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PubMed1964

BINDING OF AN ALPHA GLOBULIN TO HYALURONATEPROTEIN IN PATHOLOGICAL SYNOVIAL FLUIDS.

Rabbits were immunized with hyaluronateprotein isolated from normal or pathological synovial fluids. Immunoelectrophoresis of hyaluroni-dase-digested pathological hyaluronateprotein and its antiserum showed a single precipitin arc extending through both alpha globulin zones. Digested normal hyaluronateprotein formed no lines with either its antiserum or with that to pathological hyaluronateprotein. The antigenic component present in pathological hyaluronateprotein formed a reaction of complete fusion with a serum protein which was identified by immunoelectrophoresis as an alpha globulin.

Alpha-Globulins↗
PubMed1962

Changes in immunodiffusion patterns and in nucleic acid content of Staphylococcus aureus grown in the presence of a nucleic acid fluorochrome.

Sonea, S. (University of Montreal, Montreal, Canada), J. de Repentigny, and A. Frappier. Changes in immunodiffusion patterns and in nucleic acid content of Staphylococcus aureus grown in the presence of a nucleic acid fluorochrome. J. Bacteriol. 84:1056-1060. 1962.-When grown in the presence of acridine orange, coagulase-positive Staphylococcus aureus exhibits changes in the number and the shape of its precipitin bands; these are more pronounced with commercial horse staphylococcal antitoxin than with normal human gamma-globulin. Simultaneously, there is an increase in the content of nucleic acids, especially deoxyribonucleic acid. Consequently, when grown in the presence of this nucleic acid fluorochrome, pathogenic staphylococci become similar to nonpathogenic strains in their antigenic structure and nucleic acid content. The bacterial population becomes a mixture of red and green fluorescing cells of different sizes. After centrifugation, most of the large and red fluorescing cells are found in the top layer, which shows more changes in antigenic composition and in nucleic acid content than the bottom layer. In subcultures grown in the absence of acridine orange, the cells revert to the original composition of the pathogenic strains.

Acridines↗
PubMed1963

IMMUNOLOGICALLY ACTIVE POLYSACCHARIDES FROM NOCARDIA ASTEROIDES AND NOCARDIA BRASILIENSIS.

Zamora, A. (University of Mexico, Mexico, D.F.), L. F. Bojalil, and Fernando Bastarrachea. Immunologically active polysaccharides from Nocardia asteroides and Nocardia brasiliensis. J. Bacteriol. 85:549-555. 1963.-Two immunologically active polysaccharides were isolated from Nocardia asteroides (Poly I Na and Poly II Na) and N. brasiliensis (Poly I Nb and Poly II Nb). These polysaccharides were isolated from cell extracts and purified by methanol precipitation, chloroform extraction of extraneous material, and deproteinization with trichloroacetic acid. The crucial step used for separation of Poly I and Poly II from both nocardias was differential solubility. From dried preparations containing both polysaccharides, Poly I was solubilized at pH 10, whereas Poly II remained insoluble and was subsequently solubilized at pH 5. Poly I Na and Poly I Nb are apparently the same. Arabinose and galactose were the monosaccharide constituents of these polysaccharides, and their molar ratios were similar. Furthermore, Poly I Na and Poly I Nb cross-reacted in agar diffusion precipitin tests with rabbit antisera prepared against either N. asteroides or N. brasiliensis. Either polysaccharide absorbed serum antibodies against the other. These polysaccharides can be regarded as groupspecific. Poly II Na and Poly II Nb are different and species-specific. They are composed of arabinose, galactose, and mannose but exhibit different molar ratios of these sugars according to species. They reacted only with homologous antisera.

Allergy and Immunology↗
PubMed1963

IMMUNOCHEMICAL ANALYSIS OF HUMAN ORAL STRAINS OF FUSOBACTERIUM AND LEPTOTRICHIA.

de Araujo, Wilson C. (National Institute of Dental Research, Bethesda, Md.), Eileen Varah, and Stephan E. Mergenhagen. Immunochemical analysis of human oral strains of Fusobacterium and Leptotrichia. J. Bacteriol. 86:837-844. 1963.-Lipopolysaccharides, isolated by phenol-water extraction of 27 strains of oral gram-negative bacteria conforming either to Fusobacterium polymorphum or Leptotrichia buccalis, were shown to be endotoxic by their ability to alter dermal reactivity to epinephrine and to be serologically specific by hemagglutination and hemagglutination-inhibition tests. Numerous serotypes of these organisms were detected by hemagglutination tests with purified lipopolysaccharides. A F. polymorphum lipopolysaccharide produced two visible precipitin bands in agar gel with antiserum prepared against the homologous organism. Each of the immunologically distinct components of the endotoxin, isolated by differential centrifugation, altered dermal reactivity to epinephrine and acted as a hapten in hemagglutination tests. Crude antigens from F. polymorphum strains, released in supernatant fluids of heat-killed bacterial suspensions, showed broad serological cross-reactivity with antiserum prepared against homologous and heterologous strains of F. polymorphum but not with antiserum prepared against L. buccalis strains. Broad serological cross-reactivity of these crude F. polymorphum antigens could be eliminated by prior treatment with phenol or trypsin, indicating that the common antigen or antigens in these organisms are protein. Double-diffusion tests in agar identified and differentiated type-specific lipopolysaccharide from other antigens extracted by heat from these organisms. Similarly prepared crude antigens from L. buccalis had broad serological activity with antiserum prepared against various strains of L. buccalis but not with F. polymorphum. In contrast to the crude antigens from F. polymorphum, this serological cross-reactivity could not be eliminated by treatment with phenol or trypsin.

Antigens↗
PubMed1963

IMMUNOLOGICAL AND TOXIC DIFFERENCES BETWEEN MOUSE-VIRULENT AND MOUSE-AVIRULENT CANDIDA ALBICANS.

Isenberg, Henry D. (Long Island Jewish Hospital, New Hyde Park, N.Y.), Jona Allerhand, James I. Berkman, and Dorothy Goldberg. Immunological and toxic differences between mouse-virulent and mouse-avirulent Candida albicans. J. Bacteriol. 86:1010-1018. 1963.-The differences between mouse-avirulent and -virulent strains of Candida albicans reside at least in part in cell surface materials which can be extracted with solvents such as ethanolethyl ether and phenol. These extracts are complex haptens which behave like endotoxins in mice and rabbits. Antibodies produced against intact and extracted cells show some strain specificity in agglutination and precipitin reactions, but underline primarily the differences between the virulent and avirulent variants. The chemical constitution of the extracted complex haptens suggests that the toxic or virulent principles are polysaccharide in nature and that the avirulent strain substitutes fats and lipids for some polysaccharides on their cell surface.

Animals↗
PubMed1963

SEROLOGICAL GROUPING OF THE PATHOGENIC CLOSTRIDIA.

Ellner, Paul D. (University of Vermont, Burlington), and Stanley S. Green. Serological grouping of the pathogenic clostridia. J. Bacteriol. 86:1098-1100. 1963.-By use of the soluble antigens of ten species of pathogenic clostridia and specific globulins, it has been possible to divide these organisms into a number of groups based upon the presence or absence of precipitin lines in agar gel. A scheme for such a grouping is presented, and the utility of this method is discussed.

Agar↗
PubMed1964

DIFFERENTIATION BY IMMUNODIFFUSION AND BY QUANTITATIVE IMMUNOFLUORESCENCE BETWEEN 5-FLUOROURACIL-TREATED AND NORMAL CELLS FROM A TOXINOGENIC STAPHYLOCOCCUS AUREUS STRAIN.

De Repentigny, J. (University of Montreal, Montreal, Quebec, Canada), S. Sonea, and A. Frappier. Differentiation by immunodiffusion and by quantitative immunofluorescence between 5-fluorouracil-treated and normal cells from a toxinogenic Staphylococcus aureus strain. J. Bacteriol. 88:444-448. 1964.-Immunodiffusion and quantitative immunofluorescence can both detect antigenic changes produced by 5-fluorouracil (FU) in Staphylococcus aureus Wood 46 strain. When FU is added to the cultures in their logarithmic phase of growth, a number of bacterial antigens are no longer detectable by immuno-diffusion and the intensity of the total immuno-fluorescence of bacteria is diminished; thus, these antigens are either profoundly modified or no longer synthesized. Uracil and, less effectively, thymine can reverse the FU inhibitory effect on the synthesis of antigens, and the number of precipitin lines remains closer to controls. The immunochemical approach provides a new way of obtaining information on the action of this pyrimidine analogue on metabolic processes in pathogenic bacteria. Microscopic quantitative immunofluorescence seems to be adaptable to give indirect information on changes in the metabolism or synthesis or antigens of a single bacterial cell.

Antigens↗
PubMed1964

ELECTROPHORETIC SEPARATION OF CONSTITUENTS OF PARTIALLY PURIFIED M PROTEIN OF STREPTOCOCCUS PYOGENES.

Pierce, William A., Jr. (Tulane University, New Orleans, La.). Electrophoretic separation of constituents of partially purified M protein of Streptococcus pyogenes. J. Bacteriol. 88:912-921. 1964.-Partially purified M protein of a group A, type 12 strain of Streptococcus pyogenes was studied by use of chemical, electrophoretic, and immunological techniques. It was demonstrated in immunodiffusion tests that the antigen contains multiple precipitating components. The type-specific antigen was identified, and evidence was presented that, in some instances at least, the cross-reactions observed between this type 12 M protein and heterologous antisera in immunodiffusion tests involve contaminating antigens rather than the component which precipitates with adsorbed homologous-typing antiserum. In passive hemagglutination tests where M protein was adsorbed to tanned sheep erythrocytes, it was found that antisera suitably adsorbed to show good specificity in capillary precipitin tests nevertheless still contain cross-reactive antibodies which are detectable by this more sensitive technique. Electrophoresis on starch paste separates some of the components of partially purified M protein, so that a fraction can be obtained which has fewer precipitating antigens, as determined in immunodiffusion tests, and which is less cross-reactive in passive hemagglutination tests with heterologous unadsorbed antistreptococcal antisera.

Animals↗
PubMed1964

USE OF A FLUORESCEIN-LABELED SONICALLY DISRUPTED BACTERIAL ANTIGEN TO DEMONSTRATE ANTIBODY-PRODUCING CELLS.

Eveland, Warren C. (University of Michigan, Ann Arbor). Use of a fluorescein-labeled sonically disrupted bacterial antigen to demonstrate antibody-producing cells. J. Bacteriol. 88:1476-1481. 1964.-Cells obtained by primary tissue culture of the spleens of chickens immunized with sonically disrupted Escherichia coli O111 organisms were stained with a fluorescein-labeled homologous antigen by use of direct immunofluorescent methods. Brilliant staining of the cytoplasm in cells from immunized birds appeared to be diffuse in certain cells and rather globular in others. In contrast, cells from nonimmunized birds showed no staining at all. The cells involved in the specific reaction appeared to be those of the lymphocyte-monocyte-plasma cell types, as shown when stained by the May-Grunwald-Giemsa method. Preparations stained by the methyl green-pyronin technique revealed an increase in the pyrinophilic cells in the preparations from the immunized birds, thus demonstrating increased amounts of ribonucleic acid in these cells, which in turn is consistent with the presence of antibody globulin. Specificity of the reaction was confirmed also by (i) staining antibody-coated E. coli O111 organisms with the conjugate, (ii) precipitin reaction with specific antibody, and (iii) specific agglutination with circulating antibody from the immunized birds.

Agglutination↗
PubMed1964

ORIGIN AND PROPERTIES OF NATURALLY OCCURRING HAPTEN FROM ESCHERICHIA COLI.

Anacker, R. L. (National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratory, Hamilton, Mont.), R. A. Finkelstein, W. T. Haskins, M. Landy, K. C. Milner, E. Ribi, and P. W. Stashak. Origin and properties of naturally occurring hapten from Escherichia coli. J. Bacteriol. 88:1705-1720. 1964.-Haptens found in preparations of endotoxin and in fractions of disrupted cells, particularly one termed "native hapten," which appeared to be associated with the protoplasm of cells rather than with cell walls, have been further investigated with a view to establishing their origin and composition as well as their host-reactive properties. For this purpose, cells from a smooth strain of Escherichia coli O111:B4 were either extracted directly or disrupted and separated into cell-wall and protoplasmic fractions. Haptens were obtained by gel filtration of endotoxins, by trichloroacetic acid extraction of protoplasm, and by a mild acid hydrolysis of endotoxin. Several lines of evidence indicated that native hapten originated in the protoplasm rather than by autolysis or degradation of cell-wall endotoxin during procedures employed in disruption. In gel diffusion and quantitative precipitin tests, no hapten was identical with endotoxin, but native hapten was serologically the most complex of the haptens and precipitated the most antibody. Native and acid haptens, on a weight basis, fixed about 1% of the quantity of complement fixed by homologous endotoxin. Haptens did not stimulate the production of antibodies in mice or rabbits and did not elicit endotoxic host reactions. Chemically, native hapten differed from endotoxin and from acid hapten in that it lacked phosphorus, heptose, long-chain fatty acids, and 2-keto-3-deoxyoctonate. These substances did not appear to be determinants of antigenic specificity, but they may provide necessary bonds for assembling hapten-like units into fully antigenic and toxic macromolecules.

Animals↗
PubMed1964

DIFFERENTIATION OF EXOTOXIN AND OTHER BIOLOGICALLY ACTIVE SUBSTANCES IN PSEUDOMONAS PSEUDOMALLEI FILTRATES.

Heckly, Robert J. (University of California, Berkeley). Differentiation of exotoxin and other biologically active substances in Pseudomonas pseudomallei filtrates. J. Bacteriol. 88:1730-1736. 1964.-Denaturing agents such as phenol, formaldehyde, and urea reduced lethal toxicity and proteolytic activity of partially purified preparations from Pseudomonas pseudomallei at about the same rate. Neither toxin nor enzyme was stable at pH 11, when the solution was adjusted with sodium hydroxide, but there was a slight difference in their rates of inactivation. However, under certain conditions, ammonium hydroxide destroyed most of the enzymatic activity with only a slight effect on lethality. Conversely, toxin was less stable in acid solutions than was the enzyme. Thus, treatment with ammonium hydroxide or acetic acid yielded preparations with either a low or a high enzyme-to-toxin ratio, indicating that lethality was not dependent on enzyme activity. Although proteolysis of any one of the essential factors in the blood coagulation system can inhibit clotting of blood, the potent anticoagulant activity of culture filtrates was not associated with its proteolytic activity, but was directly correlated with lethal toxicity. It is of considerable interest that the necrotoxicity was, however, associated with enzymatic activity and not with lethality. Serological reactivity of the enzyme, as well as its proteolytic activity, was altered by ammonium hydroxide. Similarly, antigenicity and toxicity of the lethal toxin were reduced by acidification. Each acid- or alkali-treated preparation produced a single precipitin line in double diffusion in agar when reacted with antisera produced by injection of crude filtrate. Partially purified preparations, having both lethal and enzymatic activity, produced two lines, one identifiable with the enzyme preparation, and one with the toxin. Furthermore, specific precipitation with the respective antisera removed either enzyme or toxin from crude preparations. Therefore, the lethal exotoxin and proteolytic enzyme are separable entities.

Animals↗
PubMed1965

MULTIPLE CELLULASE SYSTEM FROM STREPTOMYCES ANTIBIOTICUS.

Enger, M. D. (North Dakota State University, Fargo), and B. P. Sleeper. Multiple cellulase system from Streptomyces antibioticus. J. Bacteriol. 89:23-27. 1965.-Starch-block zone electrophoresis was used to isolate five electrophoretically distinct, active cellulolytic components (I to V) from the crude extracellular cellulase system of Streptomyces antibioticus (strain C2A). Agar diffusion precipitin analyses demonstrated the immunological identity of components I, II, and III, and the nonidentity of IV and V with each other and with I to III. Kinetic studies of the purified enzymes showed a sharp decrease in the viscosity of the substrate, carboxymethylcellulose, with only a small increase in reducing sugars. These results indicated that all five enzymes are endocellulases.

Carbohydrates↗
PubMed1965

ISOLATION OF L FORMS FROM GROUP A STREPTOCOCCI EXPOSED TO BACITRACIN.

Rotta, Jiri (Washington University School of Medicine, St. Louis, Mo.), Walter W. Karakawa, and Richard M. Krause. Isolation of L forms from group A streptococci exposed to bacitracin. J. Bacteriol. 89:1581-1585. 1965.-L forms were obtained from group A streptococci by exposure to bacitracin on gradient plates, although novobiocin was ineffective in this respect. Subcultures of these L forms had morphological and bacteriological properties similar to those obtained with penicillin. M protein was detected in L-form colony smears by immunofluorescent staining with type-specific conjugate. The L forms were not stained with group-specific conjugate. Parallel precipitin tests performed with extracts from a heavy growth of L forms on agar confirmed these findings. Thus, the L forms obtained with bacitracin continue to produce M protein but are devoid of the group-specific carbohydrate which is a major component of cell-wall structure.

Bacitracin↗
PubMed1973

Relevance of antigenicity of Candida albicans growth phases to diagnosis of systemic candidiasis.

The antigenicity of the two growth phases of Candida albicans has been compared by using crossed immunoelectrophoresis and double-diffusion techniques. Qualitative and quantitative differences in antigenic composition between the phases have been revealed and moreover a specific mycelial antigenic component demonstrated.It is postulated that the use of specific mycelial antigens for routine diagnostic precipitin testing in patients with suspected systemic candidiasis would give more reliable results than at present obtained with yeast cell antigens.

Antigens, Fungal↗
PubMed1974

Qualitative and quantitative aspects of the human antibody response to streptococcal group A carbohydrate.

The lack of impressive quantitative differences in antibody to various streptococcal extracellular and cellular antigens among patients with acute rheumatic fever, acute glomerulonephritis, and following uncomplicated streptococcal infection has prompted investigation of qualitative aspects of the antibody response among these patients. By using a radiolabeled antigenically univalent hapten derived from streptococcal A carbohydrate, affinity of serum antibody to A-carbohydrate (A-antibody) was studied by an ammonium sulfate precipitation technique. The data obtained demonstrate average association constants (K0S) of acute rheumatic fever patient sera to be significantly lower than those of acute glomerulonephritis or streptococcal infection patients (P<0.02 and P<0.001, respectively). Further analysis of the data from hapten binding studies documents the fact that the radioimmune precipitin assay for the determination of A-antibody level is little influenced by K0 but directly correlates with the concentration of antibody binding sites. These data suggest that qualitative differences in A-antibody are present between rheumatic and non-rheumatic individuals. It is unclear whether the finding of low-affinity A-antibody among acute rheumatic fever patients reflects a generalized phenomenon or one restricted to the A-antibody-A-carbohydrate system.

Adolescent↗
PubMedDate not supplied

Human sera with precipitating antibodies to human soluble immune complexes. A brief communication.

INTRODUCTION: Previous numerous papers by the senior author dealt with the human serum factor referred to as anti-antibody which is specifically directed against IgG antibodies that underwent molecular transformation in the course of the reactions with their corresponding antigens. The reactions of this serum factor could be conveniently detected by means of agglutination of Rh-positive erythrocytes sensitized by anti Rh antibodies. No precipitation tests could be developed. MATERIAL AND METHODS: Most studies were conducted by means of double diffusion in gel precipitation. RESULTS: A rheumatoid arthritis serum, G, was noted that produced a strong reaction of double diffusion in gel precipitation with serum samples of a renal graft recipient, T. Further screening detected one more rheumatoid arthritis serum reacting with T; of 28 sera from renal graft recipients, 6 reacted in a similar way to T, but the reactions were considerably weaker and poorly reproducible. Evidence was presented that the precipitin in the two rheumatoid arthritis sera under study had properties of previously described anti-antibody. CONCLUSIONS: Sera with precipitating anti-antibodies may serve as exquisite reagents for detection of soluble immune complexes in human sera.

Antibodies, Anti-Idiotypic↗
PubMed1989

Further characterization and immunochemical studies on the carbohydrate specificity of jackfruit (Artocarpus integrifolia) lectin.

The lectin from jackfruit (Artocarpus integrifolia) seeds has been purified by Rivanol (6,9-diamino-2-ethoxyacridine lactate) treatment. The specific activity, molecular weights of parent lectin and its subunit, its glycoprotein nature, and hemagglutination-inhibition assays suggest that this preparation is identical to that obtained by affinity chromatography on melibiose-agarose adsorbent (Ahmed, H., and Chatterjee, B. P. (1986) in Lectins, Biology, Biochemistry, Clinical Biochemistry (Bøg-Hansen, T. C., and van Driessche, E., eds) Vol. 5, pp. 125-133, Walter de Gruyter, New York). The lectin strongly agglutinates human and several animal erythrocytes. The lectin contains five isolectins of pI values 7.1, 6.85, 5.5, 5.3, and 5.1. It is thermally stable and loses its activity above 75 degrees C. The hemagglutinating activity remains unchanged in the presence of bivalent cations viz., Ca2+, Mg2+, Mn2+, etc. It is a metalloprotein. The lectin retains its activity by dialysis with acetic acid followed by EDTA. It agglutinates Ehrlich ascites cells. Equilibrium dialysis of lectin with melibiose and quenching of fluorescence of 4-methylumbelliferyl-alpha-D-galactopyranoside by the lectin show that homotetrameric jackfruit lectin has two sugar-binding sites. The lectin precipitates well several galactomannans and glycoproteins having terminal D-Gal-alpha-(1----6)- or D-Gal-beta-(1----3)-D-GalNAc residues. It hardly or does not precipitate polysaccharides having terminal D-Gal-alpha-(1----3) residues. Quantitative precipitin-inhibition studies using various haptens suggest that the -OCH2- group at C-1 and -OH groups at C-4 and partially at C-6 in the alpha-glycoside of D-galactose configuration are important for lectin-sugar interaction.

Animals↗
PubMed1983

Fc-mediated immune precipitation. IV. Antigen dependency and specificity.

The antigen dependency of Fc-mediated immune precipitation was investigated by comparing the immune precipitation of three different protein antigens (bovine serum albumin, BSA, human plasma transferrin, HPT, and human fibrinogen, HFg) using specific intact rabbit IgG antibodies and isomolar solutions of the corresponding F(ab')2 fragments. We found that this precipitin mechanism is highly antigen-dependent both quantitatively and qualitatively. Sucrose density gradient ultracentrifugation was used for the identification of Fc-precipitating immune complexes, and we demonstrated that different types of complexes take part in Fc-mediated immune precipitation in the different antigen-antibody systems. Thus, only small complexes are involved in the HFg system, whereas small as well as large complexes precipitate by this mechanism in the BSA and the HPT systems. The specificity of Fc-mediated immune precipitation was studied by mixing human serum albumin (HSA)-anti-HSA IgG complexes with either HPT-anti-HPT IgG or HFg-anti-HFg IgG complexes. These investigations show that Fc-mediated immune precipitation is a specific process due to the preferential binding of homologous complexes.

Animals↗