expression and sequence analysis of a second Porphyromonas gingivalis gene that codes for a protein involved in hemagglutination.

It has been suggested that Porphyromonas gingivalis may possess more than one hemagglutinin. We have previously reported the cloning of a gene (hagA) that encodes a hemagglutinin. In this study we report the cloning, characterization, and sequencing of a second gene (hagB) that encodes a protein that also appears to be involved in hemagglutination. Antiserum to the clone (ST 7) was found to inhibit hemagglutination by P. gingivalis 381, and hemagglutinating inhibition activity of anti-P. gingivalis antiserum was reduced by adsorption of the antiserum with cells of clone ST 7. Restriction mapping and Southern analysis indicates there is little or no DNA homology between this cloned 4.8-kb HindIII DNA fragment and a cloned hemagglutinin gene we have previously described. Minicell analysis of the cloned P. gingivalis chromosomal DNA fragment revealed that the major gene product is a 49-kDa protein. Immunoaffinity chromatography using purified rabbit immunoglobulin G against the cloned protein resulted in the purification of a major reactive 49- to 50-kDa protein from a P. gingivalis cell lysate. Nucleotide sequence analysis revealed the hagB open reading frame to be 1053 nucleotides in length with a mol% G+C of 59.9% coding for a protein of 350 residues with a calculated molecular weight of 39.375 kDa. This protein was also determined to be basic and hydrophilic and to contain a potential signal peptide. Comparison of both the nucleotide and derived amino acid sequences with computer-based databases did not reveal any significant homologies between habB and any other previously sequenced genes.

Adhesins, Bacterial↗