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At least 19 recordsLinked to original sources
PubMed1955

The use of precipitin analysis in agar for the study of human streptococcal infections. I. Oudin technic.

Using a highly concentrated and partially purified streptolysin O preparation, migrating agar precipitins have been found in 94 of 143 human sera from patients with a variety of diseases. Most of those showing no bands, had very low antistreptolysin titers. A correlation was found between the migration rates of these bands and the antistreptolysin titer. A strong trend toward a straight line relationship was apparent when the ASO titers were plotted on a logarithmic scale. In addition, a roughly positive correlation was found between the intensity of these bands and the antistreptolysin O titers. The finding of high levels of antistreptolysin O activity and slowly migrating heavy bands in normal pooled human gamma globulin supported the above observations. Very similar results were obtained with rabbit and guinea pig sera after immunization with the streptolysin O concentrates. The data strongly indicate that antistreptolysin O activity in human sera is generally due to precipitating antibody, and that non-specific inhibitors are not usually involved, even with low titered sera. Rabbit and guinea pig antisera to the oxidized inactive and to the reduced active forms of streptolysin O showed no obvious differences. Attempts to demonstrate immunological differences between the two states of streptolysin were apparently complicated by proteolysis, due to contamination of the concentrates with proteinase precursor.

Agar↗
PubMed1955

The use of precipitin analysis in agar for the study of human streptococcal infections. II. Ouchterlony and Oakley technics.

It has been shown by agar precipitin tests (Ouchterlony and Oakley) that human sera may contain from 0 to 5 antibodies against antigens present in a partially purified streptolysin O preparation, and from 0 to 7 antibodies against antigens in a crude ammonium sulfate concentrate of the streptococcal culture supernate used. These antigens were prepared from a Group A hemolytic streptococcus (strain C203S). Strong evidence was presented suggesting that some of the bands seen with streptolysin O concentrate represented antibody reponses to streptococcal antigens heretofore undescribed. Tests were also carried out with other streptococcal antigens, including streptokinase-desoxyribonuclease mixture from Group C streptococci (varidase-Lederle), crystalline proteinase, proteinase precursor, C carbohydrate, and sonic vibrated streptococcal cell extracts (group A, C203S). Fewer bands were seen with these preparations, and with some they were quite uncommon. The observations indicated that the predominating antibody responses in human streptococcal infections were to extracellular products of the micro-organisms, and only very slightly and infrequently to intracellular antigens. The human sera studied included sera from patients with active or convalescent rheumatic fever, and non-rheumatic subjects suffering from a variety of illnesses. As was expected, the rheumatic subjects showed antibody responses to many more of the antigens present in these preparations than did the nonrheumatic group. Pooled normal human gamma globulin was found to contain many of the antibodies found in potent human sera. This finding confirmed the antigen-antibody nature of the bands seen with individual sera. The epidemiological significance of these findings with gamma, globulin was briefly discussed. It was found that rabbit, guinea pig, and human antibody precipitin bands join quite readily in the Ouchterlony tests. This finding adds another tool for the identification of the precipitin bands found with human sera. Evidence was obtained which indicated differing immunological specificities of two samples of streptococcal desoxyribonuclease, one from Group A, the other from a Group C streptococcus. The value of these technics as representing a new approach to the study of human infectious disease was discussed.

Agar↗
PubMed1958

Localization of streptococcal antigens in tissues. I. Histologic distribution and persistence of M protein, types 1, 5, 12, and 19 in the tissues of the mouse.

A method has been described for the detection of streptococcal antigens in tissues using the indirect immunofluorescent technique. This method has been applied to the histologic distribution in the mouse of M protein of types 1, 5, 12, and 19. Histologic localization of these M proteins was similar, and their rates of disappearance from the tissues were comparable. The major sites of deposition were the endocardium and adjacent subendocardium of the heart, alveolar walls of the lung, glomerular tufts of the kidney, and reticulo-endothelial cells of liver, spleen, lymph nodes, and adrenal gland. M protein was distributed in considerably lesser concentration in capillary endothelium and connective tissue sites in myocardium, kidney, skin, and gastrointestinal tract. Traces were also present in adrenal cortical cells. It was observed only rarely in cell nuclei. After injection of 0.5 mg. M protein fraction, the concentration of antigen diminished to undetectable levels in all organ sites by 4 days, except in the renal glomerulus, where traces were visible at 8 days. In mice injected with streptococcal culture intraperitoneally, M protein was detected at sites of focal abscesses in liver and spleen, and on the serous surfaces of these organs. The histologic distribution of M protein is compared with that described previously for pneumococcal polysaccharide and animal protein. Differences in the extent of distribution and in the characteristics of antigen deposition are pointed out.

Animals↗
PubMed1958

The use of precipitin analysis in agar for the study of human streptococcal infections. III. The purification of some of the antigens detected by these methods.

As evidenced by precipitin analysis with pooled human gamma globulin, at least 12 distinct antigens were produced in cultures by one strain of Group A streptococcus (C203S). It was suggested on this basis, that these antigens were produced in vivo during human infections. By the combined use of continuous flow electrophoresis on paper curtains, and column chromatography with calcium phosphate gels, five of these have been isolated in a probable high state of purity. One of the components was obtained from culture filtrates of a Group C streptococcal strain. Three of the purified antigens have been tentatively identified as streptolysin "O", diphosphopyridinenucleotidase, and proteinase precursor. The latter could be very readily crystallized, and appears "identical" with that described by Elliott. The DPNase was of extremely high potency, 1 mg. being capable of destroying 12.6 gm. of DPN in 7(1/2) minutes at 37 degrees C. The identity of the other two components is uncertain as yet. They are distinct from each other and the above products immunologically, and are not related to the "C" carbohydrate. The applicability of these methods for the analysis of infectious diseases generally was discussed.

Agar↗
PubMed1959

Persistence of type-specific antibodies in man following infection with group A streptococci.

Whole blood or sera were collected from individuals who had had infections with Group A streptococci of known serological type as long ago as 10 to 32 years. Most of these patients had not been treated with chemotherapeutic drugs. By means of bactericidal tests with all these sera, and mouse protection tests with some, type-specific antibodies could be demonstrated in at least half of them after a lapse of many years, the longest interval being 32 years. Two biological methods for estimating the amount of M antigen produced by Group A streptococci are described. By selecting strains for use by these methods, optimal proportions of M antigen and antibody could be employed in the tests and small amounts of antibody were, therefore, demonstrable. The assay methods for M antigen are also of value for other experimental purposes.

Animals↗
PubMed1959

Evaluation of the "long chain reaction" as a means for detecting type-specific antibody to group a streptococci in human sera.

Certain strains of Group A streptococci showed striking increase in chain length when grown in liquid media to which was added human sera that contained antibody to M protein of homologous type. This "long chain reaction" was shown to be a highly specific and sensitive biological test for human type-specific antibody and correlated closely with the classical bactericidal test. Patients infected with Type 12 or Type 3 Group A streptococci showed the appearance of anti-M antibody in their sera by both methods at similar intervals during convalescence. Of 217 sera studied in these patients the two tests showed agreement in all but 11 specimens. Of 99 patients who were bled serially following Type 12 or Type 3 infections, and whose sera were tested by both methods, there was close agreement, the bactericidal test being only slightly more sensitive. The advantages and limitations of this new biological test for human type-specific immunity are discussed.

Antibodies↗
PubMed1960

Host-parasite factors in group A streptococcal infections. Pyrogenic and other effects of immunologic distinct exotoxins related to scarlet fever toxins.

The factors present in streptococcal lesion extracts (SLE) which enhanced the lethal and tissue-damaging properties of Gram-negative bacterial endotoxins and streptolysin O were identified with the scarlet fever group of toxins. Toxic manifestations attributed to this group of toxins included lethality, cardiotoxic and other tissue damage, enhancement of toxicity, and pyrogenicity. Of these, the measurement of febrile response in American Dutch rabbits was the most useful parameter of toxicity. In rabbits, repeated daily intravenous injections of 0.125 Lf of a purified erythrogenic toxin immunizes specifically against the pyrogenic activity; this technique was used to type the toxins and to distinguish them from exogenous and endogenous pyrogens; non-specific pyrogens, such as streptococcal endotoxin, were not found in SLE. All types of the Lancefield Group A streptococci tested produced one or or more immunologically distinct toxins in vivo in contrast to Groups B and C which did not produce them; toxins A and B, previously distinguished by neutralization of rash-inducing activity in the skin, were produced in vivo. The A toxin was the most common, as indicated by its presence in extracts prepared with Types 28, 12, 17, and 10 (NY-5); B toxin was found in 10 (NY-5) and 19. A new toxin, designated C, was obtained from a Type 18. In American Dutch rabbits, purified toxin at a concentration of 15 Lf (900,000 STD) neither gave a Dick test nor prepared the skin for the local Shwartzman reaction; by this route, however, in contrast to classical endotoxins, they enhance the lethal and tissue-damaging properties of sublethal doses of these and other toxins. These properties of the immunologic distinct exotoxins as demonstrated in American Dutch rabbits suggest by analogy their importance in the pathogenesis of streptococcal disease in man. Evidence that might implicate them in sequelae, in addition to scarlet fever, is discussed.

Animals↗
PubMed1961

The analysis of streptococcal infections. VI. Immunoelectrophoretic observations on extracellular antigens detectable with human antibodies.

It has been found by immunoelectrophoresis, that Group A streptococci release at least 20 distinct extracellular antigens in human tissues, as judged by naturally occurring antibodies present in normal pooled human gamma globulin. Several of these precipitin arcs have been identified with streptococcal antigens previously purified by electrophoresis and chromatography. Human gamma globulin, as well as several rheumatic fever sera, were shown to be remarkably potent in antistreptococcal antibodies, when compared to four horse antibody concentrates obtained by hyperimmunization with several streptococcal filtrates. A Group C streptococcal culture concentrate revealed 8 or 9 antigens for which corresponding antibodies were present in human gamma globulin.

Animals↗