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PubMed1971

Pathogenicity and Antigenicity of Clones from Strains of Marek's Disease Virus and the Herpesvirus of Turkeys.

Virus was extracted by filtration from chicken embryo fibroblast cultures infected with the JM, high passage JM(JMHP), GA, and RPL39 strains of Marek's disease virus (MDV) and from the herpesvirus of turkeys (HVT) and purified by cloning. The plaques produced by clones of HVT, JMHP, and other MDV strains differed in morphology from one another. Clones of MDV varied greatly in pathogenicity for chickens, but JMHP and HVT were nonpathogenic. Two pathogenic clones of JM virus and a clone of JMHP virus lacked the A precipitin antigen present in all other clones tested. All clones had at least one B antigen in common. HVT and MDV clones with and without the A precipitin antigen could be distinguished from each other by the indirect fluorescent antibody test. Changes in virus-host cell relationships, loss of pathogenicity, and loss of the A antigens were independent events.

Journal Article↗
PubMed1971

Chemical structure and immunological specificity of the streptococcal group e cell wall polysaccharide antigen.

The streptococcal group E cell wall polysaccharide antigen was extracted from strain K129 cells with hot trichloroacetic acid and purified. It contained rhamnose and glucose in a 2:1 molar ratio, 2% protein, 1% phosphorus, and was free of muramic acid and glycerol. No type polysaccharide antigen was present. The reaction of specific group E rabbit antiserum with the polysaccharide was effectively inhibited by d-glucose and beta-glucosides such as 1-methyl-beta-d-glucose, cellobiose, and gentiobiose. The 1-methyl-alpha-d-glucose was one-half as effective as the beta isomer. l-Rhamnose and N-acetyl-d-glucosamine were ineffective. Partial acid hydrolysis of the antigen followed by chromatographic separation of the oligosaccharides resulted in the isolation and analysis of five fractions. These fractions were di-, tri-, and tetrasaccharides. A study of these fractions by chemical analysis, reduction with borohydride, inhibition of the antigen-antibody reaction, release of glucose by beta-glucosidase, and other evidence indicate that beta-d-glucose is the immunodominant sugar in the antigen. A glucose-rhamnose trisaccharide (1:2 molar ratio) was the most effective inhibitor of the precipitin reaction; the glucose was readily released by beta-glucosidase, and one-half of the rhamnose was reduced with borohydride. This trisaccharide is considered to be a repeating unit in the native polysaccharide and probably has the following structure: O-beta-d-glucosyl-(1-2)-O-alpha-l-rhamnosyl- (1-4)-l-rhamnose. A glucose-rhamnose disaccharide in which the hexose and pentose are linked as in the trisaccharide was an effective inhibitor of the precipitin reaction. Strain K129 cells do not appear to contain a type polysaccharide antigen.

Journal Article↗
PubMed1982

Common antigens of Treponema denticola: chemical, physical, and serological characterization.

A sodium deoxycholate-ethanol extractable antigen (DES-Ag) was obtained from four serotypes of Treponema denticola and characterized by chemical, physical, and serological procedures. The cross-reactivity of these antigens was demonstrated by indirect microhemagglutination, immunodiffusion, and immunoelectrophoresis with hyperimmune rabbit antiserum against each of the T. denticola serotypes. Antiserum against two nonoral treponemes, T. phagedenis biotype Reieter and T. pallidum Nichols strain, did not cross-react with the DES-Ag of T. denticola. Chemical analysis of the DES-Ag indicated that proteins (84%) and hexoses (12%) accounted for 96% of the total dry weight of the antigen. Trace amounts of N-acetylglucosamine (0.6%) were also detected. Fatty acids, including palmitic, oleic, and stearic, were identified by gas-liquid chromatography. Polyacrylamide gel electrophoresis of the DES-Ag of each serotype revealed the presence of two bands. The molecular weights of the bands were estimated to be 58,000 and 31,000 by comparing the electrophoretic mobility of the DES-Ag to that of five protein standards of known molecular weights. Although only a single precipitin line was observed by immunodiffusion when each antigen was reacted against its homologous antiserum, two precipitin lines were evident by immunoelectrophoresis. Antiserum against the DES-Ag of T. denticola was shown to agglutinate whole cells of the homologous serotype. Adsorption of this anti-DES-Ag serum with whole cells of T. denticola resulted in the elimination of precipitating antibodies to the DES-Ag by immunodiffusion. It is concluded that the DES-Ag is a component of the outer sheath of T. denticola.

Animals↗
PubMed1982

Purification of a protective antigen from a saline extract of Pasteurella multocida.

It has been shown previously that soluble material extracted from Pasteurella multocida P-1059 by a 2.5% NaCl solution protects turkeys from generalized septicemia at a subsequent challenge exposure to the organism. In the present study, a protective antigen was purified from the crude soluble material by chromatographic methods. Four protein peaks were obtained by gel filtration with Sephadex G-200. The protective antigen was detected only in the first peak fraction, which contained a substantial amount of carbohydrate. The peak 1 fraction was adsorbed onto DEAE-cellulose and eluted by a linear gradient of NaCl. Fractions corresponding to a single protein peak were pooled and passed through an immunoadsorbent column to remove any possible serum component originating from the growth medium. The purified antigen had a carbohydrate/protein ratio of 1.5 and formed a single precipitin line with rabbit antiserum against the crude material in gel diffusion and immunoelectrophoresis analyses. The antigen produced antibodies in rabbits and turkeys which formed a single precipitin line against the crude material. Upon sodium dodecyl sulfate-polyacryl-amide gel electrophoresis, the purified antigen showed three protein bands, corresponding to molecular weights of 44,000, 31,000, and 25,000, and one carbohydrate band. The carbohydrate band did not correspond to any of the three protein bands. Upon isoelectric focusing gel analysis, the purified antigen showed two bands (pI = 3.5 to 4.0 and 4.5 to 5.5), but the two bands were antigenically identical by isoelectric focusing crossed immunoelectrophoresis. The 50% protective dose of the purified antigen was between 10 and 50 mug of protein in trials where two doses were given at 14-day intervals to 10- to 20-week-old turkeys.

Animals↗
PubMed1983

Purification and immunochemical characterization of Streptococcus sanguis serotype I carbohydrate antigen.

The serotype-specific antigen of Streptococcus sanguis ST3 (serotype I, biotype A) was extracted, chromatographically purified, and characterized by immunological and chemical methods. The antigen was extracted from purified cell walls with hot trichloroacetic acid, followed by ion-exchange chromatography on a DEAE-Sephadex A-25 column and gel filtration through a Sephadex G-100 column. A peak fraction was obtained that gave a single precipitin band when reacted with anti-type I serum. The type I antigen was a polysaccharide composed of glucose, rhamnose, and N-acetylglucosamine in a molar ratio of 1.4:2.5:1.0. Quantitative precipitin inhibition tests with various haptenic sugars indicated that an alpha-glucosidic linkage is the immunodeterminant of the type I antigen.

Chromatography, Gel↗
PubMed1983

Purification and immunochemical characterization of Streptococcus sanguis ATCC 10557 serotype II carbohydrate antigen.

Cell wall carbohydrate antigen of Streptococcus sanguis ATCC 10557 (serotype II/biotype B) was extracted from purified cell walls by treatment with 5% trichloroacetic acid at 4 degrees C for 8 h. The extract was purified by chromatography on DEAE-Sephadex A-25 and Sephadex G-100 columns. The purified carbohydrate antigen produced a single precipitin band against anti-type II serum, which fused with the band produced by the autoclaved extract or the phenol-water extract of the S. sanguis cells. The type II antigen was a polysaccharide composed of glucose, galactose, rhamnose, and N-acetylgalactosamine in a molar ratio of approximately 3:6:3:2. Quantitative precipitin inhibition tests with various haptenic sugars indicated that N-acetylgalactosamine was a major determinant of the type II antigen.

Amino Acids↗
PubMed1985

Antigenic heterogeneity of an alkali-soluble, water-soluble cell wall extract of Coccidioides immitis.

The antigenic composition of an alkali-soluble, water-soluble cell wall extract of Coccidioides immitis, designated C-ASWS, was assessed by two-dimensional immunoelectrophoresis against goat antisera to C-ASWS and coccidioidin. The results established that C-ASWS from mycelia or spherule cell walls is heterogeneous in composition, containing two distinct antigenic components. One is present as a polymer that is antigenically identical to a polymeric antigen in coccidioidin, designated antigen 2. The other component detected in C-ASWS presented an unusual precipitin pattern in that a cathodal leg was demonstrable in the absence of an anodal leg. This incomplete precipitinogen was also detected in coccidioidin. In addition to the finding that C-ASWS is antigenically heterogeneous, the results provide evidence that the conformational and/or configurational structure of the C-ASWS antigen 2 (or antigen 2-like polymer) is altered during physicochemical extraction. This conclusion is based upon the finding that the immunoelectrophoretic profile of the C-ASWS polymer differs from that of coccidioidin antigen 2. The C-ASWS polymer is characterized by having a small cathodal precipitin peak connected to a large anodal peak, whereas coccidioidin antigen 2 is characterized by a predominant cathodal peak.

Antigens, Fungal↗
PubMed1986

Comparison of immunoblot analyses of spherule-endospore-phase extracellular protein and mycelial-phase antigen of Coccidioides immitis.

The extracellular proteins produced by Coccidioides immitis during growth of the spherule-endospore-phase and mycelial-phase antigen (coccidioidin) were studied by polyacrylamide gel electrophoresis followed by immunoblot analysis to detect specific serologic function. Filtrates obtained from 28- and 120-h growth of the spherule-endospore phase were compared with each other and with coccidioidin by using negative, immunoglobulin M (IgM) precipitin-positive, or complement fixation-positive pooled and single human sera followed by peroxidase-labeled anti-human IgA, IgE, IgG, or IgM (heavy chain specific) or peroxidase-labeled concanavalin A to detect the reaction. A total of 35 bands was seen in the stained gels. Different patterns were noted among the two spherule-endospore preparations and unheated and heated coccidioidin. At least 15 electrophoretically separate antigens were detected with positive serum ranging in approximate molecular weight (Mr) from 100,000 to 18,000. Most were clustered between 45 and 60 kilodaltons (kDa). Common bands were noted at 48 and 18 kDa. At least one band at 48 kDa was strongly reactive with complement fixation-positive serum demonstrated by reaction with anti-IgG and anti-IgE. In contrast, doublet bands in the 50- to 65-kDa area were highly reactive with IgM precipitin-positive serum detected by anti-IgM. IgM antibodies present in both positive sera reacted with a band at 46 kDa which was not reactive with IgG. Heating the antigens altered the reactivity of many of the antigens, including the 48-kDa band, but not the 46-kDa band.

Antigens, Fungal↗
PubMed1989

Effect of chemical modification of histidine and tyrosine residues in toxic shock syndrome toxin 1 on the serologic and mitogenic activities of the toxin.

Modification of three or four of the five histidine residues in the toxic shock syndrome toxin 1 (TSST-1) with diethylpyrocarbonate did not inhibit the precipitin reaction of the modified TSST-1 with polyvalent antisera to the toxin. Monoclonal antibody 7T did not react with the modified TSST-1, but monoclonal antibody 8T did react with the toxin. Up to 50% of the mitogenic reaction of TSST-1 was inhibited by the histidine modification. Modification of one or two of the nine tyrosine residues in TSST-1 did not inhibit the precipitin reaction with polyclonal antisera to the toxin but did inhibit 85% of the mitogenic reaction.

Animals↗
PubMed1995

Characterization of a human monoclonal immunoglobulin M (IgM) antibody (IgMBEN) specific for Vi capsular polysaccharide of Salmonella typhi.

A search for human monoclonal antibodies to protective antigens of bacteria revealed an immunoglobulin M lambda chain [IgM(lambda); designated IgMBEN] reactive with the Vi capsular polysaccharide of Salmonella typhi. Vi, a linear homopolymer of alpha(1-->4)GalApNAc that is O acetylated at C-3, is a licensed vaccine for typhoid fever. Immunologic properties of IgMBEN were compared to those of burro globulin prepared by intravenous injections of S. typhi (B339-340). IgMBEN and B339-340 yielded identical precipitin lines with Vi by double immunodiffusion. IgMBEN and B339-340 produced similar precipitation results with Vi and its derivatives prepared by de-O-acetylation, carboxyl reduction, and removal or replacement of the N-acetyl at C-2 with O-acetyl. B339-340 yielded maximal precipitation with Vi (0.41 mg of antibody per ml with 1.4 micrograms of Vi); next was carboxyl-reduced, O-acetylated Vi, which precipitated 0.325 mg of antibody per ml with 2.5 micrograms of Vi. IgMBEN yielded maximal precipitation with de-O-acetylated, carboxyl-reduced Vi (approximately 11.0 mg of antibody per ml with approximately 1.3 micrograms of antigen); next were de-O-acetylated Vi (9.89 mg/ml) and Vi (9.19 mg/ml). The precipitin curves and equivalence points of these three antigens were similar. Pneumococcus type 1, which contains GalApNAc, did not precipitate with Vi or its derivatives. These slight differences in specificity between IgMBEN and B339-340 were related to our proposed structure of Vi. We plan to use IgMBEN as a reference for measurement of vaccine-induced Vi antibodies.

Antibodies, Monoclonal↗
PubMed1974

BCG antibody profiles in tuberculoid and lepromatous leprosy.

In sera from 12 patients with polar tuberculoid leprosy, 12 with subpolar tuberculoid leprosy, and 16 with lepromatous leprosy were demonstrated a total number of 125 anti-BCG precipitins by means of crossed immunoelectrophoresis with intermediate gel. Up to 14 different precipitins were found in individual sera, and the complexity in antibody response was higher than previously realized. The specificity of 69% of the antibodies was defined, and these antibodies were titrated in three arbitrary titer units. A highly significant difference (P < 0.002) was found in antibody response between the tuberculoid and the lepromatous group. Due to simplicity, sensitivity, and high resolution, the method used is a promising tool for providing exact data to be used as guidelines for purification of important individual mycobacterial antigens. The need for reference antisera is emphasized.

Animals↗
PubMed1971

"In vivo" detection of L-arabinose-binding protein, CRM-negative mutants.

An "in vivo" assay for the detection of mutants negative to CRM (cross-reacting material) is described. l-Arabinose-negative mutants of Escherichia coli B/r were grown on Casamino Acids-l-arabinose plates to which a 3-ml agar layer, containing antiserum to the l-arabinose-binding protein (ABP), had been applied. After incubation and partial lysis of the clones "in situ," the plates were refrigerated for 36 hr, rinsed of colonial growth with water, and observed for the presence or absence of an immune precipitation. ABP-minus and l-arabinose regulator (araC)-minus mutants do not produce a precipitin reaction. l-Arabinose isomeraseless (EC 5.3.1.4; araA), kinaseless (EC 2.7.1.16; araB), and epimeraseless (EC 5.1.3.a; araD) mutants produce precipitin reactions. Mutants of E. coli B/r generated by treatment of the wild type with ethyl methane sulfonate or ultraviolet irradiation were isolated, tested for l-arabinose uptake, and screened for the presence or absence of ABP by the described assay. The applications of such an assay are discussed.

Agar↗
PubMed1963

Antigenicity of some Brucella melitensis cell fractions.

Glenchur, Harry (Minneapolis Veterans Administration Hospital, and University of Minnesota School of Medicine, Minneapolis), Ulysses S. Seal, Horace H. Zinneman, and Wendell H. Hall. Antigenicity of some Brucella melitensis cell fractions. J. Bacteriol. 85:363-368. 1963.-The components of a Brucella melitensis strain were obtained by differential centrifugation and diethylaminoethyl-cellulose ion-exchange chromatography. Rabbit antisera to these Brucella fractions were tested for agglutinins, precipitins, and blocking phenomena. Dermal hypersensitivity was also determined in rabbits. Insoluble (cell-wall) fractions provoked agglutinins, blocking antibodies and skin sensitivity, and precipitins for soluble antigens. Most soluble antigen fractions were capable of producing all the secondary immunological phenomena.

Antigens↗
PubMed1965

Control of Tissue Reactions in Monkeys Vaccinated with Viable Coccidioides immitis by Prevaccination with Killed Coccidioides immitis.

Converse, J. L. (U.S. Army Biological Laboratories, Fort Detrick, Frederick, Md.), G. A. Deauville, E. M. Snyder, J. G. Ray, and M. E. Seaquist. Control of tissue reactions in monkeys vaccinated with viable Coccidioides immitis by prevaccination with killed Coccidioides immities. J. Bacteriol. 90:783-788. 1965.-Control of undesirable tissue reactions resulting from the subcutaneous injection of 150 viable arthrospores of Coccidioides immitis (strain D-76) was obtained by four injections of formalin-killed arthrospores 14, 12, 8, and 4 weeks (total dose, 36 mg) before injection of the viable arthrospores. Only 6 and 12% of these vaccinated animals exhibited ulceration and lymphadenopathy, respectively, as compared with 100 and 83% of the animals receiving only the viable vaccine. Agar-gel immunodiffusion precipitin titers of approximately 1:64 were evident 3 months after vaccination in animals receiving both vaccines, as compared with 1:128 in those injected with the viable vaccine alone. The above data indicated that somatic reactions to injection of a viable vaccine could be eliminated by preinjection of a killed vaccine. However, 6 months after vaccination, respiratory challenge (7,500 strain Cash arthrospores) indicated that this treatment also impaired the protective effect of the viable vaccine. All animals receiving both vaccines developed mild pulmonary coccidioidomycosis, whereas only 50% of the animals receiving only the viable vaccine were infected. In addition, the group receiving both vaccines demonstrated a more rapid and higher postchallenge precipitin titer. All vaccinated animals (those receiving the killed, the viable, or a combination of the two vaccines) survived for 4 months after challenge, as compared with 88% mortality (50% within 14 days) in the nonvaccinated controls.

Journal Article↗
PubMed1966

Isolation and characterization of two antigens of Corynebacterium hofmannii.

Banach, T. M. (University of Manitoba, Winnipeg, Canada), and R. Z. Hawirko. Isolation and characterization of two antigens of Corynebacterium hofmannii. J. Bacteriol. 92:1304-1310. 1966.-A serologically active substance, extracted from sonically treated cells of Corynebacterium hofmannii with hot HCl, produced two precipitin lines by immunodiffusion tests with a hyperimmune homologous serum. Extracts of other species failed to precipitate with the hofmannii antiserum. The active fraction was eluted from a diethylaminoethyl cellulose column in the third adsorption peak at a linear concentration of 0.5 m KCl, and produced two precipitin lines which corresponded in identity to those formed by the acid extract. Separation of the antigens was achieved by rechromatography on a Sephadex G-200 column; the major antigen was designated A; the minor, B. The homogeneity and purity of each antigen was established by immunoelectrophoresis and, in addition, that of antigen A by disc electrophoresis. Biochemical analyses showed that both antigens were composed of a major protein component with polysaccharide and nucleic acid present in an approximate ratio of 17:3:1, respectively. Glutamic acid, aspartic acid, alanine, glycine, valine, and leucine were the main amino acids present. Antigen A contained 17% less protein and 3.5% less carbohydrate than antigen B. The principal sugars of antigen A were identified as arabinose and glucose. The molecular weight, estimated by gradient centrifugation, was 16,500 for antigen A and 21,000 for antigen B.

Amino Acids↗
PubMed1967

Serological comparison of the three morphological phases of Coccidioides immitis by the agar gel diffusion method.

Hyperimmune sera against spherules and against arthrospores of Coccidioides immitis were prepared by inoculation of rabbits. The antibody content of these sera was studied by the agar gel diffusion method. It was observed that antispherule pooled sera formed multiple precipitin bands with extracts of spherules and of arthrospores. The antiarthrospore pooled serum, however, failed to precipitate with the spherule extract, and formed a single band in the presence of an arthrospore solution. When the spherule and the arthrospore extracts were tested with a variety of different antisera, it was observed that the spherule preparation formed bands only in combination with anti-purified spherule pooled serum, whereas the arthrospore extract precipitated with anti-purified spherule, antiarthrospore, and anti-Histoplasma capsulatum pooled sera. It was also observed that a spherule culture supernatant solution formed five precipitin bands in combination with anti-spherule pooled sera, formed one band with pooled antiserum from rabbits with coccidioidomycosis, and did not precipitate in the presence of antiarthrospore pooled serum. Coccidioidin, however, formed two bands in the presence of any of these antisera. It was therefore concluded that extracts from the spherule phase of C. immitis differed from solutions obtained from the arthrospore and mycelial phases.

Animals↗
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↗
PubMed1967

Ribosomes and ribosomal protein from Neurospora crassa. I. Physical, chemical, and immunochemical properties.

Ribosomes from Neurospora crassa, initially characterized by ultracentrifugal and immunochemical analyses, have been used to prepare ribosomal protein for physical, chemical, and immunochemical study. The acrylamide gel disc electrophoretic profiles of Neurospora ribosomal protein exhibit a degree of heterogeneity comparable to what has been observed in other systems. Only by chemical modification or by aggregation of the protein do alterations in the profile become apparent. Disulfide-bond formation appears to play a role in the aggregation of ribosomal protein to complexes of S(20,w) = 200. The aggregation can be prevented by alkylation of -SH groups, and protein treated in this fashion has a subunit molecular weight of about 20,000 as determined by equilibrium centrifugation. Finger-printing of tryptic peptides indicates that more than one unique sequence of amino acids must be present in ribosomal protein, although gross primary structural heterogeneity is questioned. Antigenic heterogeneity is much less apparent; only a few precipitin bands are resolved by immunodiffusion tests, although complete reactivity of total ribosomal protein is suggested by quantitative precipitin analysis. The antigenically active ribosomal protein components appear to reside in at least two fractions; one is removed readily from the ribosome by CsC1 treatment. Ribosomal protein of N. crassa possesses antigenic determinants present in E. coli ribosomal protein as judged by spur formation in immunodiffusion tests.

Amino Acids↗