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PubMed1968

Hemagglutination by rabies virus.

Goose erythrocytes were agglutinated by five strains of rabies virus grown in monolayer cell cultures at pH 6.4 and at 0 to 4 C. Hemagglutination was not affected by the cell type in which the virus was grown. Prerequisites for occurrence of hemagglutination are absence of hemagglutination inhibitors (such as those contained in bovine serum) and a relatively high virus concentration (> 10(6) plaque-forming units of virus per ml). "Soluble" hemagglutinin was not present in crude preparations of extracellular virus. Treatment of purified preparations of extracellular virus with Tween 80 and ether did not result in release of a "soluble" hemagglutinin. The hemagglutinating property of extracellular virus seemed to be conditioned by the integrity of its coat. Preparations of infectious intracellular virus exhibited about 15 times lower hemagglutinating activity than extracellular virus. This decreased hemagglutinating activity did not seem to be caused by binding of hemagglutination inhibitors to the virus particles. Rabies virus can be quantitatively adsorbed onto and eluted from erythrocytes. Erythrocytes pretreated with rabies virus retained their ability to be agglutinated by the same virus strain. The reaction with rabies virus of erythrocytes treated with the receptor-destroying enzyme or KIO(4) was the same as that of nontreated erythrocytes. The hemagglutinating component of rabies virus, therefore, does not exhibit neuraminidase activity. Treatment of extracellular virus by various agents indicated that the hemagglutinating component consists of protein or lipoprotein. Sulfhydryl groups present in the viral hemagglutinin are essential for hemagglutination.

Animals↗
PubMed1990

Hemagglutination and hemolysis by Escherichia coli isolated from bovine intramammary infections.

Seventy-six Escherichia coli isolated from bovine intramammary infections were tested for hemagglutination and hemolysis of erythrocytes. Fifty-seven percent of isolates were hemagglutination-positive for bovine erythrocytes compared with 46% that agglutinated guinea pig erythrocytes. Twenty-eight percent of isolates were hemagglutination-positive for erythrocytes from both species. Only 14.5 and 2.6% of isolates were mannose-resistant, hemagglutination-positive for bovine and guinea pig erythrocytes, respectively. Neither duration nor severity of infection from which isolates were obtained differed between isolates that were hemagglutination-positive and hemagglutination-negative. Percentage distribution of hemagglutination-positive isolates did not differ among isolates from infections that originated at calving, during lactation, or the first half of the dry period. Hemagglutination reactions were also not related to in vitro growth in cell-free dry cow secretion. Percent of isolates that caused hemolysis of washed bovine erythrocytes was 2.6% compared to 3.9% for sheep erythrocytes. Hemolysis was not related to hemagglutination. Hemagglutination and hemolysis of erythrocytes did not appear to be virulence factors for E. coli isolated from bovine intramammary infections.

Animals↗
PubMed1994

Hemagglutinating properties of enteroaggregative Escherichia coli.

Many intestinal bacterial pathogens possess hemagglutinating properties, which are indicative of their adhesive properties to the intestinal mucosal surface. To understand the bacteria-mucosa interaction, 41 strains of enteroaggregative Escherichia coli (EAggEC), a recently described category of diarrheagenic E. coli, isolated mostly from children with diarrhea in Bangladesh, India, Thailand, Central America, and South America were screened for mannose-sensitive hemagglutination and mannose-resistant hemagglutination of erythrocytes from humans, rats, mice, sheep, cattle, and rabbits. Some strains demonstrated mannose-sensitive hemagglutination of erythrocytes. Most isolates showed mannose-resistant hemagglutination of erythrocytes from all species except rabbits. The hemagglutination patterns could be classified into 18 groups. Studies with three selected isolates suggested that hemagglutinins are cell bound and are protein in nature. On the basis of the pattern of inhibition of hemagglutination by various chemicals, 39 isolates were classified into 19 groups. Hemagglutinations of many isolates were inhibited by sialic acid-containing compounds, suggesting that these compounds may be the receptors for these organisms on erythrocytes and possibly on the intestinal mucosa. These data indicate that strains of EAggEC are a heterogeneous group of organisms with different types of hemagglutinins or adhesins for the intestinal mucosal surface. Also, the adhesion characteristics of EAggEC strains may be too complex to be assessed by simple hemagglutination tests.

Adhesins, Escherichia coli↗
PubMed1980

Bluetongue virus hemagglutination and its inhibition by specific sera.

Bluetongue-virus (BTV) was found to agglutinate a variety of erythrocytes including sheep-, chicken-, guinea pig- and mouse-erythrocytes. Hemagglutination was inhibited specifically with type specific serum. A temperature dependence was only found for chicken erythrocytes, which showed a hemagglutination optimum at 37 degrees C. The hemagglutination was lost upon treatment of the virus with 0.4% trypsin as well as after treatment with 0.01 M KJO4. Heating of the virus preparation to 56 degrees C resulted in the loss of the HA-activity. Gelchromatographic studies indicated that the hemagglutinating capacity is associated with the complete virion. Whereas virulent strains of BTV hemagglutinate a number of different erythrocytes the avirulent type tested produced only a slight hemagglutination with sheep red blood cells. However, specific antiserum produced with the avirulent strain yielded strong hemagglutination inhibition (HI) with the corresponding virulent strain. Treatment of sera prior to their use in the HI proved necessary to remove nonspecific inhibitors. The efficiency of KJO4 in removing nonspecific inhibitors. The efficiency of KJO4 in removing nonspecific inhibitors indicates that carbohydrates represent the major group of nonspecific inhibitors. The data represented recommended the hemagglutination inhibition tests as a new method to identify the various BTV serotypes.

Animals↗
PubMed1989

Hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin isolated from chicken enterotoxigenic Escherichia coli.

The hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin (LTc-B) produced by chicken enterotoxigenic Escherichia coli was studied by hemagglutination and hemagglutination inhibition. No or weak hemagglutination of intact human erythrocytes was found by the LTc-B at the highest concentration used, whereas strong hemagglutination of both neuraminidase- and pronase-treated human erythrocytes was found. Enhancement in hemagglutination of treated human erythrocytes induced by the LTc-B was over 2 to 120-fold for type A and B erythrocytes and over 8-fold for type O erythrocytes, respectively. With intact and treated sheep erythrocytes, on the other hand, no hemagglutination was found by the LTc-B at the highest concentration used. Hemagglutination of pronase-treated human type B erythrocytes by the LTc-B was inhibited by methyl-alpha-D-galactopyranoside, galactose, melibiose, hog A + H, asialo-bovine salivary mucin and asialo-thyroglobulin among mono-, di- and polysaccharides and glycoproteins used as inhibitors. These results suggest that the LTc-B is a galactose-specific bacterial lectin.

Animals↗
PubMed1999

Characterization of the relationship between polysaccharide intercellular adhesin and hemagglutination in Staphylococcus epidermidis.

To determine whether a relationship exists between biofilm formation and hemagglutination in Staphylococcus epidermidis, 20 skin isolates and 19 prosthetic valve endocarditis isolates were characterized for biofilm formation, hemagglutination, and the presence of a 357-bp polymerase chain reaction product within icaA. A strong association existed between biofilm formation, which has been linked to strains that produce polysaccharide intercellular adhesin (PIA), and hemagglutination. Strains that produced biofilm were significantly (P<.001) more likely to mediate hemagglutination (16 biofilm-positive/hemagglutination-positive strains and 19 biofilm-negative/hemagglutination-negative strains) within the 39 clinical strains tested. In addition, Staphylococcus carnosus TM300, a biofilm-negative, hemagglutination-negative strain, carrying the ica operon-containing plasmid pCN27, produced significant biofilm on glass and mediated hemagglutination (>/=1/128). It was concluded that production of PIA and hemagglutination are strongly associated and that PIA, at least in part, mediates hemagglutination in S. epidermidis.

Adhesins, Bacterial↗
PubMed2004

Inhibition of Porphyromonas gingivalis hemagglutinating activity by synthetic peptides derived from phage display selection using MAb against the recombinant outer membrane protein.

Porphyromonas gingivalis has been implicated as an pathogen in the development of periodontitis, and hemagglutinins have been identified as an important adhesion onto the gingival tissue cells, and to attach and lyse erythrocytes to uptake Fe ion as an essential nutriant. The 40-kDa outer membrane protein (OMP) has been moleculary cloned from P. gingivalis 381. Since the antibody against recombinant (r) 40-kDa OMP inhibited the hemagglutinating activity, and the polymeric form of r40-kDa OMP itself expressed hemagglutinating activity, the 40-kDa OMP is thought to be one of the hemagglutinins. Moreover, we established MAbs against r40-kDa OMP which were capable of inhibiting hemagglutinating activity of P. gingivalis vesicles. In the present study, a phage-displayed epitope mapping system was used to identify the functional domain expressing hemagglutinating activity by biopanning using the neutralizing mAb, Pg-ompA1. The minimal epitope requirements of the MAb and the predicted amino acid sequences were identified in the region of (96)IALDQTLGIP(105) in 40-kDa OMP. Synthetic peptide, (87)WPRVGQLFIALDQTLGIPTFSVCRME(116), mapped the relevant molecule within a short stretch and is corresponding to residues of 40-kDa OMP. Chemically synthesized peptide was used to determine its inhibitory activity against hemagglutinating activity. The synthetic peptide significantly abolished hemagglutinating activity in a dose-dependent manner. These findings suggest that the synthetic peptide is an effective antagonist of erythrocyte binding, and this peptide may be a potent inhibitor of hemagglutination of P. gingivalis cells. The use of synthetic peptide neutralizing hemagglutinating activity of P. gingivalis represents a possible new therapeutic approach to P. gingivalis infected periodontitis.

Amino Acid Sequence↗
PubMed1983

Isolation and characterization of receptor sialoglycoprotein for hemagglutinating virus of Japan (Sendai virus) from bovine erythrocyte membrane.

Sialoglycoprotein which exhibits inhibitory activity for hemagglutination by Hemagglutinating Virus of Japan (HVJ, Sendai virus) was isolated from the membrane of bovine erythrocytes. Purification steps for this sialoglycoprotein included extraction with lithium diiodosalicylate, phenol partition, precipitation with ethanol, and chromatography on a phosphocellulose column and an SDS-Sepharose CL-4B column. Purified sialoglycoprotein (GP-2) has high specific activity for inhibiting the hemagglutination with HVJ, and a lesser activity for that with Newcastle disease virus, but it does not inhibit the hemagglutination by influenza A virus. Inhibitory activity of GP-2 on hemagglutination by HVJ is 2,500-fold higher than that of fetuin. Liposomes containing a 10,000-fold larger amount of ganglioside mixture of bovine erythrocytes and those containing a 5,000-fold larger amount of each ganglioside of bovine erythrocytes, N-glycolylneuraminosyl-lactosyl ceramide, sialosyllacto-N-neotetraosyl- and sialosyl-lacto-N-norhexaosyl ceramide, had no inhibitory activity toward hemagglutination with HVJ. GP-2 (mol. wt. 250 K daltons) behaved homogeneously in SDS-polyacrylamide gel electrophoresis. It contained 70% carbohydrate and 30% protein, by weight. N-Acetylgalactosamine, N-acetylglucosamine, galactose, sialic acid (N-glycolylneuraminic acid, 96%; N-acetylneuraminic acid, 4%) were identified as carbohydrate components, in molar ratios of 1.0:4.0:5.2:2.9. All the oligosaccharides of GP-2 appeared to be linked to polypeptide chains by alkali-labile O-glycosidic linkages. Sialidase treatment of GP-2 and conversion of sialic acid residue of the glycoprotein to C8 and C7 analogues resulted in the loss of the inhibitory activity on hemagglutination by HVJ. Oligosaccharides isolated by gel filtration after treatment of GP-2 with alkaline borohydride had also lost the ability to inhibit the hemagglutination by HVJ. The above results indicate that isolated sialoglycoprotein is the endogenous receptor in bovine erythrocyte membrane specific to HVJ, and the hydroxy group linked to the 9-carbon atom of sialic acid and probably also the hydrophobic protein moiety are important for the recognition of HVJ attachment.

Animals↗
PubMed1993

Herpes simplex virus type 1-induced hemagglutination: glycoprotein C mediates virus binding to erythrocyte surface heparan sulfate.

We recently reported that herpes simplex virus type 1 (HSV-1) can cause agglutination of murine erythrocytes (E. Trybala, Z. Larski, and J. Wisniewski, Arch. Virol. 113:89-94, 1990). We now demonstrate that the mechanism of this hemagglutination is glycoprotein C-mediated binding of virus to heparan sulfate moieties at the surface of erythrocytes. Hemagglutination was found to be a common property of all gC-expressing laboratory strains and clinical isolates of HSV-1 tested. Mutants of HSV-1 deficient in glycoprotein C caused no specific hemagglutination, whereas their derivatives transfected with a functional gC-1 gene, thus reconstituting gC expression, regained full hemagglutinating activity. Hemagglutination activity was inhibited by antibodies against gC-1 but not by antibodies with specificity for glycoproteins gB, gD, or gE or by murine antiserum raised against the MP strain of HSV-1, which is gC deficient. Finally, purified gC-1 protein, like whole HSV-1 virions, showed high hemagglutinating activity which was inhibited by heparan sulfate and/or heparin and was completely prevented by pretreatment of erythrocytes with heparitinase, providing evidence that gC-1 mediates hemagglutination by binding to heparan sulfate at the cell surface. Thus, HSV-1-induced hemagglutination is gC-1 dependent and resembles the recently proposed mechanism by which HSV-1 attaches to surface heparans on susceptible cells, providing a simple model for initial events in the virus-cell interaction.

Animals↗
PubMed1982

Indirect hemagglutination test in equine infectious anemia.

An indirect hemagglutination was developed for the diagnosis of equine infectious anemia using sheep red blood cells coated with group specific virus antigen which had been highly purified by affinity chromatography. The presence of indirect hemagglutination antibodies was demonstrated in horses with equine infectious anemia since the cells were specifically agglutinated by all the serum samples obtained from experimentally infected horses. Antibodies appeared within 35 days after inoculation, and development of which coincided well with that of precipitating and complement fixing antibodies. Titer of indirect hemagglutination antibodies were ten to 320 times greater than those of precipitating antibodies. Test results could be read more clearly by the indirect hemagglutination test especially in weakly positive cases. Ninety-six samples from suspected field cases collected from every region of Japan which were positive on the immunodiffusion test were also positive on indirect hemagglutination test. Serum samples from 420 horses in one race track were examined by both the indirect hemagglutination and immunodiffusion tests to determine the reliability of the indirect hemagglutination test for diagnosis of equine infectious anemia. The same result was obtained on both tests. Based on this evidence, the indirect hemagglutination test can be employed as a very sensitive serological test for the diagnosis of equine infectious anemia.

Animals↗
PubMed1975

Bacterial hemagglutination by Neisseria gonorrhoeae.

Direct bacterial hemagglutination was investigated with 20 clinical isolates of Neisseria gonorrhoeae. The hemagglutination tests were performed by both a macrotechnique with glass slides and a microtechnique with autotrays. Only organisms from form type 1 or 2 colonies caused hemagglutination. There was no statistical difference at a 10% or higher level in hemagglutination powers of type 1 and type 2 organisms, of male urethral and female cervical isolates, and of the eight major human blood types (ABO-Rh). Of seven erythrocyte species tested, only human cells were agglutinated. D-Mannose did not prevent the agglutination. Rabbit antigonococcal serum and high-titer antigonococcal human sera inhibited the hemagglutination. The results suggest the pili are the mediators of hemagglutination and that their specific agglutination of human erythrocytes may be a correlate of their adherence to human mucosal cells in natural infection. Also, although the procedure is presently insensitive, it is possible to detect human antigonococcal antibody by inhibition of direct bacterial hemagglutination.

Animals↗
PubMed1952

Studies on hemagglutination and hemolysis by escherichia coli antisera.

A study on hemagglutination and hemolysis by Escherichia coli O111 and O55 (rabbit) antisera and on hemagglutination and hemolysis inhibition by E. coli O111 and O55 antigens revealed the following facts. 1. Red blood cells of man, dog, rabbit, guinea pig, sheep, rat, and chicken adsorb E. coli O111 and O55 antigens and thus become specifically agglutinable by the homologous E. coli antisera. 2. The adsorption of these E. coli antigens is a function of the concentration of the antigen, the time (from 5 minutes to 2 hours) of treatment of the red blood cells with the antigen, and the concentration of the red blood cells used. 3. Red blood cells of man and sheep adsorb simultaneously both antigens, as indicated by the fact that both antisera give agglutination of all red blood cells. Complete agglutination does not occur when a mixture of red blood cells treated separately with the two antigens is added to one or the other of the two antisera. 4. Treatment of red blood cells of man with one of the antigens does not block the adsorption of the second antigen. Human cells treated with either or both antigens are still agglutinated by the homologous blood group (A, B, and Rh)-specific antibodies. 5. In the presence of guinea pig complement, E. coli O111 and O55 antisera produce hemolysis of modified human red blood cells in titers of the same order of magnitude as those giving hemagglutination and bacterial agglutination. The same antisera produce hemolysis of sheep cells treated with the identical antigens in titers exceeding by far those giving agglutination of modified human or sheep red blood cells. 6. Both sediment and supernate of a boiled E. coli suspension are capable of modifying red blood cells for E. coli hemagglutination; in contrast, the supernate obtained from an unboiled suspension and then heated does not modify red blood cells for hemagglutination, although it contains the antigen which can specifically adsorb E. coli antibodies, as shown by means of the hemagglutination and hemolysis inhibition tests. 7. Both the unheated and the boiled suspensions of E. coli O111 and O55 inhibit hemagglutination and hemolysis specifically. 8. Rabbit red blood cells modified by either E. coli O111 or 055 antigens, upon intravenous injection into rabbits, engender specific E. coli antibodies. The significance of the results is discussed.

Animals↗
PubMed2004

Effects of denaturation and amino acid modification on fluorescence spectrum and hemagglutinating activity of Hericium erinaceum Lectin.

A sialic acid-binding lectin (Hericium erinaceum lectin, HEL), isolated from fresh fruiting bodies of Hericium erinaceum, was treated with various temperature and pH to investigate its fluorescence spectra and hemagglutinating activity. It was found that the hemagglutinating activity of HEL was relatively steady below 60 degrees and at pH from 6 to 11, and the change of hemagglutinating activity was relative to the change of hydrophobic areas where tryptophan residues located. In fluorescence quenching study of HEL by acrylamide and KI, it was indicated that nearly all the tryptophan residues of HEL located on the surface of the molecule, and most of them were in hydrophobic areas or negatively charged areas. Chemical modification of HEL proved that there were about twelve tryptophan residues in a HEL molecule and all of them were located on the surface or in the shallow groove of the molecule, and eight of them were essential for hemagglutinating activity; aspartic acid or glutamic acid residues were involved in maintaining the crucial conformation of activity center and made great contribution to the hemagglutinating activity of HEL, but they could not touch the sialic acid molecule directly; tyrosine residues also played a role in the hemagglutinating activity of HEL; while arginine, serine, threonine, histidine residues had no effect on the hemagglutinating activity of HEL.

Amino Acid Sequence↗
PubMed1992

Hemagglutination activity of Treponema denticola grown in serum-free medium in continuous culture.

Hemagglutination by different Treponema denticola strains was observed for erythrocytes of human, horse, bovine, and rabbit origin. The growth of T. denticola ATCC 33520 in serum-free medium in continuous culture enabled us to study the hemagglutinating activity of freshly harvested spirochetes of a defined physiological status. The hemagglutinating activity was cell bound and not related to motility or appendages, such as fimbriae. The activity was destroyed by proteolytic enzymes, heat, and alkylation, indicating that the agglutinin is of a proteinaceous nature. In addition, periodate oxidation of the spirochetes indicated the involvement of carbohydrate groups. Microscopic inspection of the hemagglutination mixtures at the titration endpoints revealed that only a part of the spirochete population was involved in the hemagglutination process. The hemagglutinating activity was found to be growth phase related. The activity was blocked by serum, while of all tested amino acids and carbohydrates, only sialic acid blocked the activity at low concentrations. In conclusion, we found a hemagglutinating activity in T. denticola which was cell bound and growth phase related. The agglutinin may be a glycoprotein, like lectin, that recognizes sialic acid as a receptor.

Animals↗
PubMed1994

Characterization of hemagglutinating components on the Anaplasma marginale initial body surface and identification of possible adhesins.

Interaction of Anaplasma marginale initial bodies with the bovine erythrocyte surface was examined by a direct hemagglutination assay. Purified initial bodies were shown to specifically hemagglutinate bovine erythrocytes but not erythrocytes from nonhost animal species. Hemagglutination was inhibited by treatment of purified initial bodies with trypsin, alpha-chymotrypsin, or proteinase K but not by treatment with neuraminidase or sodium periodate. Treatment of bovine erythrocytes with alpha-chymotrypsin or neuraminidase partially inhibited hemagglutination of the treated cells by initial bodies. In contrast, no inhibition occurred after treatment of erythrocytes with trypsin, phospholipases, or sodium periodate or when monosaccharides and disaccharides were used as potential competitive inhibitors. Thus, the initial body receptor is probably a surface protein, whereas the bovine receptor may comprise both protein and carbohydrate. Hemagglutination was unaffected by treatment of initial bodies with monoclonal or polyclonal antibodies raised against the A. marginale 31-kDa (MSP4) major surface polypeptide or non-A. marginale proteins or by treatment with a monoclonal antibody to the A. marginale MSP1a neutralization-sensitive epitope. In contrast, antiserum raised against whole A. marginale initial bodies or monospecific antibodies raised against purified A. marginale major surface polypeptides with molecular sizes of 105 (MSP1a), 100 (MSP1b), 61, and 36 (MSP2) kDa completely or partially inhibited hemagglutination. These data confirm the proposed surface location of the proteins susceptible to inhibition and suggest that they mediate hemagglutination of bovine erythrocytes. We propose that these surface proteins are possible adhesins.

Anaplasma↗
PubMed1998

Molecular characterization of hemagglutination domains on the fibers of subgenus D adenoviruses.

The adenovirus fiber mediates the agglutination of erythrocytes. Based on differential hemagglutinating properties, subgenus D adenoviruses can be subdivided into clusters DI, DII, and DIII. While subgenus DI adenoviruses agglutinate rat and human erythrocytes, DII adenoviruses simply agglutinate rat erythrocytes and DIII adenoviruses display no or only weak rat erythrocyte agglutination. Amino acid sequence comparisons revealed distinct domains on the fiber knob which could be involved in hemagglutination. In order to localize and characterize the domains responsible for the interaction with rat and human erythrocytes, potential hemagglutination domains of the adenovirus type 9 (Ad9) (subgenus DI) fiber knob were introduced into Ad17 (subgenus DII) and Ad28 (subgenus DIII) fiber knobs by primer-directed mutagenesis. Furthermore, rat erythrocyte hemagglutination domains were also introduced into the Ad3 (subgenus B) fiber knob, which only agglutinated monkey erythrocytes. Altogether, 27 chimeric and mutated fiber proteins were expressed in Escherichia coli and subsequently tested for hemagglutination activity. The hemagglutination tests revealed that at least two domains can mediate the agglutination of rat erythrocytes. While one domain is located on the GH loop, the other domain extends from the C beta strand to the CD loop. The domain on the GH loop was partially conserved in all adenoviruses showing an incomplete hemagglutination pattern with rat erythrocytes. The domains involved in the agglutination of human erythrocytes are located on the CD and HI loops of the subgenus DI fiber knob.

Adenoviruses, Human↗
PubMed1975

Hemagglutinating properties of Salmonella typhimurium strains isolated from avian sources.

A total of 565 strains of Salmonella typhimurium and S. typhimurium var. copenhagen, isolated from avian species, were examined for their ability to cause hemagglutination of turkey erythrocytes. Results showed that 541 (95.7%) of the strains caused varying degrees of hemagglutination. The hemagglutinating principle was maintained in cultures stored at 5 degrees C. as formalized suspensions for as long as 6 months. It was destroyed by exposure to a temperature of 80 degrees C. for 1 minute or to absolute ethyl alcohol at 37 degrees C. for 24 hours. The hemagglutinating principle was best preserved in cultures by infrequent transfers, growth in liquid media, lyophilization or storage at low temperatures. Addition of d-mannose to bacteria-erythrocyte mixtures at a final concentration of 0.5% completely inhibited the hemagglutinating activity of the cultures. A concentration of 1% d-mannose added to crystal-violet-stained antigen preparations of S. typhimurium eliminated entirely the hemagglutinating effect of positive cultures and did not interfere with regular agglutination reactions. The hemagglutinating activity of S. typhimurium strains is apparently due to the presence of rigid appendage (fimgriae) on the surface of the bacterial cells. Results from these studies showed that fimbriated cultures are quite common among strains of S. typhimurium.

Animals↗
PubMed1986

Microtiter latex agglutination--quantitative and qualitative equivalent to hemagglutination inhibition for detection of rubella antibody.

Sera were tested for rubella antibody by a standard hemagglutination inhibition method and by latex agglutination in microtiter plates (Virogen Rubella Micro Test). When 157 sera were examined by hemagglutination inhibition and by microtiter latex agglutination for immune status, 149 of the results agreed. The eight discrepant sera (all hemagglutination inhibition-negative, latex agglutination-positive) were tested by a card latex agglutination method (Rubascan) and a passive hemagglutination method (Rubacell). Results, except where noted, agreed with those of the microtiter latex agglutination. One hundred forty-eight of the 149 sera that were in agreement as to immune status were also within a fourfold variation when hemagglutination inhibition and latex agglutination titers were compared. An additional 100 sera were tested for immune status by microtiter latex agglutination and by passive hemagglutination with the single discrepant result agreeing with the latex agglutination when tested by a third method. Both microtiter latex agglutination and hemagglutination inhibition agreed in detection of fourfold or greater rises in each of 20 paired sera.

Antibodies, Viral↗