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PubMedDate not supplied

Peptide autoantigenicity of the small nuclear ribonucleoprotein C.

OBJECTIVE: This study determines the antigenic regions of the nRNP C lupus autoantigen. METHODS: Twenty-one anti-nRNP C sera, six patients with other autoimmune serology, and five normal control sera were assessed for binding with the overlapping octapeptides of the nRNP C protein. Column absorptions were conducted to assess the percentage of the anti-nRNP response which was directed against one major epitode of nRNP C: RESULTS: Eleven regions of nRNP C are bound in different combinations by anti-nRNP C patient sera. Neither normal controls nor patients without anti-nRNP C antibodies significantly bind any regions of nRNP C: The antigenic region spanning amino acids 117-126, PAPGMRPP, is recognized by all twelve Sm, nRNP precipitin positive patients tested. Indeed, from 14 to 32% of the anti-nRNP reactivity in Sm, nRNP precipitin positive patient sera is directed against PAPGMRPP: All of these patients also bind a very similar sequence which is repeated three times in the Sm B/B' protein. Patients sera with only anti-nRNP antibodies, however, do not recognize this proline rich sequence as antigenic. CONCLUSION: This elucidation of the specific areas of nRNP C which are important in the autoantigenicity of nRNP C will hopefully lead to a better understanding of the involvement of these autoantibodies in the etiology and pathogenesis of SLE.

Amino Acid Sequence↗
PubMed1995

Allergic bronchopulmonary aspergillosis: a case report.

Aspergillus-associated pulmonary diseases are aspergilloma, invasive aspergillosis, and allergic bronchopulmonary aspergillosis. Allergic bronchopulmonary aspergillosis is caused by a complex of immunologic reactions to the presence of the Aspergillus species colonizing the bronchial trees. The disease is not common in Taiwan. The major diagnostic criteria for allergic bronchopulmonary aspergillosis are 1) bronchial asthma, 2) pulmonary infiltration, 3) peripheral eosinophilia, 4) positive skin test to Aspergillus fumigatus, 5) serum precipitin to Aspergillus fumigatus, 6) elevated serum Ig E, and 7) central bronchiectasis. We report a case who has had a chronic asthmatic-like cough for 5 years. He worked in a silo for two years before he was troubled by the disease. He was admitted to hospitals four times in the past, and received five bronchoscopic examinations and one open lung biopsy without definite diagnosis. Sputum eosinophilia directed our attention to the differentiation of eosinophilic lung diseases. A bronchogram which revealed central brochiectasis helped us to make the diagnosis of allergic bronchopulmonary aspergillosis, despite negative sputum culture for Aspergillus fumigatus and negative serum precipitin to Aspergillus fumigatus.

Aspergillosis, Allergic Bronchopulmonary↗
PubMed1975

The serology of Pseudomonas aeruginosa analysed by means of quantitative immunoelectrophoretic methods. II. Comparison of the antibody response in man against thirteen O groups of Ps. aeruginosa.

The occurrence of antibodies against antigens prepared from strains representing 13 O groups of Pseudomonas aeruginosa and against a polyvalent Ps. aeruginosa antigen (St-Ag) has been investigated in sera from 100 patients. By means of fused rocket immunoelectrophoresis with intermediate gel it was found that the humoral immune response against Ps. aeruginosa resulting in precipitating antibodies will be detected by St-Ag as well as by any other of the antigen samples investigated. Six of the sera contained group-specific antibodies which were revealed by only one of the antigen samples used and not by St-Ag. These six sera were further studied by means of various quantitative immunoelectrophoretic methods using St-Ag as well as antigens prepared from the infecting Ps. aeruginosa strain in the patient concerned. In all six sera, only one extra precipitin could be detected using antigens prepared from the homologous strain instead of St-Ag. This extra precipitin corresponded presumably to group-specific O-antigens not included in St-Ag. In sera from patients, these group-specific antibodies were always accompanied by antibodies against antigens common to all strains of Ps. aeruginosa.

Antibodies, Bacterial↗
PubMed1975

Covalently bound FAD in d-6-hydroxynicotine oxidase. Immunological studies of D- and L-6-hydroxynicotine oxidase: evidence for a D-enzyme precursor.

Antersera prepared against both enantiozymes, D- and L-6-hydroxynicotine oxidase, formed precipitins in double diffusion tests with their respective antigens only. A mixture of the two antisera caused spur formation of the two precipitin lines obtained with the pure enzymes. Antiserum to L-apoprotein reacted with native L-enzyme and L-apoprotein but not with the D-sspecific enzyme. D-6-hydroxynicotine oxidase activity was inhibited by the anti-D-antiserum, leaving the L-enzyme fully active, while anti-L-antiserum inhibited the L- but not the D-specific activity. The delayed induction of D-6-hydroxynicotine oxidase as compared to the other activities of the nicotine-degrading sequence and the differential immunochemical behavior of the enantiozymes allowed the search for a D-enzyme precursor. In cells harvested 3 hours after the addition of DL-nicotine, the L-enzyme activity was present, whereas no D-enzyme activity could be detected. However, an extract of these cells did form an immunoprecipitin line with anti-D-antiserum. L-6-Hydroxynicotine oxidase, but no D-6-hydroxynicotine oxidase activity, could also be induced in Arthrobacter oxidans grown in a medium with a high glucose content and DL-nicotine as the sole nitrogen source. An extract of these L-induced cells produced the specific immunoprecipitation with anti-D-antiserum. A pulse-chase experiment with cells grown first on glucose and DL-nicotine in the presence of [14C]leucine and then in an unlabeled medium which induces D-6-hydroxynicotine oxidase activity resulted in a radioactive D-enzyme-immunoprecipitin line. From these experiments it is concluded that a precursor of the active D-enzyme is induced simultaneously with the other nicotine-degrading enzymes.

Arthrobacter↗
PubMed1975

Fractionation of a soluble somatic extract and solubilized cuticular extracts of Dipetalonema viteae adult worms.

A soluble somatic preparation (SSP) of adult Dipetalonema viteae was prepared. Aliquots of the aqueous insoluble debris (cuticles and membranes) left after the extraction of SSP were solubilized separately with Triton X-100 and lithium diiodosalicylate to yield a Triton solubilized preparation (TSP) and lithium diiodosalicylate solubilized preparation (LSP), respectively. SSP was sequentially chromatographed on a series of Sephadex columns, G50; then fraction 1 from G50 on G100 and finally fraction 1 from G100 on G200 yielding 5, 4, and 5 fractions on G50, G100, and G200, respectively. TSP and LSP were each sequentially chromatographed on Sephadex G50 and G200 to yield 5 and 4 fractions for TSP and 6 and 3 fractions for LSP, respectively. Each Sephadex fraction from each separation was further resolved by polyacrylamide gel electrophoresis (PAGE). Immunodiffusion studies with a rabbit antiserum to SSP gave 4 precipitin bands with SSP, 1 with TSP, and none with LSP. The single precipitin arc produced with TSP showed partial identity with an SSP arc. Disc immunoelectrophoresis allowed the identification of the proteins separated by PAGE, which precipitated with the rabbit anti-SSP serum.

Animals↗
PubMed1978

Antigenic glycopolypeptides HA1 and HA2 of influenza virus haemagglutinin. II. Reactivity with rabbit sera against intact virus and purified undissociated haemagglutinin.

Rabbit sera produced against either intact virus or purified undissociated haemagglutinin were examined for reactivity with highly purified haemagglutinin glycopolypeptides. Sensitive radioimmunoassay for 125I-labelled glycopolypeptides revealed antibody reactive with either glycopolypeptide HA1, or glycopolypeptide HA2. Antibodies against the carbohydrate moiety were responsible only for a part of the binding activity. Under the conditions employed, the binding activity for glycopolypeptide HA2 was much stronger than for glycopolypeptide HA1. Competition assays suggested that immune reactivities were due to distinct antibody populations (i.e. with a specifity for glycopolypeptide HA1 and glycopolypeptide HA2, respectively). The immune reactivity to both haemagglutinin constituents, glycopolypeptides HA1 and HA2, was also shown by gel double diffusion. The precipitin line(s) corresponding to glycopolypeptide HA1 was (were) usually more distinct than precipitin line(s) corresponding to glycopolypeptide HA2. The glycopolypeptides HA1 and HA2 showed the reaction of nonidentity in immunodiffusion analysis.

Animals↗
PubMed1976

Rapid specific identification of group D streptococci by counterimmunoelectrophoresis.

Clinical isolates of group D streptococci have been examined by counterimmunoelectrophoresis (CIE) to determine if this method might be of value in the rapid identification of the members of this group. Group D organisms identified by classical biochemical and serologic procedures were inoculated into Todd Hewitt broth and incubated at 37 degrees C. After 4 hours of incubation, free group D streptococcal antigen was detected in broth cultures from 70 of 70 group D enterococcal strains. Precipitin lines were readily visible immediately after electrophoresis in each case. In contrast, 10 nonenterococcal group D strains failed to produce detectable free group D antigen in the Todd Hewitt broth after 4, 24, or 48 hours incubation. Such antigen was detectable, however, after 48 hours incubation in Mueller Hinton broth containing 10 grams of glucose per liter. Representative strains of group A, C, G, and B streptococi, Streptococcus viridans and Streptococcus pneumoniae grown in Todd-Hewitt broth for 4 hours gave no precipitin lines when reacted against adsorbed monospecific group D antiserum. Group D antigen was also detected in broth cultures of direct swabs and in 18-hour blood culture broths. CIE appears to be a rapid and sensitive procedure for identification of the enterococcal strains of group D streptococci from clinical isolates.

Counterimmunoelectrophoresis↗
PubMed1976

Platelet glycocalicin. II. Purification and characterization.

Glycocalicin, a major glycoprotein of the platelet glycocalyx, is obtained in soluble forms following platelet homogenization and has been purified to homogeneity. Glycalicin has a molecular weight of 148,000 (+/- 5,000) as determined by gel electrophoresis. It contains 60 grams % carbohydrate (46.6 mol %) comprising galactose, N-acetylgalactosamine, N-acetylglucosamine, and sialic acid as its principal sugars in a ratio of 2:1:1:2, but with a small amount of glucose (2.3 mol %), mannose (1.2 mol %), and fucose (1.9 mol %). The principal amino acids are serine and threonine (4.9 and 7.6 mol %), leucine (6.7 mol %), proline, (6.8 mol %), and aspartic and glutamic acids (4.7 and 5.8 mol %). Tryptic digestion of glycocalicin yielded a macroglycopeptide (Mr = 118,000 +/- 5,000) identical with that previously obtained from intact platelets (Pepper, D.S., and Jamieson, G.A. (1970) Biochemistry 9, 3706-3713) and a peptide of molecular weights 45,000 (+/- 2,000) which contained only 7 mol % carbohydrate. This peptide showed a significant enrichment of serine, glycine, and glutamic acids compared with glycocalicin and together these amino acids comprised over 50 mol % of the peptide. Purified glycocalicin gave a single precipitin line with antiserum prepared in chickens. It showed reactions of partial identity with both the macroglycopeptide and the (non-glyco)peptide obtained by tryptic digestion and these showed lines of partial identity with each other. These results suggest that at least three determinants are present in the intact molecule. Glycocalicin gave precipitin reactions with wheat germ agglutinin and with the lectin of Agaricus bisporus.

Amino Acids↗
PubMedDate not supplied

[Serological researches in the bacterial respiratory tract infections (author's transl)].

Previous studies on the serological diagnosis of the lower respiratory tract infections caused by bacteria have been reviewed. The most significant results have been up to today obtained with the double immunodiffusion technique (Ouchterlony) for detecting different, specific and aspecific, bacterial precipitins in the serum of the patients, and with the immunoelectrophoresis which allows to distinguish specific precipitine lines from the aspecific ones. Among the other immunological methods, bacterial agglutination, passive haemagglutination, cross-over-immunoelectrophoresis, complement fixation, and immunofluorescence have been only occasionally used, but further comparative studies are needed and suggested to establish their diagnostic value. Other technical problems, as purity of antigens or cross-reactivity of antibody or antibodies level evaluation, are raised and discussed. Further improving of the serological methods would allow their routine use in clinical bacteriology as a useful tool in the assessment of pathogenicity of the bacterial species in the sputum and in the ethiological diagnosis of broncho pulmonary infections, at least of those cases in which exclusive relaying on sputum cultures could be fallacious.

Antibodies, Bacterial↗
PubMed1976

Heterogeneity of concanavalin A receptors on Ehrlich tumor cells.

Concanavalin A (Con A)-binding glycoproteins have been purified from Ehrlich ascites tumor cells by precipitation of cell extracts with Con A in agarose gels and by lithium diiodosalicylate (LIS) extraction. Antisera prepared against these two glycoprotein fractions indicate the presence of a minimum of five different antigens in the Con A-cell extract precipitate and a minimum of three different antigens in the LIS-extracted preparation. That both kinds of antisera are directed towards surface membrane antigens is strongly suggested by the fact that they give precipitin bands with purified plasma membrane from Ehrlich cells, they agglutinate whole cells, and they no longer give precipitin bands after absorption by whole cells. Cell extract material which was specifically eluted from a Con A-Sepharose 4B column with alpha-methylmannoside was recognized by antisera to both glycoprotein preparation, demonstrating that the antigens were Con A-binding components; material which did not bind the column failed to react with either antisera. Immunochemical analysis indicated that one of the antigens present in the LIS-extracted material was distinct from the five antigens prepared by lectin precipitation in agarose gels suggesting that a minimum of six individual Con A receptors are present on the surface of Ehrlich tumor cells. Immunochromatography was found to be a convenient method to purify the antigens obtained by the LIS extraction of Ehrlich cells.

Animals↗
PubMed1995

Immunodiagnostic moieties in somatic and excretory/secretory antigens of Fasciola gigantica.

Immunodiagnostic potential fractions in fluke antigens and excretory/secretory (E/S) antigen of F. gigantica have been identified using double immunodiffusion (DID), immunoelectrophoresis (IEP) and sodium dodecyl sulphate (SDS) PAGE electrophoresis. Hyperimmunised rabbits elicited considerable level of antibody response with few precipitin lines showing reaction of identity in DID suggesting presence of some common fractions in all antigens. Mature fluke somatic (MFSAg) and immature fluke somatic (IMFSAg) antigens showed exactly similar pattern of precipitin lines in both DID and IEP. Antibodies to experimentally infected rabbits with F. gigantica were also detected by DID using MFSAg and E/S antigens at 4 weeks post infection. However, out of 6-7 fractions obtained from Sephadex G-200 column chromatography in MFSAg and IMFSAg antigens only F3, F4 and F5 along with E/S antigen were able to detect antibodies by DID. Mature fluke and E/S antigen separated out in 9 bands in the range of 12 to 95 kDa and 5 bands in the range of 12 to 29 kDa respectively of which proteins of molecular weight 12, 15, 18, 28 and 29 kDa were common in both antigens. Therefore, it appears that immunodiagnostic fractions of antigens may be present in between 12 and 29 kDa.

Animals↗
PubMed1997

[A case of humidifier lung characterized by histopathologic feature].

A 61-year-old man was discharged from our hospital after recovering from bilateral fractures in the neck of each femur. However, a productive cough, dyspnea, and a high grade fever occurred eight hours after returning home. He was thus admitted once more. At rehospitalization, there was radiographic evidence of bilateral infiltrates and hypoxemia. Hypersensitivity pneumonitis was strongly suggested by radiographic evidence, by the fact that no new drugs had been administered, and by a positive result after an environmental provocation test. A diagnosis of humidifier lung was confirmed by a positive precipitins test for humidifier water. Several microorganisms were isolated from humidifier water, and precipitins tests for the isolated microorganisms were mostly positive. Microscopic examination revealed focal alveolitis, bronchiolitis, and perivasculitis. Perivascular leucocytic infiltrations around venules suggested that inhaled antigens might have also caused humidifier lung via a vascular route. Humidifier lung may be due in part to soluble factors, such as endotoxin, present in humidifier water.

Alveolitis, Extrinsic Allergic↗
PubMedDate not supplied

[Immuno-electro-diffusion on cellulose acetate membrane for serological testing in human malaria (author's transl)].

An immuno-electro-diffusion assay for human malaria, using cellulose acetate gel, is described. More than 3500 sera have been tested by this method, which proved very useful for epidemiology since 400 sera a day can be tested by one person, with simple equipment. Its sensitivity compared well to the IFA test, although the antibodies revealed are quite different. A constnat precipitin line appeared, against 56 degrees C labile antigens, in sera of subjects infected by P. falciparum, and up to 8 other precipitins per serum tested. The test may be useful in analyzing these multiple antibodies occurring in patients with malaria.

Adolescent↗
PubMed1979

Different Tridacnins in different Tridacnid clams: a comparative study.

1. Haemolymph samples from different Tridacnid clams were tested for haemagglutinin activity, using normal and enzyme-treated red cells from different sources. 2. Precipitin reactions with these haemolymph fluids were performed in agar gel, using several defined glycosubstances of different origin. 3. In several experiments it could be demonstrated that in all Tridacnid haemolymph samples anti-galactosyl ("anti-galactan") specific lectins do occur, however, they definitely differ from each other.

Agglutinins↗
PubMed1964

SEPARATION OF TEICHOIC ACID OF STAPHYLOCOCCUS AUREUS INTO TWO IMMUNOLOGICALLY DISTINCT SPECIFIC POLYSACCHARIDES WITH ALPHA- AND BETA-N-ACETYLGLUCOSAMINYL LINKAGES RESPECTIVELY. ANTIGENICITY OF THEICHOIC ACIDS IN MAN.

Human sera were found to contain antibodies precipitating with each of two samples of teichoic acid of Staphylococcus aureus prior to immunization; these antibodies were probably formed as a result of contact or infection with this microorganism. Injection of teichoic acid into two individuals resulted in a rise in circulating antibody to teichoic acid; a third subject probably had a primary response to alpha-teichoic acid. Quantitative precipitin and agar diffusion studies revealed the presence of two distinct antibodies in the sera and showed that each specimen of teichoic acid was a mixture of two polymers an alpha-linked N-acetylglucosaminyl-ribitol polymer and a beta-linked N-acetylglucosaminyl-ribitol polymer, termed alpha- and beta-teichoic acids respectively. The alpha-teichoic acid anti-alpha-teichoic acid system was inhibited best by alpha-linked glucosaminides and the beta-anti-beta-teichoic acid system was inhibited best by a beta-linked glucosaminide. The alpha- and (beta-teichoic acids could be separated from each other by specific precipitation under appropriate conditions and recovered from the washed specific precipitates. The existence of two distinct teichoic acid polymers raises important questions as to cell wall structure and the biosynthesis of the teichoic acids.

Bacteriological Techniques↗
PubMed1965

A STUDY OF THE CROSS-REACTIVITY OF ANTIPURIN-6-OYL SERUM WITH DEOXYRIBONUCLEIC ACID (DNA).

The specificity of the reaction of antipurin-6-oyl sera with thermally denatured DNA has been studied by means of hapten inhibition techniques. The relative order of effectiveness of various haptens as inhibitors of the complement fixation reaction between DNA and antipurin-6-oyl serum was found to be comparable to their relative order of effectiveness as inhibitors of the precipitin reaction between purin-6-oyl-protein conjugates and antipurin-6-oyl serum. Antipurin-6-oyl antibody has been purified and has been shown to be capable of reacting with thermally denatured DNA. It is concluded that the reactivity of these purine-specific antisera with DNA is a property of antibody with specificity for the purin-6-oyl moiety. In addition, the reaction between antipurinoyl sera and DNA has been demonstrated by the techniques of radioimmunoelectrophoresis and passive cutaneous anaphylaxis.

Anaphylaxis↗
PubMed1965

THE CELL WALLS OF GROUP D STREPTOCOCCI. I. THE IMMUNOCHEMISTRY OF THE TYPE 1 CARBOHYDRATE.

Group D Types 1 and 26 cell walls and the corresponding type-specific carbohydrates, extracted from the walls by various means, contain rhamnose, glucose, galactose, N-acetylglucosamine, and N-acetylgalactosamine. Mucopeptide elements are also present in the walls and in enzymatically-extracted carbohydrates. Types 1 and 26 carbohydrates extracted by formamide contain no mucopeptide, but the serologic reactivity of Type 1 antigen is destroyed by this procedure. The Type 1 antigen was successfully extracted, however, by a new technique involving autolysis of cell walls at pH 6.2. The type carbohydrate prepared by this procedure has chemical and serological similarities to the antigens prepared by the S. albus enzyme and the lysozyme methods. Quantitative precipitin inhibition studies with Type 1 antigen and antibody indicate that D-glucose and N-acetylglucosamine may be components of the antigenic determinant. The terminal residue is probably bound by an beta-glycosidic bond to the subterminal sugar. Similar studies with the Type 26 carbohydrate have not revealed any of the chemical features of the antigenic determinant.

Antibodies↗
PubMed1983

Study of immunological parameters in farmer's lung.

A cross-sectional epidemiological study was carried out on 2932 farmers (response rate 92%) living in Northern Italy. A questionnaire on respiratory symptoms was supplied, chest X-ray taken and simple spirometry tests made. Thirty-nine subjects reported attacks of breathlessness associated with fever after exposure to mouldy hay; thirty-six had a clinical history of farmer's lung and X-ray and/or respiratory function changes indicative of chronic farmer's lung; 113 were classified as having bronchial asthma. These 118 subjects and a random sample of 131 non-symptomatic subjects were examined by intracutaneous skin tests and double diffusion precipitation tests with antigens associated with farmer's lung. All sera positive by precipitation were examined by immunoelectrophoresis, counterimmunoelectrophoresis, and C1q binding test, and Bovine conglutinin test in solid phase for the detection of circulating immunocomplexes. 27.8% cases of chronic farmer's lung, 4.4% of cases of bronchial asthma and 2.3% of non-symptomatic subjects showed precipitating antibodies against farmer's lung antigens. Of the precipitin-positive subjects, the majority had precipitating antibodies against Micropolyspora faeni. No differences in immunoelectrophoregrams in number and pattern of precipitation arcs for M. faeni were found between chronic farmer's lung and bronchial asthma subjects. Circulating immune complexes were present in 50% of chronic farmer's lung patients, 40% of those with bronchial asthma and 33.3% of non-symptomatic subjects. Three farmer's lung subjects (9.3%) showed immediate skin-test reactions to rural environmental allergens.

Antibody Formation↗