scholarly journals CHEMICAL STUDIES ON BACTERIAL AGGLUTINATION

1945 ◽  
Vol 81 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Elvin A. Kabat ◽  
C. Phillip Miller ◽  
Hilda Kaiser ◽  
Alice Z. Foster
Keyword(s):  
Specific Antibody ◽  
Quantitative Method ◽  
Type I ◽  
Type Ii ◽  
Subsequent Infection ◽  
Protective Antibody ◽  
Specific Polysaccharide ◽  
Chemical Studies ◽  
Bacterial Agglutination

1. The quantitative method for the estimation of agglutinins has been applied to antimeningococcal horse, rabbit, and chicken sera and to the sera of humans convalescing from meningococcus meningitis. The type-specific and group-specific agglutinin N can be measured, using homologous and heterologous suspensions of meningococci. 2. Type I horse, rabbit, and chicken antimeningococcal sera contain considerable amounts of antibody which cannot be removed either by Type II meningococcus suspension or by preparations of the Type I specific polysaccharide. This residual type-specific antibody has marked potency in protecting mice against subsequent infection with meningococci. 3. Most human convalescent sera contain group-specific antibody. Small amounts of protective antibody and of antipolysaccharide are also formed. 4. Type I antisera absorbed with Type I polysaccharide and with Type II meningococci could be used as a guide in the purification of this new antigen.

scholarly journals CHEMICAL STUDIES ON BACTERIAL AGGLUTINATION

1936 ◽  
Vol 63 (5) ◽  
pp. 737-744 ◽  
Author(s):  
Michael Heidelberger ◽  
Elvin A. Kabat
Keyword(s):  
Specific Antibody ◽  
Horse Serum ◽  
The Other ◽  
Type I ◽  
Specific Polysaccharide ◽  
Chemical Studies ◽  
The Absolute ◽  
Bacterial Agglutination

1. The absolute, quantitative agglutinin method has been used for the determination of the presence or absence of small amounts of specific polysaccharide in pneumococcus variants. 2. A technique is described for the removal of group specific antibody from antipneumococcus horse serum. 3. The type specific anticarbohydrate agglutinin and precipitin are not only present in identical amounts in Type I antipneumococcus horse serum, but a reduction in one is also accompanied by a quantitatively identical reduction in the other, providing evidence for their actual identity. In purified antibody solutions somewhat more agglutinin than precipitin is found, possibly owing to alteration of a portion of the antibody in the process of purification.

scholarly journals SPECIFIC ANTIBODY RESPONSE OF HUMAN SUBJECTS TO INTRACUTANEOUS INJECTION OF PNEUMOCOCCUS PRODUCTS

1932 ◽  
Vol 55 (6) ◽  
pp. 853-865 ◽  
Author(s):  
Maxwell Finland ◽  
W. D. Sutliff
Keyword(s):  
Human Subjects ◽  
Type I ◽  
Type Ii ◽  
Specific Antibody Response ◽  
Specific Antibodies ◽  
Virulent Strains ◽  
Before And After ◽  
Specific Polysaccharide ◽  
Protective Antibodies ◽  
Intracutaneous Injection

The blood of 63 human subjects selected because of the absence of recent infections, was studied for its content of specific antibodies against virulent strains of Types I, II, and III pneumococci before and after intracutaneous injections of minute amounts of pneumococcus products. The simultaneous injection of the specific polysaccharides of all three types of pneumococci and of proteins and autolysates derived from Types I and II pneumococci was followed by the appearance or increase of pneumococcidal power in the whole defibrinated blood and, in most instances, by the appearance of mouse-protective antibodies and agglutinins for one or more types. A single intracutaneous injection of 0.01 mg. of the protein-free type-specific polysaccharide of either Type I, Type II, or Type III pneumococci or 4 similar daily injections was followed, in most of 29 subjects, by the appearance of antibodies against the homologous, but not against the heterologous type pneumococci. Some subjects showed a simultaneous lowering of a preexisting pneumococcidal power for heterologous or homologous types. A single intracutaneous injection of O.1 mg. of pneumococcus protein in 13 individuals was not followed by the appearance of specific antibodies to any appreciable degree. Single intracutaneous injections of small amounts of autolysates derived from virulent strains of Type I, II, or III pneumococci were followed in 11 subjects by a more or less general rise in the pneumococcidal power with the appearance of homologous type agglutinins and protective antibodies in about one-third of the subjects.

scholarly journals STUDIES ON PHOTO-OXIDATION OF ANTIGEN AND ANTIBODIES

1941 ◽  
Vol 73 (2) ◽  
pp. 223-242 ◽  
Author(s):  
Hans Smetana ◽  
David Shemin
Keyword(s):  
Specific Antibody ◽  
Horse Serum ◽  
Amino Nitrogen ◽  
Rabbit Serum ◽  
Type I ◽  
Egg Albumin ◽  
Photo Oxidation ◽  
Precipitin Reaction ◽  
Antigenic Properties ◽  
Chemical Studies

1. Quantitative precipitin studies indicate that progressive photo-oxidation progressively destroys the antigenic function of egg albumin. 2. Quantitative precipitin reactions of antisera (anti-egg albumin rabbit serum and antipneumococcus Type I horse serum) demonstrate that progressive photo-oxidation causes progressive lowering of the potency of the sera. 3. Quantitative precipitin reactions of the photo-oxidized globulin gamma fraction of anti-egg albumin rabbit serum and of Felton solution of antipneumococcus Type I horse serum show that these specific antibody fractions behave similarly to antibodies in whole sera. 4. Egg albumin whose precipitin reaction is destroyed by photo-oxidation no longer causes anaphylaxis in guinea pigs and does not produce precipitins in rabbits. 5. Chemical studies of progressively photo-oxidized egg albumin show a progressive destruction of tryptophane and histidine while tyrosine remains intact and cystine is reversibly oxidized. Sulfhydryl groups can no longer be demonstrated in photo-oxidized egg albumin whose antigenic characteristics are greatly weakened. 6. Similar studies on the globulin gamma fraction of anti-egg albumin rabbit serum and on Felton solution show no diminution of these amino acids in photo-oxidized material whose antigenic properties are destroyed. 7. The non-coagulable nitrogen and the amino nitrogen of egg albumin, antisera, and their specific antibody fractions show but an insignificant increase during photo-oxidation, indicating that the loss of the precipitin reaction is not due to splitting of the respective protein molecules. 8. Electrophoretic studies of egg albumin, antisera, and their specific antibody fractions show that photo-oxidation causes a marked alteration of the pattern of these substrates. 9. Photo-oxidation of proteins causes the formation of aggregates, indicating denaturation. 10. Hematoporphyrin migrates with the albumin fraction of unaltered as well as the photo-oxidized anti-egg albumin rabbit serum and pneumococcus Type I horse serum; in isolated proteins such as egg albumin, globulin gamma, or Felton solution, etc., the dye moves independently of the protein; after progressive photo-oxidation Hp becomes progressively fixed to the protein. Eosin behaves similarly to hematoporphyrin.

scholarly journals CRYSTALLINE PNEUMOCOCCUS ANTIBODY

1949 ◽  
Vol 32 (6) ◽  
pp. 705-724 ◽  
Author(s):  
John H. Northrop ◽  
Walther F. Goebel
Keyword(s):  
Ammonium Sulfate ◽  
Horse Serum ◽  
Insoluble Fraction ◽  
Rabbit Serum ◽  
Type I ◽  
Type Ii ◽  
Serum Globulin ◽  
Saturated Ammonium Sulfate ◽  
Diphtheria Antitoxin ◽  
Specific Polysaccharide

1. The immune precipitate formed by antipneumococcus horse serum and the specific polysaccharide is not hydrolyzed by trypsin as is the diphtheria toxin-antitoxin complex, and purified pneumococcus antibody cannot be isolated by the method used for the isolation and crystallization of diphtheria antitoxin. 2. Type I pneumococcus antibody, completely precipitable by Type I polysaccharide, may be obtained from immune horse serum globulin by precipitation of the inert proteins with acid potassium phthalate. 3. The antibody obtained in this way may be fractionated by precipitation with ammonium sulfate into three main parts. One is insoluble in neutral salts but soluble from pH 4.5 to 3.0 and from pH 9.5 to 10.5. This is the largest fraction. A second fraction is soluble in 0.05 to 0.2 saturated ammonium sulfate and the third fraction is soluble in 0.2 saturated ammonium sulfate and precipitated by 0.35 saturated ammonium sulfate. The second fraction can be further separated by precipitation with 0.17 saturated ammonium sulfate to yield a small amount of protein which is soluble in 0.17 saturated ammonium sulfate but insoluble in 0.25 saturated ammonium sulfate. This fraction crystallizes in poorly formed, rounded rosettes. 4. The crystallization does not improve the purity of the antibody and is accompanied by the formation of an insoluble protein as in the case of diphtheria antitoxin. 5. None of the fractions obtained is even approximately homogeneous as determined by solubility measurements. 6. Purified antibody has also been obtained by dissociating the antigen-antibody complex. 7. The protective value of the fractions is quite different; that of the dissociated antibody being the highest and that of the insoluble fraction, the lowest. 8. All the fractions are immunologically specific since they do not precipitate with Type II polysaccharide nor protect against Type II pneumococci. 9. All the fractions give a positive precipitin reaction with antihorse rabbit serum. The dissociated antibody gives the least reaction. 10. Comparison of the various fractions, either by their solubility in salt solution or through immunological reactions, indicates that there are a large number of proteins present in immune horse serum, all of which precipitate with the specific polysaccharide but which have very different protective values, different reactions with antihorse rabbit serum, and different solubility in salt solutions.

scholarly journals CHEMICAL STUDIES ON BACTERIAL AGGLUTINATION

1941 ◽  
Vol 74 (2) ◽  
pp. 105-114 ◽  
Author(s):  
Sverre D. Henriksen ◽  
Michael Heidelberger
Keyword(s):  
Specific Antibody ◽  
Experimental Conditions ◽  
Chemical Studies ◽  
Yield Values ◽  
Bacterial Agglutination

1. Application of the quantitative agglutination procedure to hemolytic streptococci and their antisera is shown to yield values indicative of the antibody content of the antisera in weight units. 2. Estimations are given of type-specific and group-specific antibody in a number of antisera. 3. An incomplete analysis is given of the antigenic components and antibodies involved in the agglutination. 4. Adaptation of the experimental conditions to a simple qualitative type determination of hemolytic streptococci is suggested.

scholarly journals THE EFFECT OF THE BACTERIOLYTIC ENZYME OF PNEUMOCOCCUS UPON THE ANTIGENICITY OF ENCAPSULATED PNEUMOCOCCI

1937 ◽  
Vol 66 (1) ◽  
pp. 113-123 ◽  
Author(s):  
René J. Dubos
Keyword(s):  
Capsular Polysaccharide ◽  
Specific Resistance ◽  
Bacterial Species ◽  
Antigenic Property ◽  
Type I ◽  
Subsequent Infection ◽  
Polysaccharide Antigen ◽  
Bacteriolytic Enzyme ◽  
Active Immunity ◽  
Specific Polysaccharide

1. Mice immunized with heat-killed cells of virulent pneumococci (Type I) which have been treated with active preparations of the bacteriolytic enzyme, develop a certain degree of type specific resistance to subsequent infection. This active immunity, however, appears to be due to the small amount of free acetyl polysaccharide present in the suspension of digested bacteria, and is always of a less pronounced degree than that obtained with intact heat-killed cells. 2. Virulent pneumococci killed by heat or iodine when subjected to the action of active preparations of the bacteriolytic enzyme lose the antigenic property of stimulating in rabbits the formation of precipitating antibodies for the type specific polysaccharide. 3. The enzyme prepared from S or R pneumococci, irrespective of type derivation, is equally effective against the capsular polysaccharide antigen of any specific type of this bacterial species. 4. The inactivation of the capsular polysaccharide antigen is observed when the cells are merely rendered Gram-negative, without being caused to undergo actual disintegration or lysis. 5. These observations emphasize the importance of minimizing the chances of alterations due to the action of cellular enzymes in the course of preparation of the cell suspension to be used as immunizing agents.

scholarly journals LOCAL SPECIFIC THERAPY OF EXPERIMENTAL PNEUMOCOCCAL MENINGITIS

1928 ◽  
Vol 47 (4) ◽  
pp. 515-530 ◽  
Author(s):  
Fred W. Stewart
Keyword(s):  
Blood Stream ◽  
Type I ◽  
Type Ii ◽  
Subsequent Infection ◽  
Luxuriant Growth ◽  
Established Disease ◽  
Brain Abscesses ◽  
Real Value ◽  
Serum Therapy ◽  
Experimental Pneumococcal Meningitis

1. With properly selected strains of Type II pneumococci, fatal meningitis may be produced by intrathecal infection in dogs. 2. The pathology of the disease differs from that produced by Type I pneumococci, at least with the strains employed. 3. Type II meningitis is characterized by early, very marked reactions, a very heavy fibrin exudation, and a tendency toward the rapid establishment of blocks. 4. Extreme vasodilatation and. hemorrhage are common. 5. The fibrinopurulent exudate tends to involve the walls and perivascular sheaths of deeply penetrating vessels, thereby causing thrombosis. 6. Thrombosis leads to foci of parenchymatous softening which, on subsequent infection, become brain abscesses. 7. The lateral venticles are a "point of election" for the luxuriant growth of pneumococci. Conversely there is evidence that Type II organisms tend somewhat to disappear from other regions, owing either to spontaneous phagocytosis or to filtration into the blood stream. The lateral ventricles, however, continually renew the supply. 8. Hydrocephalus occurs early—sometimes during the 2nd day of the disease. 9. Central myelitis is common and appears early in the disease. 10. Deep nerve cell lesions with necrosis and neuronophagia are encountered. Their pathology suggests a toxic source. 11. In most cases treatment has been impossible owing to severe early reactions, and only as a prophylactic has optochin-serum therapy any real value. It delays death, but has in no instance cured established disease in the dog. 12. Systemic generalization of Type II meningeal infection in the dog occurs, but it is rarely of sufficient extent to modify prognosis.

scholarly journals Comparative Analysis of the Mucosal Adjuvanticity of the Type II Heat-Labile Enterotoxins LT-IIa and LT-IIb

2000 ◽  
Vol 68 (1) ◽  
pp. 281-287 ◽  
Author(s):  
Michael Martin ◽  
Daniel J. Metzger ◽  
Suzanne M. Michalek ◽  
Terry D. Connell ◽  
Michael W. Russell
Keyword(s):  
Lymph Nodes ◽  
Specific Antibody ◽  
Antibody Responses ◽  
Interleukin 4 ◽  
Enzyme Linked Immunosorbent Assay ◽  
Antibody Activity ◽  
Type I ◽  
Type Ii ◽  
Cervical Lymph Nodes ◽  
Heat Labile

ABSTRACT Cholera toxin (CT) and the heat-labile enterotoxin ofEscherichia coli (LT-I) are members of the serogroup I heat-labile enterotoxins (HLT) and can serve as systemic and mucosal adjuvants. However, information is lacking with respect to the structurally related but antigenically distinct serogroup II HLT, LT-IIa and LT-IIb, which have different binding specificities for ganglioside receptors. The purpose of this study was to assess the effectiveness of LT-IIa and LT-IIb as mucosal adjuvants in comparison to the prototypical type I HLT, CT. BALB/c mice were immunized by the intranasal (i.n.) route with the surface protein adhesin AgI/II ofStreptococcus mutans alone or supplemented with an adjuvant amount of CT, LT-IIa, or LT-IIb. Antigen-specific antibody responses in saliva, vaginal wash, and plasma were assayed by enzyme-linked immunosorbent assay. Mice given AgI/II with LT-IIa or LT-IIb by the i.n. route had significantly higher mucosal and systemic antibody responses than mice immunized with AgI/II alone. Anti-AgI/II immunoglobulin A (IgA) antibody activity in saliva and vaginal secretions of mice given AgI/II with LT-IIa or LT-IIb was statistically similar in magnitude to that seen in mice given AgI/II and CT. LT-IIb significantly enhanced the number of AgI/II-specific antibody-secreting cells in the draining superficial cervical lymph nodes compared to LT-IIa and CT. LT-IIb and CT induced significantly higher plasma anti-AgI/II IgG titers compared to LT-IIa. When LT-IIb was used as adjuvant, the proportion of plasma IgG2a relative to IgG1 anti-AgI/II antibody was elevated in contrast to the predominance of IgG1 antibodies promoted by AgI/II alone or when CT or LT-IIa was used. In vitro stimulation of AgI/II-specific cells from the superficial lymph nodes and spleen revealed that LT-IIa and LT-IIb induced secretion of interleukin-4 and significantly higher levels of gamma interferon compared to CT. These results demonstrate that the type II HLT LT-IIa and LT-IIb exhibit potent and distinct adjuvant properties for stimulating immune responses to a noncoupled protein immunogen after mucosal immunization.

scholarly journals PREPARATION OF THE TYPE-SPECIFIC POLYSACCHARIDE OF THE TYPE I MENINGOCOCCUS AND A STUDY OF ITS EFFECTIVENESS AS AN ANTIGEN IN HUMAN BEINGS

1944 ◽  
Vol 80 (4) ◽  
pp. 299-307 ◽  
Author(s):  
Elvin A. Kabat ◽  
Hilda Kaiser ◽  
Helen Sikorski
Keyword(s):  
Type I ◽  
Human Beings ◽  
Reactive Material ◽  
Protective Antibody ◽  
Specific Polysaccharide

1. Methods for preparing small amounts of Type I meningococcal polysaccharide which are electrophoretically homogeneous and contain only traces of other immunologically reactive material are given. 2. These polysaccharides are very poor antigens in man but in a small number of instances definite amounts of precipitin and protective antibody were formed. 3. The significance of these findings is discussed.

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