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PubMed1977

Rickettsial hemolysis: adsorption, desorption, readsorption, and hemagglutination.

The energy-dependent adsorption of radioiodinated rickettsiae to sheep erythrocytes was demonstrated. The iodination procedure, however, decreased the hemolytic activity of the rickettsiae. No desorption of rickettsiae from isolated rickettsia-erythrocyte complexes (prevented from lysing by NaF) could be measured. On the other hand, rickettsiae desorbed from this complex during or after lysis and readsorbed and lysed other erythrocytes. Thus, the usual hemolytic assay measures multiple rounds of adsorption and lysis. Although lysis of the rickettsia-erythrocyte complex was insensitive to anti-rickettsial rabbit serum, adsorption and readsorption were completely inhibited by such antiserum. Hemagglutination of erythrocytes by rickettsiae was observed (in the presence of NaF to prevent lysis) and was sensitive to the same inhibitors as adsorption.

Adsorption↗
PubMed1977

Hemagglutination of human group A erythrocytes by enterotoxigenic Escherichia coli isolated from adults with diarrhea: correlation with colonization factor.

Enterotoxigenic Escherichia coli (ETEC) of several different serotypes isolated from adults with diarrhea and known to possess the colonization factor antigen (CFA) were found to cause mannose-resistant hemagglutination (HA) of human group A erythrocytes. CFA-negative E. coli isolated during the same study did not possess the mannose-resistant hemagglutinin, although some non-ETEC, CFA-negative isolates did exhibit mannose-sensitive HA activity. The mannoseresistant hemagglutinin of ETEC was found to possess many characteristics previously associated with CFA, which is a surface-associated fimbriate heatlabile antigen, and the functionally and morphologically similar K88 and K99 antigens of animal-specific ETEC. Mannose-resistant HA and CFA titers were maximal when ETEC cells were grown on an agar medium (CFA agar) composed primarily of 1% Casamino Acids and 0.15% yeast extract, pH 7.4. Neither CFA nor HA were produced at a growth temperature of 18 degrees C; HA was completely inhibited by pretreatment of CFA-positive cells with the anti-CFA serum. The mannose-resistant hemagglutinin was lost spontaneously and simultaneously with CFA when clinical ETEC isolates were passaged on artificial medium in the laboratory, indicating plasmid control of both entities. The mannose-resistant hemagglutinin of ETEC was shown to be thermolabile, i.e., sensitive to heating at 65 degrees C, as was the CFA. Also, there was correlation between possession of CFA, as detected serologically and by demonstration of biological activity (adherence in the infant rabbit small intestine), presence of CFA-type fimbriae, and the ability of various E. coli isolates to cause mannose-resistant HA of human group A erythrocytes. These results indicate that the mannose-resistant HA of ETEC is another manifestation of CFA.

Agglutinins↗
PubMed1980

Ciliostatic, hemagglutinating, and proteolytic activities in a cell extract of Mycoplasma pneumoniae.

An extract of Mycoplasma pneumoniae, prepared from glass-grown organisms by extraction with 2 M NaCl, followed by freeze-thaw, ultracentrifugation, dialysis, and lyophilization, yielded approximately 20% of the total mycoplasmal protein. The extract contained at least 20 protein bands on sodium dodecyl sulfate-polyacrylamide gels and 2 to 5% carbohydrate and inhibited 70 to 100% of the ciliary activity of hamster tracheal organ cultures (ciliostasis). The extent of ciliostasis was dependent on the concentration of the extract. The extract also produced hemagglutination of human O-positive erythrocytes and showed proteolytic activity with a synthetic tetrapeptide substrate, S-2222. These in vitro tissue-damaging activities may be associated with the virulence of the mycoplasmas and with the pathogenesis of M. pneumoniae disease.

Animals↗
PubMed1981

Antigenic characterization of human and animal rotaviruses by immune adherence hemagglutination assay (IAHA): evidence for distinctness of IAHA and neutralization antigens.

An immune adherence hemagglutination assay (IAHA) and a modified enzyme-linked immunosorbent assay for antigenic characterization of human rotaviruses were developed. The designations of type 1 and type 2 were identical to those established previously by specific complement fixation, enzyme-linked immunosorbent assay, and immune electron microscopy. By IAHA (and modified enzyme-linked immunosorbent assay) certain animal rotaviruses were found to be closely related to human rotavirus type 1. The pattern of IAHA reactivity and the cell culture neutralization serotype were found to be distinct properties. The separation of neutralization and IAHA reactivity was apparent when animal rotaviruses which were distinguishable from each other by neutralization assays were found to share IAHA specificity. Further evidence for the dissociation of the neutralization and IAHA specificities was found in studies of human and bovine rotaviruses which underwent genetic reassortment during coinfection. Thus, it appeared that the IAHA and neutralization antigens were coded for by different genes. In view of these findings, we suggest that the term serotype be reversed to identify the antigen that reacts with neutralizing antibodies as is customary for other viruses and that the term subgroup (instead of serotype) be used for the specificity detected by specific complement fixation, enzyme-linked immunosorbent assay, and now IAHA.

Animals↗
PubMed1983

Receptor-like glycocompounds in human milk that inhibit classical and El Tor Vibrio cholerae cell adherence (hemagglutination).

The two biotypes of Vibrio cholerae were found to have cell-associated hemagglutinins which differ with regard to binding to different species of erythrocytes and inhibition by monosaccharides. A total of 12 classical V. cholerae strains (Inaba or Ogawa) strongly agglutinated human erythrocytes in a reaction specifically inhibited by L-fucose, whereas 12 El Tor strains preferably agglutinated chicken erythrocytes, a reaction reversed by D-mannose or by higher concentrations of D-fructose, D-glucose, alpha-methyl-D-mannoside, or sucrose. Milk from Swedish women inhibited both of these adherence reactions, and the predominating inhibitory activity for each reaction resisted boiling, was destroyed by periodate treatment, and bound a concanavalin A-Sepharose column, suggesting a carbohydrate structure. Further characterization indicated that the inhibitory activity for classical V. cholerae hemagglutination was distributed about equally on glycoprotein and free oligosaccharide, but was not present on glycolipid. The El Tor inhibiting activity, on the other hand, was almost exclusively of a high-molecular-weight glycoprotein nature. These results support our previous suggestion (Holmgren et al., Infect. Immun. 33:136-141, 1981) that human milk may contain receptor-like glycocompounds which can prevent bacterial adherence by competition with receptors on target cells.

Binding Sites↗
PubMed1984

Gene clusters governing the production of hemolysin and mannose-resistant hemagglutination are closely linked in Escherichia coli serotype O4 and O6 isolates from urinary tract infections.

The genes encoding alpha-hemolysin and mannose-resistant hemagglutination were shown to be closely linked in cloned DNA from two Escherichia coli urinary tract isolates of serotypes O4 (J96) and O6 (C1212). DNA hybridization experiments demonstrated that the hly and mrh gene clusters of other E. coli O6 serotypes were also linked. Colony hybridizations showed that most normal fecal E. coli do not contain hly and mrh DNA but much of the intervening DNA between these two gene clusters is common among all E. coli. We have further demonstrated that there is a small (about 1 kilobase) region of homology located on both sides of the hly sequence and present elsewhere in the C1212 strain. We suggest that linkage of hly and mrh occurred through a transposition event, and we discuss the potential significance of this linkage in the acquisition of virulence determinants by these bacteria.

Base Sequence↗
PubMed1972

Hemagglutination assay of antibodies associated with pulmonary acariasis in rhesus monkeys (Macaca mulatta).

Antibodies associated with infection by lung mites (Pneumonyssus simicola) in rhesus monkeys were measured by passive hemagglutination methods. Tanned human Rh negative O red blood cells or sheep red blood cells coated with soluble acarine antigens were used to detect mite-specific antibodies. Large quantities of host-specific mite antigens (P. simicola) were difficult to obtain, so free-living mite species such as Dermatophagoides farina, Acarina sheldonii, and Tyrophagus putrificiensis were also utilized. Although the best serological specificity and sensitivity were obtained with P. simicola and its derivatives (1:640), several free-living acarine species were useful in detecting antibodies to mites. Skin tests carried out on a limited number of animals were positive for both immediate and delayed hypersensitivity.

Age Factors↗
PubMed1989

Involvement of the MN blood group antigen in shear-enhanced hemagglutination induced by the Escherichia coli F41 adhesin.

An adhesin from Escherichia coli F41 with an apparent subunit molecular weight of 28,000 daltons was isolated by using (NH4)2SO4 precipitation at pH 10 and Sephacryl S-500 gel filtration. The hemagglutination (HA) properties of the native high-molecular-weight adhesin were studied by using a viscometric assay, which provided a quantitative index of the degree of agglutination present as a function of time at a known rate of shear. Shear was found to enhance the degree of agglutination over a 20-min period. A strong, shear-enhanced HA was observed for all donors with the MM or MN blood type studied, but those with the NN blood type showed very little HA. In the microtiter HA assay, the selectivity of the adhesin for MM over NN erythrocytes was found to be dependent on pH and temperature. At 21 degrees C and pH 7.4, there was little difference in HA between the two blood types, but NN cells were progressively more weakly agglutinated than MM cells as the pH or the temperature was increased. Glycophorin A, which bears the M or N determinant, was isolated from individuals with the MM and NN blood types and was shown to be an effective inhibitor of the reaction, with the MM type being the more effective in both microtiter and viscometric assays. Acidic monosaccharides, particularly sialic acid, were also effective inhibitors of HA, although they were less potent on a molar basis than glycophorin. The adsorption isotherm of 125I-labeled adhesin was measured, and the binding was shown to be strongly inhibited by MM glycophorin and somewhat less strongly by NN glycophorin. Collectively, these data strongly suggest that glycophorin AM is a receptor for the F41 adhesin.

Adhesins, Escherichia coli↗
PubMed1972

Hemagglutination by BK virus, a tentative new member of the papovavirus group.

Some characteristics of hemagglutination (HA) by the BK virus, a new candidate for the papovavirus group, have been studied. Hemagglutinin prepared from cell cultures was found to be partially masked by inhibitors which could be dissociated from the virus by incubation at 37 C or by fluorocarbon extraction. Optimal conditions for HA are outlined. In routine tests, 0.5% human erythrocytes were used. The reaction was carried out at pH 7.0 on ice-water slurry. BK hemagglutinin receptors on human erythrocytes were found to be more resistant to neuraminidase than polyoma receptors. By gradient centrifugation analysis, two types of particles were found to be responsible for HA: (i) full, deoxyribonucleic acid-containing particles with a density of 1.325 g/cm(3) and (ii) empty capsids with a density 1.29 g/cm(3). Based on particle counting, one HA unit was calculated to correspond to 3 x 10(6) virus particles.

Agglutinins↗
PubMed1992

Aggregative adherence fimbriae I of enteroaggregative Escherichia coli mediate adherence to HEp-2 cells and hemagglutination of human erythrocytes.

Strains of enteroaggregative Escherichia coli (EAggEC) have been implicated in several studies as important agents of persistent diarrhea among infants in the developing world. We have previously shown that the aggregative adherence (AA) property of EAggEC is associated with the presence of a 60-MDa plasmid which confers AA when introduced into E. coli HB101. Here, we report the cloning of the AA determinant from EAggEC strain 17-2 into the 21.5-kb cosmid vector pCVD301. TnphoA mutagenesis of the AA cosmid clone pJPN31 implicated an AA region of approximately 12 kb. Transmission electron microscopy of HB101 (pJPN31) revealed the presence of bundle-forming fimbriae, which were absent in AA- TnphoA insertion mutants. The presence of these fimbriae, AA, and hemagglutination (HA) of human erythrocytes were all concurrently lost by single-insertion mutations. A 14-kDa protein was seen on polyacrylamide gel electrophoresis and Western blotting (immunoblotting) of surface shear preparations from fimbriated clones. Twelve of nineteen volunteers fed EAggEC 17-2 developed rises in antibodies to the 14-kDa protein as determined by Western blot. We have termed the cloned bundle-forming fimbriae aggregative adherence fimbriae I (AAF/I); positivity with a previously described EAggEC probe and human erythrocyte HA appear to correlate with the presence of AAF/I.

Antibodies, Bacterial↗
PubMed1997

Identification of a Fusobacterium nucleatum PK1594 galactose-binding adhesin which mediates coaggregation with periopathogenic bacteria and hemagglutination.

Attachment of Fusobacterium nucleatum to various oral surfaces is mediated by several adhesins anchored on its outer surface. Monoclonal antibodies (MAbs) were prepared and used to identify the putative galactose-binding adhesin of F. nucleatum PK1594. Four unique MAbs, 8G7, 26B9, 28G11, and 29D4, were isolated on the basis of their ability to inhibit coaggregation of F. nucleatum PK1594 with Porphyromonas gingivalis PK1924. All four MAbs were also capable of inhibiting galactose-inhibitable interactions of F. nucleatum PK1594 with other oral gram-negative bacteria and with erythrocytes. Preincubation of F. nucleatum PK1594 with MAb 26B9 or its Fab fragments at concentrations lower than 1 microg/ml resulted in complete inhibition of coaggregation with P. gingivalis PK1924 or hemagglutination. F. nucleatum PK1594 surface components prepared by mild sonication or by extracting whole cells with detergents were subjected to Western blot analysis. None of the MAbs were able to recognize any polypeptide in these experiments. Therefore, detergent extracts of F. nucleatum PK1594 surface components were subjected to three experimental procedures: (i) separation by ion-exchange chromatography and testing of fractions for reaction with MAb 26B9 in an enzyme-linked immunosorbent assay (ELISA), (ii) lactose-Sepharose affinity chromatography and testing of the lactose eluate in ELISA with MAb 26B9, and (iii) immunoseparation with either MAb 26B9 or 8G7. Collectively, the results suggest that the putative adhesin is a 30-kDa outer membrane polypeptide which mediates the coaggregation with P. gingivalis PK1924 as well as other galactose-sensitive interactions of F. nucleatum PK1594.

Adhesins, Bacterial↗
PubMed1973

Passive hemagglutination test for bovine chlamydial abortion.

Purified chlamydial elementary bodies were subjected to sonic lysis to produce soluble antigen for passive hemagglutination (PHA). PHA was more sensitive than complement fixation (CF) in detecting antibody in hyperimmunized rabbits, lambs, and calves. Both CF and PHA tests were used to monitor antibody responses in experimentally infected pregnant cows. All animals responded with rises in titers after experimental infection. Titers declined and then increased a second time near the time of abortion. PHA titers were considerably higher than CF titers.

Abortion, Veterinary↗
PubMed1973

Hemagglutination-inhibition test in rhinovirus infections of volunteers.

The hemagglutination-inhibition (HI) test for antirhinovirus antibody was carried out on paired sera from volunteers inoculated with rhinovirus type 3 or type 4 (RV4). The HI test gave results which paralleled the neutralization test and was at least as sensitive as a microneutralization method for detection of serotype-specific antibody. Although high levels of HI antibody in the serum were associated with protection from infection, in the case of RV4 low serum HI antibody levels did not necessarily imply susceptibility to challenge with small doses of virus. HI activity could be measured in concentrated nasal-washing fluids, and this antibody also seemed relevant to protection against infection.

Adolescent↗
PubMed1980

Agglutination of human erythrocytes by Fusobacterium nucleatum: factors influencing hemagglutination and some characteristics of the agglutinin.

Various aspects of agglutination of human erythrocytes by fusobacterium nucleatum were examined. Titration experiments done in buffered saline at pH 6 to 10 showed the same agglutination endpoint. The presence of high concentrations of NaCl in reaction mixtures did not alter titers, but KCl in concentrations of 0.5 to 3.6 M increased titers twofold. The agglutinin was inactivated by heat, acid, alkali, 5% Formalin, and the proteolytic enzyme subtilopeptidase A and therefore appeared to be a protein. Treatment of bacterial cells with 2-mercaptoethanol had no effect. Hemagglutination inhibition experiments revealed that arginine and other compounds containing a guanido group as part of their structure were inhibitory at low concentrations. Various hexoses, some hexose derivatives, and most common metal ions, when added to bacterium-erythrocyte mixtures, had no effect. The binding of dansyl-L-arginine to bacteria, but not erythrocytes, was demonstrable by ultraviolet fluorescence microscopy.

Agglutinins↗
PubMed1967

Differences between Brucella antigens involved in indirect hemagglutination tests with normal and tanned red blood cells.

Brucella antigens capable of sensitizing normal and tanned sheep red blood cells for indirect hemagglutination were compared with antigens involved in agglutination, gel diffusion, and immunoelectrophoresis. Hyperimmune rabbit sera, before and after absorption with various antigenic preparations from smooth and rough B. abortus, were used in the tests. Normal erythrocytes could be sensitized with an NaOH-treated ether-water extract (EW-T) of smooth Brucella. Tanned erythrocytes could be sensitized with a water-soluble extract from ultrasonically disrupted smooth or rough Brucella. The EW-T produced a single precipitation band and the water-soluble antigens produce 6 to 23 bands in immunoelectrophoresis with unabsorbed sera. After absorption of antisera with water-soluble extracts from smooth or rough Brucella cells or from smooth or rough cell walls, the hemagglutinins for sensitized tanned erythrocytes and the precipitins for water-soluble antigens were removed. Absorption with living smooth or rough Brucella cells or with EW-T did not remove these antibodies. The precipitins and hemagglutinins for the antigen EW-T, and agglutinins for smooth cells, were absorbed by smooth antigens but not by rough antigens. It appears that the antigens which sensitize tanned erythrocytes and diffuse through agar gels are present in both smooth and rough forms and may be situated in the cytoplasm or in the internal part of the cell wall, whereas the agglutinogen and the antigen which attaches to normal erythrocytes are surface antigens found only on the smooth Brucella cell.

Animals↗
PubMed1968

Serological activity of protein A of Staphylococcus aureus: the precipitinogen as an antigen for determining antibodies by the passive hemagglutination test.

Tanned sheep erythrocytes have been considered incapable of sensitization with the precipitinogen of protein A of Staphylococcus aureus, so that the activity of this antigen in serological reactions has so far been studied by means of the agar diffusion test (ADT) only. The precipitinogen of the protein A in this study was found to become attached to the tanned erythrocytes and to sensitize them for the passive hemagglutination test (PHT). It was determined that, in contrast to nonspecific reactivity between normal human serum and the precipitinogen in the ADT, the reaction in the PHT was of specific nature. Of seven species studied, all normal human, dog, and hog sera tested were positive in the PHT. However, the hemagglutinin titers of the sera of the two animal species by far exceeded those of the human sera. The data emphasized the usefulness of the highly sensitive PHT for assaying antibodies to protein A.

Animals↗
PubMed1980

Indirect hemagglutination employing enterobacterial common antigen and Yersinia somatic antigen: a technique to differentiate brucellosis from infections involving cross-reacting Yersinia enterocolitica.

The existence of enterobacterial common antigen in Yersinia enterocolitica and its absence in Brucella abortus were utilized in an attempt to provide a method to distinguish Brucella infections from infections with cross-reacting Yersinia. The indirect hemagglutination test was employed for this purpose. In experimental laboratory animals, the presence of anti-enterobacterial common antigen was found to be indicative of prior exposure to Y. enterocolitica rather than B. abortus. In cattle, however, low titers of anti-enterobacterial common antigen were present in all animals. It was observed that anti-enterobacterial common antigen titers either equaled or exceeded anti-Yersinia O titers in Yersinia-exposed animals, whereas in animals infected with B. abortus the anti-Yersinia O titer generally exceeded the anti-enterobacterial common antigen titer.

Animals↗