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PubMed1960

Immunologic production of antiangiotensin. II. Production and detection of antiangiotensin.

The parenteral administration of benzoylangiotensin II-azo-BGG to rabbits produced an antiserum with antiangiotensin activity. Antiangiotensin inhibited the biological action of p-aminobenzoylangiotensin II, valine(5)-angiotensin II (free acid form), isoleucine(5)-angiotensin II and valine(5)-angiotensin II (amide form), but it was totally inert towards angiotensin 1. Antiangiotensin activity was distinguished from that of serum angiotensinase by the following observations: (a) an angiotensinase-free gamma-globulin fraction contained antiangiotensin, (b) angiotensinase inactivated angiotensin II (both the amide and free acid forms) and angiotensin I in contrast to the remarkable specificity for angiotensin II exhibited by antiangiotensin. Serological demonstration of antiangiotensin included: (a) a comparison of its precipitin reaction with the angiotensin BGG complex with the reaction with BGG alone, (b) the partial inhibition of the precipitin reaction with the angiotensin BGG complex by angiotensin II, (c) a precipitin reaction with a different angiotensin II protein complex (cat serum). Angiotensin II administered parenterally as the free polypeptide was not antigenic.

Angiotensin Amide↗
PubMed1960

Preparation and antigenicity of M protein released from group A, type 1 streptococcal cell walls by phage-associated lysin.

The lysis of Group A type 1 streptococcal cell walls by phage-associated lysin has been described. In the preparation of lysin, a new semisynthetic non-protein media to support growth of the propagating strain of Group C streptococci was employed. Following lysis of the cell walls, the resulting digest was partially purified by ion-exchange chromatography and ammonium sulfate precipitation. In addition to M protein, the resulting preparation (called lysin M protein) contained the group-specific carbohydrate and the T protein-but did not contain antigens, detectable by precipitin tests, which cross-reacted with absorbed heterologous group or type antisera. Capillary precipitin reactions between the lysin M protein and type-specific antiserum did not occur in the presence of high ionic strength buffers; these buffers did not similarly affect precipitin reactions of acid M protein. Type 1 lysin M protein is shown to be a good antigen. A total of 1.5 mg. injected intradermally in saline produced bactericidal antibody in eight of nine rabbits; when injected in adjuvant in one rabbit, protective serum antibodies developed. Streptococci grown in sera from seven of nine rabbits immunized with lysin M protein demonstrated significantly longer chains than when grown in normal rabbit serum. Antibody as demonstrated by each of these three tests was shown to be type-specific. No local or systemic toxicity was noted following intradermal injection in rabbits of lysin M protein.

Animals↗
PubMed1963

Antigenic relationships of Bence Jones proteins, myeloma globulins, and normal human gama-globulin.

By means of immunodiffusion and immunoelectrophoresis study has been made of antigenic relationships of Bence Jones proteins, and the three classes of normal and pathological immunoglobulins, 7S gamma, beta(2A), and beta(2M). All thirty-nine Bence Jones proteins studied could be classified into either one of two distinct antigenic types, A or B. Both types are related to the immunoelectrophoretically slow (S) fragment of a papain digest of normal gamma-globulin; B is related more closely than A, but neither has antigenic determinants in common with the fast (F) fragment. The 7S gamma myeloma globulins were either immunological type I or II. The papain digests of these proteins produced the S and F precipitin lines in immunoelectrophoresis but multiple bands in starch gel electrophoresis, especially in the F region. The S fraction of type I myeloma globulins is antigenically similar to Bence Jones protein of type B, and the S component of type II myeloma globulins has antigenic determinants in common with type A Bence Jones protein. Correspondingly, myeloma patients with type I globulins and proteinuria usually excrete type B Bence Jones proteins, whereas patients with type II excrete type A proteins. The F fragment is the part common to normal 7S gamma-globulin and types I and II myeloma globulins but is absent in beta(2A) and beta(2M) pathological globulins and in both types of Bence Jones proteins. Papain digests of beta(2A) myeloma globulins produced a single precipitin line in immunoelectrophoresis. beta(2A) myeloma globulins appeared to have two antigenic units, one in common with type B Bence Jones protein and normal gamma-globulin, and another specific to beta(2A). The beta(2A) myeloma patients excreted type B Bence Jones protein. The papain digest of a macroglobulin produced two precipitin lines, the faster of which had antigenic determinants in common with type B Bence Jones protein, the slower seemed specific for the macroglobulin. Five serum micromolecular globulins proved to be either type A or B Bence Jones proteins. From the above results, an antigenic map was constructed showing which determinants are shared and which are specific for normal 7S gamma-globulin, types I and II myeloma globulins, beta(2A) myeloma globulins, a macroglobulin, and types A and B Bence Jones proteins.

Aged↗
PubMed1950

The role of non-precipitating antibodies in the passive sensitization of human skin by rabbit anti-ovalbumin.

Sera of fourteen rabbits injected with alum-precipitated recrystallized ovaltumin, containing 0.046 to 0.604 mg. of precipitable antibody nitrogen per ml. (average 0.299 mg.), passively sensitized human skin, while the sera of nine rabbits injected with dissolved recrystallized ovalbumin, containing from less than 0.05 to 0.420 of antibody nitrogen per ml. (average 0.176 mg. or less), were inactive in human skin. The skin-sensitizing activity of the sera bore no relation to the precipitin content. Removal of 68 to 90 per cent of the precipitin nitrogen by a single addition of antigen did not affect the activity of the sera in sensitizing human skin. Removal of all precipitable antibody nitrogen in one serum by a single addition of antigen removed the skin-sensitizing activity. The "univalent" antibody remaining after complete removal of precipitin by fractional addition of antigen showed the same activity in passive sensitization of human skin as the original serum.

Anaphylaxis↗
PubMed1987

Immunological properties of a penicillinase produced by Alcaligenes denitrificans subsp. xylosoxydans.

Rabbit antiserum was prepared to the penicillinase of Alcaligenes denitrificans subsp. xylosoxydans GN14062. The antibody gave a single precipitin line in double immunodiffusion assays with the penicillinases from strain GN14062 and from two other A. denitrificans subsp. xylosoxydans strains. The precipitin line given by the GN14062 enzyme gave a reaction of complete identity with the precipitin lines of the penicillinases from the other A. denitrificans subsp. xylosoxydans strains. Furthermore, activity of the penicillinases from all three A. dentrificans subsp. xylosoxydans strains was neutralized by the antiserum to the GN14062 enzyme. Thus it was proved that the penicillinases produced by the three A. denitrificans subsp. xylosoxydans strains were immunologically identical. Penicillinases types I, II, III, IV, V, SHV-1, TEM-1, TEM-2, and the chromosomal penicillinases of Klebsiella pneumoniae GN69 and A. faecalis GN14061 formed no immunoprecipitate with, nor were neutralized by, the antiserum to the GN14062 enzyme. From these results, it was concluded that the penicillinase produced by A. denitrificans subsp. xylosoxydans was immunologically distinct from the penicillinases produced by these other bacteria.

Alcaligenes↗
PubMed1985

Antigenic determinants of acylphosphatase from porcine skeletal muscle.

Analysis of the quantitative precipitin reaction of acylphosphatase from porcine skeletal muscle with rabbit antiserum indicated the presence of at least two antigenic determinants on the porcine enzyme molecule. Immunological cross-reactivities of acylphosphatases from equine and rabbit skeletal muscles were examined. In double immunodiffusion with the antiserum, the precipitin lines of the porcine and equine enzymes completely fused, while the rabbit enzyme gave no precipitin line. The reaction between the 125I-labeled porcine enzyme and its antibody was inhibited to the same extent by the porcine and equine enzymes, but not by the rabbit enzyme. The three enzymes were similar in net charge and molecular weight on polyacrylamide gel electrophoreses. No conformational difference among the three enzymes was observed in their circular dichroism spectra. The amino acid composition of the rabbit enzyme differed from those of the porcine and equine enzymes in the contents of Glu, Gly, Lys, and Arg. Differences in the sequence of the rabbit enzyme from that of the porcine enzyme were investigated by comparison of the peptide maps of the tryptic peptides of the two enzymes. Four peptides of the rabbit enzyme were located at different positions from those of the porcine enzyme. Three of the four peptides from both enzymes were sequenced and all the tryptic peptides of both enzymes were characterized by amino acid analysis. The tryptic peptides of rabbit enzyme were tentatively aligned on the basis of their amino acid compositions and sequence homologies, compared with the corresponding peptides of the porcine enzyme. Among five amino acid residues of the porcine enzyme, Arg-4, Asp-28, Arg-31, Glu-56, and Ile-68, which are replaced in the rabbit enzyme, Arg-4 and Asp-28 are considered to be included in the antigenic determinants.

Acid Anhydride Hydrolases↗
PubMed1994

A glycoprotein secreted by lung cancer cells is present in human serum as an immunoglobulin-binding protein.

The 6B3-Ag recognized by a monoclonal antibody 6B3 to human large cell lung carcinoma cell line (HLC-2) is a high-molecular-weight glycoprotein of 1,000,000. Its serum level is increased in various adenocarcinoma patients. When a patient's serum with a high concentration of 6B3.Ag (54 micrograms/ml) or concentrated 6B3.Ag from normal human serum was analyzed by immunoelectrophoresis, 6B3.Ag showed a long bimodal precipitin line extending from the per-beta to beta globulin region. However, the precipitin line of 6B3.Ag in the HLC-2 culture medium was formed only in the pre-beta globulin region. The 6B3.Ag was purified from pooled patients' serum by salting out, precipitation by acidification at pH 4.5 and Sepharose 4B and immunoaffinity chromatographies. Western blotting indicated that the 6B3.Ag from human serum contained IgG and/or IgM. The 6B3.Ag from human serum showed a dose-dependent reaction in a sandwich enzyme-linked immunosorbent assay with anti-6B3.Ag antibody as a solid-phase antibody and anti-human IgG or anti-human IgM antibody labeled with alkaline phosphatase. The 6B3.Ag was concluded to be partly present as a complex with IgG and/or IgM in human serum, and this complex showed a precipitin line in the beta globulin region on immunoelectrophoresis.

Antigens, Neoplasm↗
PubMed1984

Experience with allergic bronchopulmonary aspergillosis: some unusual features.

The clinical and immunologic features of ten patients with allergic bronchopulmonary aspergillosis (ABPA), observed over periods varying from 12 months to 10 years, are reported. Acute attacks of ABPA were characterized by several, or all of: increased cough and sputum, haemoptysis, pleuritic pain, expectoration of sputum plugs, and increasing airways obstruction. Peripheral blood eosinophilia and acutely elevated serum IgE levels were seen in all patients during acute attacks, sputum eosinophilia and recovery of Aspergillus in sputum was less common. However, blood eosinophilia was not present in all attacks of ABPA and sputum eosinophilia varied similarly from one attack to another. Six patients with previously documented multiple precipitin lines have had no demonstrable precipitins to Aspergillus on several occasions between attacks, three of these patients have also been negative during attacks. Five of the six patients have again developed positive precipitin lines. The total number of episodes in these ten patients was fifty two, three patients have had more than nine acute attacks of ABPA. There is no seasonal variation in this group of patients. Since diagnosis, only three patients have had an attack-free interval longer than 12 months. Two patients are steroid-dependent because of severe asthma, and nine have symptoms of bronchiectasis.

Adult↗
PubMed1986

Enzyme-linked immunofiltration assay (ELIFA) for the detection of specific antibodies (IgG-IgM-IgA-IgE) in farmer's lung disease.

Until now the detection of chymotrypsic or polysaccharidic arcs among precipitating systems indicated a positive diagnosis of Farmer's lung disease (FLD). It was shown that the occurrence of chymotrypsic activity is not absolutely correlated with the presence of clinical disease. The presence of different classes of specific precipitating antibodies was looked for and correlated with clinical symptoms in an attempt to find additional positive criteria for the diagnosis of FLD. The enzyme-linked immunofiltration assay (ELIFA) was adapted to detect the different specific antibody classes. 1400 serum samples were studied from 1350 farmers exposed to mouldy hay. Of 1358 samples examined from asymptomatic subjects tested as part of a systematic screening of the profession, 1356 had either no precipitins or have precipitins detected solely against non-chymotrypsic and non-polysaccharidic antigens. Ten specimens with precipitins joined the study. Only two serum samples from two symptomless individuals showed positive serological criteria for FLD as evidenced by the presence of a chymotrypsic band. The remaining forty-two serum samples from twenty-four patients with clinical signs of extrinsic allergic alveolitis had serological criteria for FLD as either chymotrypsic or polysaccharidic arcs. Only specific IgG in asymptomatic subjects was demonstrated, and when a supplementary class of specific antibody (IgM, IgA or IgE) was detected, there was clinical evidence of FLD in all except one case. Thus ELIFA could prove to be a useful tool for the positive diagnosis and prognosis of patients with FLD. In addition this method allows the recognition of a particular functional antigenic fraction of M. faeni by all classes of specific antibodies between different serum samples.

Antibodies, Bacterial↗
PubMed1993

Pigeon breeders' lung; IgG subclasses to pigeon intestinal mucin and IgA antigens.

Sera from all symptomatics with pigeon breeders' lung and many non-symptomatic pigeon breeders react specifically with the pigeon antigens and in particular pigeon intestinal secretions and isolated pigeon intestinal mucin and IgA. In sera from all 82 precipitin-positive pigeon breeders investigated, IgG1 reacted with both IgA and mucin, while IgG2 reacted predominantly with mucin only. Sera from all 32 symptomatic patients with pigeon breeders' lung demonstrated an IgG3 reaction with mucin, but only three sera showed reactivity against IgA and this was very weak. In contrast, only three out of 27 pigeon breeders with pulmonary pathology other than pigeon breeders' lung and only three out of 23 sera from healthy pigeon breeders showed detectable IgG3 reactivity with mucin. IgG4 from eight sera only reacted with mucin (n = 7) or IgA (n = 1) and showed no consistent pattern between subject groups. Precipitin-negative sera from 30 volunteers with no previous pigeon exposure showed no IgG subclass reactivity with either the pigeon intestinal secretions or the isolated mucin and IgA antigens. These results show specific IgG2 and IgG3 subclass reactivity to pigeon intestinal mucin antigen in precipitin-positive sera from pigeon breeders. Further IgG3 subclass reactivity specific to pigeon mucin is strongly associated with sera from patients with the active pigeon breeders' lung disease.

Adolescent↗
PubMed1977

Antigens of the subcellular fractions of Trypanosoma cruzi. II. Flagellar and membrane fraction.

A method for isolation of membrane and flagellar fractions from Trypanosoma cruzi epimastigotes, and descriptions of their ultrastructural characteristics and antigenic activity are presented. Electron-microscopic observation revealed that the membrane fraction resembled vesicles, as occurs frequently when the pressure-depressure method is used for cell disruption. The flagellar fraction revealed flagella and some membranes, both related and unrelated to the flagellar structure. Flagellar and membrane fractions had 5 and 3 precipitin lines respectively against anti-whole homogenate of T. cruzi, in double diffusion tests. One of the precipitin bands common to both fractions gave a reaction of identiy with one precipitin line of the microsomal fractions, that was not present in the mitochondrial, nuclear and cell sap fractions. Data from tests of protective activity activity obtained during a period of 3 years with whole homogenate and F and M fraction are also presented Protective activity against lethal challenge doses of trypomastigotes is strongly associated with the flagellar fraction.

Animals↗
PubMed1986

Immunoreactivity of fractionated antigens obtained from autoclaved extracts of an arthritogenic isolate of Erysipelothrix rhusiopathiae.

The immunoreactive antigens in heat-extracted (autoclaved) preparations of an arthritogenic strain of Erysipelothrix rhusiopathiae (isolate VRS 229, serotype 1a) have been identified by gel diffusion precipitin (GDP) tests and a novel application of the enzyme linked immunosorbent assay (ELISA) procedure. Antigens precipitated by ethanol treatment of autoclaved extracts of this strain were resolved into 4 major peaks (A,B,C and D) after gel permeation chromatography on Sephacryl S200. Peak A was confirmed as a protein peak (Lowry positive) which was excluded from the gel. This peak was identified to be ELISA-reactive when assayed with serum from pigs infected with other isolates corresponding to serotypes 1a, 1b and 2. However, it did not form precipitin lines in GDP tests. Peak B was Lowry-positive and also contained carbohydrates. It was not as reactive in ELISA tests but rapidly formed precipitin lines with serum from pigs infected with the homologous isolate, but only erratically with serums from pigs infected with other serotype 1a and 1b isolates, and not with serotype 2 isolates. Peaks C and D were high in carbohydrate and phosphate content respectively but were both non-reactive in GDP tests and only slightly so by ELISA. Since serotypes 1 and 2 are the most predominant among isolates from infected pigs it is likely that the commonly recognised A antigen is a useful ELISA reagent for the diagnosis of E. rhusiopathiae infection; B antigen on the other hand, would probably be of limited diagnostic value.

Animals↗
PubMed1979

The presence of precipitating antibodies in the sera of horses with chronic obstructive pulmonary disease (COPD).

The sera of horses affected and not affected with chronic obstructive pulmonary disease (COPD) were examined for precipitins to Micropolyspora faeni and Aspergillus fumigatus. Precipitins to both antigens were not restricted to COPD cases but occurred more frequently in animals affected with COPD. Many animals without detectable precipitins responded clinically to inhalation challenge with these antigens.

Animals↗
PubMedDate not supplied

Comparative evaluation of the Premier enzyme immunoassay, micro-immunodiffusion and complement fixation tests for the detection of Histoplasma capsulatum var. capsulatum antibodies.

A total of 178 sera, including 68 from proven cases of histoplasmosis (65 positive for the presence of Histoplasma capsulatum var. capsulatum antibodies and three positive for antigen), 93 from patients with suspected histoplasmosis but with no laboratory evidence of H. capsulatum var. capsulatum infection, 14 from humans with heterologous fungal and non-fungal infections and three from normal individuals, were tested for IgG H. capsulatum antibodies and M or M and H precipitins by enzyme immunoassay (EIA) (Meridian Diagnostics, Cincinnati, OH, USA) and microimmunodiffusion (MID) respectively. Sixty-three of the 68 histoplasmosis case sera demonstrated IgG antibody, and 65 of 68 demonstrated the presence of specific precipitins in the MID test. Nine positive case sera, when tested with the Laboratory Branch complement fixation (LBCF) test, reacted positively to whole yeast and histoplasmin antigens (titres 1:8 to 1:512). Three histoplasmosis case sera repeatedly tested negative for IgG, specific precipitins and complement-fixing antibodies, whereas they were positive for Histoplasma antigen. Eighteen of 95 sera from patients without evidence of histoplasmosis demonstrated IgG antibody in the EIA only. Among these positive sera, three out of three cases of aspergillosis and three out of five cases of blastomycosis were confirmed. Sera from HIV-infected and healthy individuals did not show IgG or M and/or H antibodies to H. capsulatum. Ninety-three sera were negative by both EIA and MID. The EIA for IgG was less sensitive (97%) than MID (100%). The specificity of EIA and MID was 84% and 100% respectively.

Antibodies, Fungal↗
PubMed1987

Antigenic characterization of Penicillium camemberti and related common cheese contaminants.

Twenty-four isolates of Penicillium (including a green-spored mutant from a French Brie cheese, Penicillium camemberti) with a proposed relationship to the white cheese mold P. camemberti were investigated by immunological procedures. These penicillia, which are representative of species that have caused considerable taxonomic confusion, had common micromorphology (terverticillate penicilli with rough and smooth stipes and smooth ellipsoidal to subglobose [(3 to 5) X 2 1/2 to 4 1/2 microns] conidia); growth rates; good growth on creatine sucrose agar, cheese, and other products with a high amount of protein and lipid as a primary habitat; production (with the exception of Penicillium solitum) of cyclopiazonic acid; and the ability to grow at low temperatures and water activities. The isolates that were investigated proved to be strictly antigenically related. Absorbed antiserum of the green-spored mutant of P. camemberti showed a specific precipitin band when tested by immunodiffusion either with its homologous reference antigen or with the exoantigens obtained from different isolates. The precipitin band was not present in any P. camemberti starter culture but in many unwanted cheese contaminants. The precipitin band can be used in the purity control of P. camemberti starter culture spore preparations. Analysis of the exoantigens of all the cultures by reversed phase high-performance liquid chromatography allowed us to subdivide these penicillia into nine groups below the species level. The results indicate that P. commune Thom is the wild-type ancestor of P. camemberti.

Antigens, Bacterial↗
PubMed1972

Differentiation between herpes simplex virus type 1 and type 2 strains by immunoelectroosmophoresis.

A method has been elaborated to differentiate between herpes simplex type 1 and type 2 viruses by immunoelectroosmophoresis. With rabbit immune sera cross-absorbed with heterologous virus antigen, a distinct difference was shown between the two virus types. Herpes simplex type 1 virus tested against cross-absorbed type 1 antiserum gave two precipitin lines. Herpes simplex type 2 virus gave one precipitin line when tested against cross-absorbed homologous serum. When the viral antigens were tested against cross-absorbed heterologous immune sera, no or only very weak precipitin reactions were observed. The test is easy and rapid, requires relatively small quantities of antigen and antibody, and is suitable for typing of herpes simplex virus in diagnostic routine work.

Absorption↗
PubMed1974

Identification of group B streptococci by immunofluorescence staining.

Gamma globulin fractions of rabbit antisera prepared with whole cell vaccines of group B types Ia, Ib, II, and III and labeled with fluorescein isothiocyanate stained group B streptococci type specifically. Type Ic cells, which contain the Ia polysaccharide antigen of type Ia and the Ic protein antigen of type Ib, were specifically stained by both Ia and Ib conjugates. A group B conjugate pool (B pool) that contained one conjugate specific for each group B type at its predetermined titer gave positive fluorescent-antibody (FA) reactions (4+ intensity) with group B stock strains and negative FA reactions (less than 2+ intensity) with stock strains of streptococcal groups A, C through H, and K through U, viridans streptococci, Streptococcus pneumoniae, Staphylococcus aureus, Neisseria gonorrhoeae, and representative Enterobacteriaceae. Examination of 883 clinical isolates submitted to the Streptococcus Laboratory (Center for Disease Control, Atlanta, Ga.) for identification revealed a 99.1% agreement between FA and culture-precipitin methods. All 305 group B streptococci identified by culture-precipitin and six nonhemolytic group B streptococci missed initially by culture tests were identified correctly by FA. Results of cultural and FA methods in a double-blind study of 99 vaginal swabs agreed on 96 of 99 strains. Three nonhemolytic group B streptococci were identified first by FA and later confirmed by culture-precipitin tests.

Cross Reactions↗
PubMed1975

Comparative antigenic analysis of pathogenic and free-living Naegleria species by the gel diffusion and immunoelectrophoresis techniques.

Antigens prepared from each of five strains (CA, CJ, HB-1, HB-3, and TY) of pathogenic Naegleria and the EG strain of nonpathogenic Naegleria gruberi were compared by the gel diffusion and immunoelectrophoresis techniques. Axenically grown amoebae were used as sources of antigens. Antisera were produced in individual rabbits against three strains (CA, CJ, and HB-1) of pathogenic Naegleria and the EG strain of N. gruberi. In the gel diffusion experiment each of the six antigens was reacted with each of the four antisera in agar gel. The results of these experiments revealed that the antigens of N. gruberi reacted strongly with the homologous antiserum but minimally with each of the three heterologous antisera. The antigens of all five pathogenic strains reacted extensively with the anti-CA, anti-CJ, and anti-HB-1 sera and moderately with the anti-EG serum. In the immunoelectrophoresis test each of the six antigens was separated electrophoretically in agar gel and reacted with each of the four antisera. The EG strain reacted extensively with its homologous antiserum and produced multiple precipitin arcs; it reacted minimally with anti-CA, anti-CJ, and anti-HB-1 sera and produced only three arcs. The antigens of all five strains of Naegleria fowleri reacted very strongly with anti-CA, anti-CJ, and anti-HB-1 sera and produced multiple precipitin arcs. They, however, reacted variably with the anti-EG serum and produced three to six precipitin arcs. Comparative immunoelectrophoretic analysis carried out on the CA and HB-1 strains revealed the antigenic identity of these two strains. Based on these results, together with those from the reciprocal absorption experiments, it was concluded that (i) the pathogenic strains of Naegleria, though they shared three to six common antigens with N. gruberi, were nevertheless distinct from it, and (ii) the five pathogenic strains were antigenically close and belonged in the same species. Antigens of Acanthamoeba castellanii, A. culbertsoni, and Entamoeba histolytica were also reacted with the four anti-Naegleria sera in gel diffusion experiments. Results of these tests indicate that these three organisms are antigenically distinct from Naegleria.

Absorption↗