scholarly journals THE PNEUMOCOCCAL CAPSULAR SWELLING REACTION, STUDIED WITH THE AID OF THE ELECTRON MICROSCOPE

1943 ◽  
Vol 78 (5) ◽  
pp. 327-332 ◽  
Author(s):  
Stuart Mudd ◽  
Ferdinand Heinmets ◽  
Thomas F. Anderson
Keyword(s):  
Capsular Polysaccharide ◽  
Specific Antigen ◽  
Immune Serum ◽  
Rabbit Serum ◽  
Surface Deposit ◽  
Specific Serum ◽  
Antibody Complex ◽  
Wall Interaction ◽  
Antigen Antibody ◽  
Serum Components

Electron micrographs indicate, in harmony with previous findings, that the pneumococcal capsule is a gel of low density outside of and closely applied to the bacterial cell wall. Interaction with homologous immune rabbit serum greatly increases the thickness and density of this capsular gel; the increase in thickness of the specifically swollen pneumococcal capsule may exceed by 25-fold the thickness of the surface deposit caused by rabbit immune serum on the cell walls and flagella of homologous non-capsulated bacteria. Conclusions drawn from these and earlier data are that homologous immune serum permeates the pneumococcal capsular gel; the specific antibody combines with the capsular polysaccharide; non-specific serum components are secondarily adsorbed to or combined with the specific antigen-antibody complex. The relatively low antibacterial titers characteristic of pneumococcal antisera can be explained in part by the permeation of the capsule by antiserum, in part by the high combining capacity of pneumococcal carbohydrate for antibody (17).

STUDIES ON A THYROID STIMULATING FACTOR IN URINARY CHORIONIC GONADOTROPHIN PREPARATIONS

1967 ◽  
Vol 55 (4) ◽  
pp. 587-599 ◽  
Author(s):  
A. Burger ◽  
R. Kunz
Keyword(s):  
Biological Response ◽  
Chorionic Gonadotrophin ◽  
Rabbit Serum ◽  
Soluble Antigen ◽  
Globulin Fraction ◽  
Human Pituitary ◽  
Antibody Complex ◽  
Antigen Antibody ◽  
Stimulating Factor ◽  
Immune Rabbit

ABSTRACT Thyroid stimulating activity was demonstrated in human urinary chorionic gonadotrophin preparations (HCG) by the method of McKenzie (1958). The biological response of the material was similar to that of bovine pituitary thyrotrophin (TSH), but no neutralization of the activity occurred with antibodies against human pituitary TSH and, even more interesting, with antibodies against human urinary chorionic gonadotrophin preparations. The latter antibodies perfectly neutralized human pituitary TSH. The Gamma-G-globulins precipitated from a mixture of HCG and anti-HCG contained biological activity whereas no activity was recovered in the Gamma-G-globulin fraction when HCG was mixed with non immune rabbit serum. This may indicate the presence of a soluble antigen-antibody complex.

scholarly journals THE PROTECTIVE ACTION OF TYPE I ANTIPNEUMOCOCCUS SERUM IN MICE

1936 ◽  
Vol 64 (3) ◽  
pp. 377-383 ◽  
Author(s):  
Kenneth Goodner ◽  
Frank L. Horsfall
Keyword(s):  
Selective Adsorption ◽  
Protective Action ◽  
Horse Serum ◽  
Rabbit Serum ◽  
Type I ◽  
Antibody Complex ◽  
Antigen Antibody

1. The addition of small amounts of cholesterol and of cephalin reduces markedly the protective action of antipneumococcus horse serum. 2. These lipids do not affect the protective action of antipneumococcus rabbit serum. 3. These findings may be explained (a)by the selective adsorption of lipid on the antigen-antibody complex, and (b) by certain lipid antagonisms. 4. The failure of large amounts of immune horse serum to protect mice against pneumococcus infection is explicable on the basis of selective participation of lipids dependent upon the species from which the antibody is derived. 5. The lipids modify the results of protection tests only through participation in the process of specific sensitization.

scholarly journals PROPERTIES OF THE TYPE SPECIFIC PROTEINS OF ANTIPNEUMOCOCCUS SERA

1937 ◽  
Vol 66 (4) ◽  
pp. 425-435 ◽  
Author(s):  
Kenneth Goodner ◽  
Frank L. Horsfall
Keyword(s):  
Capsular Polysaccharide ◽  
Horse Serum ◽  
Total Content ◽  
Immune Serum ◽  
Rabbit Serum ◽  
Antibody Activity ◽  
Subsequent Paper ◽  
Type I ◽  
Protective Capacity ◽  
Precipitable Protein

The generally held view has been that in any immune serum only a single antibody would be induced by and react with a single antigen. Were this true the various manifestations of antibody activity should show a quantitative parallelism. It has already been shown (1), however, that with antipneumococcus horse serum the mouse protective potency does not parallel the maximum amount of specifically precipitable protein except within certain well defined groups of antisera. The simplest explanation of this situation is that different horses form antibodies differing in specific protective capacity, but from our studies it seems probable that in any immune serum there may occur a mixture of antibodies which, while directed against the same antigen, possess different protective capacities, different avidities, etc. It would now appear that this latter hypothesis is the more tenable since the experiments here reported indicate the existence of antibodies of various protective potencies in horse antisera. It would not be unreasonable to hold that the antibodies of a single serum represent a series of substances with varying properties. On the basis of the present immunological fractionation experiments, the following deductions seem permissible. 1. Antipneumococcus horse sera must contain at least three, possibly many, antibody substances which react with the capsular polysaccharide. These are: (a) A substance which precipitates upon the addition of a relatively small amount of polysaccharide. This antibody possesses a low protective potency. (b) A substance which is precipitated with intermediate amounts of polysaccharide and which possesses an extremely high protective value. (c) A third substance which is precipitated only with the addition of relatively large amounts of polysaccharide. The protective value of this antibody is very low It may represent a degraded form. 2. With antipneumococcus rabbit serum the situation is somewhat simpler. This is in accord with the fact that with Type I antipneumococcus sera from this species there is a direct proportionality between the amount of specifically precipitable protein and the protective potency of the serum (1). The results with antipneumococcus rabbit serum indicate the existence of at least two antibody substances: (a) An antibody with high protective value which makes up the greater proportion of the total content. (b) A second substance which is precipitated only upon the addition of relatively large amounts of capsular polysaccharide. The existence of this second antibody is not clearly demonstrated by the present findings but the lower protective ratios obtained as greater amounts of antibody are removed probably indicate its existence. This may also represent degraded material. The observations on the antibodies of both horse and rabbit antisera will be supported by experiments with immunochemical fractionation which will be reported in a subsequent paper.

scholarly journals Immunity to the group B streptococci: interaction of serum and macrophages with types Ia, Ib, and Ic.

1976 ◽  
Vol 143 (5) ◽  
pp. 1186-1198 ◽  
Author(s):  
B F Anthony
Keyword(s):  
Group B Streptococcus ◽  
Immune Serum ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Group B Streptococci ◽  
Opsonic Activity ◽  
Heat Stable ◽  
Group B ◽  
Antigen Antibody

The opsonization and phagocytosis of group B streptococci of types Ia, Ib, and Ic were studied in vitro by measuring the uptake of radioactivity by coverslip cultures of rabbit alevolar macrophages during incubation with radiolabeled, nonviable bacteria which had been exposed to rabbit serum. The uptake of counts per minute was quantitative, reproducible, and reversibly inhibited by cold, indicating that it was largely a measurement of phagocytic ingestion rather than of attachment of bacteria-immunoglobulin complexes to macrophage membranes. Moreover, suspended macrophages killed approximately 90% of viable streptococci in the presence of specific antiserum. The opsonic activity of immune serum was heat stable, and phagocytosis of streptococci was insignificant after incubation with normal serum and antiserum to some heterologous group B streptococci. By absorption studies, it was possible to identify the effect of antibodies to specific bacterial antigens. Phagocytosis of streptococci containing the corresponding antigens was maximal after opsonization with homologous or heterologous sera containing antibody to IaCHO, IbCHO, or Ibc protein. Phagocytosis of all three serotypes was intermediate when opsonization could be attributed to anti-IabcCHO. The opsonization of a specific group B streptococcus is complex and may involve two or more antigen-antibody systems.

scholarly journals Identification of the Chromosomal Region Essential for Serovar-Specific Antigen and Virulence of Serovar 1 and 2 Strains ofErysipelothrix rhusiopathiae

2018 ◽  
Vol 86 (9) ◽  
Author(s):  
Yohsuke Ogawa ◽  
Kazumasa Shiraiwa ◽  
Sayaka Nishikawa ◽  
Masahiro Eguchi ◽  
Yoshihiro Shimoji
Keyword(s):  
Capsular Polysaccharide ◽  
Chromosomal Region ◽  
Specific Antigen ◽  
Gene Organization ◽  
Rabbit Serum ◽  
Erysipelothrix Rhusiopathiae ◽  
Functional Connection ◽  
Content Type ◽  
Antigenic Reactivity ◽  
Specific Rabbit

ABSTRACTErysipelothrix rhusiopathiaecauses swine erysipelas, an infection characterized by acute septicemia or chronic endocarditis and polyarthritis. Among 17E. rhusiopathiaeserovars, determined based on heat-stable peptidoglycan antigens, serovars 1 and 2 are most commonly associated with the disease; however, the molecular basis for the association between these serovars and virulence is unknown. To search for the genetic region defining serovar 1a (Fujisawa) strain antigenicity, we examined the 15-kb chromosomal region encompassing a putative pathway for polysaccharide biosynthesis, which was previously identified in theE. rhusiopathiaeFujisawa strain. Six transposon mutants of Fujisawa strain possessing a mutation in this region lost antigenic reactivity with serovar 1a-specific rabbit serum. Sequence analysis of this region in wild-type strains of serovars 1a, 1b, and 2 and serovar N, which lacks serovar-specific antigens, revealed that gene organization was similar among the strains and that serovar 2 strains showed variation. Serovar N strains displayed the same gene organization as the serovar 1a, 1b, or 2 strain and possessed certain mutations in this region. In two of the analyzed serovar N strains, restoration of the mutations via complementation with sequences derived from serovar 1a and 2 strains recovered antigenic reactivity with 1a- and 2-specific rabbit serum, respectively. Several gene mutations in this region resulted in altered capsule expression and attenuation of virulence in mice. These results indicate a functional connection between the biosynthetic pathways for the capsular polysaccharide and peptidoglycan antigens used for serotyping, which may explain variation in virulence among strains of different serovars.

scholarly journals DELAYED HYPERSENSITIVITY

1958 ◽  
Vol 108 (6) ◽  
pp. 891-904 ◽  
Author(s):  
Jonathan W. Uhr ◽  
A. M. Pappenheimer ◽  
Keyword(s):  
Guinea Pigs ◽  
Single Injection ◽  
Skin Testing ◽  
Specific Antigen ◽  
Delayed Hypersensitivity ◽  
Skin Reactions ◽  
Antibody Complex ◽  
Antigen Antibody ◽  
Free Antigen ◽  
Circulating Antibody

Guinea pigs rendered hypersensitive (delayed-type) to protein antigen can be completely and specifically desensitized by a single injection containing a sufficient amount of the corresponding antigen. Although 1 to 2 mg. of specific antigen are required for complete desensitization, as little as 20 µg. suffices to decrease the size of specific skin reactions in sensitized animals. The duration of non-reactivity lengthens as the amount of antigen in the desensitizing injection is increased, but skin reactivity eventually returns and is accompanied by the appearance of excess circulating antibody. Desensitization can be accomplished with the antigen-antibody complex as well as by "free" antigen. The appearance of delayed skin reactions can be prevented in fully sensitized animals by intravenous desensitization 2 or more hours after intradermal challenge or by simply skin testing with a desensitizing dose of specific antigen. Injection of a desensitizing dose of antigen into specifically sensitized animals also results in a transient anergic state, the implications of which are discussed.

Visualization of Antibody Transport in Rat Visceral Yolk-Sac Placenta

1982 ◽  
Vol 40 ◽  
pp. 246-247
Author(s):  
William P. Jollie
Keyword(s):  
Phosphate Buffer ◽  
Yolk Sac ◽  
Female Rats ◽  
Thin Sections ◽  
Visceral Yolk Sac ◽  
Antibody Complex ◽  
Cytochemical Reaction ◽  
Hind Foot ◽  
Antigen Antibody ◽  
Yolk Sac Placenta

A technique has been developed for visualizing antibody against horseradish peroxidase (HRP) in rat visceral yolk sac, the placental membrane across which passive immunity previously has been shown to be transferred from mother to young just prior to birth. Female rats were immunized by injecting both hind foot pads with 1 mg HRP emulsified in complete Freund's adjuvant. They were given a booster of 0.5mg HRP in 0.1 ml normal saline i.v. after one week, then bred and autopsied at selected stages of pregnancy, viz., 12, 1 7 and 22 days post coitum, receiving a second booster, injected as above, five days before autopsy. Yolk sacs were removed surgically and fixed immediately in 2% paraformaldehye, 1% glutaraldehye in 0.1 M phosphate buffer with 0.01% CaCl2 at pH 7.4, room temperature, for 3 hr, rinsed 3X in 0.1 M phosphate buffer plus 5% sucrose, then exposed to 1 mg HRP in 1 ml 0.1 M phosphate buffer at pH 7.4 for 1 hr. They were refixed in aldehydes, as above, for 1 5 min (to assure binding of antigen-antibody complex). Following buffer washes, the tissues were incubated in 3 mg diaminobenzidine tetrahydrochloride and 0.01% H2O2 in 0.05 M Tris-HCl buffer for 30 min. After brief buffer washes, they were postfixed in 2% OsO4. in phosphate buffer at pH 7.4, 4°C for 2 hr, dehydrated through a graded series of ethanols, and embedded in Durcupan. Thin sections were observed and photographed without contrast-enhancement with heavy metals. Cytochemical reaction product marked the site of HRP (i.e., antigen) which, in turn, was present only where it was bound with anti-HRP antibody.

INHIBITION OF LIPOLYTIC ACTIVITY OF SYNTHETIC β1–24 AND β1–39 CORTICOTROPHIN BY ANTI-ACTH ANTISERUM

1966 ◽  
Vol 51 (1) ◽  
pp. 88-94 ◽  
Author(s):  
A. Villanueva ◽  
S. J. H. Ashcroft ◽  
J. P. Felber
Keyword(s):  
Guinea Pig ◽  
Lipolytic Activity ◽  
Peptide Hormones ◽  
Fat Pad ◽  
Double Antibody ◽  
Epididymal Fat ◽  
Antibody Complex ◽  
Radio Immunoassay ◽  
Antigen Antibody

ABSTRACT The synthetic ACTH peptides β1–39 and β1–24 stimulated lipolysis as determined by the rat epididymal fat pad in vitro. The stimulating effect of these peptides was diminished by prior incubation of the peptides with antibodies produced by the guinea-pig against ACTH. The stimulating effect of these hormones was also diminished by the double antibody system used in the radio-immunoassay of ACTH and other peptide hormones, in which incubation with antiserum is followed by precipitation of the antigen-antibody complex by rabbit anti-guinea-pig-γ-globulin.

IDENTIFICATION OF LATS AS AN ANTIGEN-ANTIBODY COMPLEX

1973 ◽  
Vol 71 (4_Suppl) ◽  
pp. S11
Author(s):  
K. Schemmel ◽  
L. Weisbecker ◽  
H. Norden ◽  
V. Mokmol ◽  
V. Becker ◽  
...  
Keyword(s):  
Antibody Complex ◽  
Antigen Antibody
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