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K Eichmann

Publications and source records attributed to K Eichmann.

At least 163 records · Page 9Linked to original sources
PubMed1973

Idiotype expression and the inheritance of mouse antibody clones.

The inheritance of idiotypes was investigated using idiotypic antisera against two monoclonal antibodies to streptococcal carbohydrates derived from A/J mice. Each of the two idiotypes was characterized by a special frequency of expression. One of the idiotypes was expressed in more than 80% of A/J mice, the other in less than 20%. The idiotypes of both antibodies were strain specific and were transmitted to (A/J x BALB/cJ)F(1) hybrid mice. Furthermore, both idiotypes remained associated with the A/J heavy chain C region allotype in (A/J x BALB/cJ)F(1) hybrid mice. The results suggest that idiotypes are specified by allelic V genes, and that the heavy chain idiotype locus is linked to the heavy chain allotype locus.

Alleles↗
PubMed1971

The inheritance of individual antigenic specificities of rabbit antibodies to streptococcal carbohydrates.

The inheritance of individual antigenic specificities (IAS) of rabbit antibodies to the Group C streptococcal carbohydrate was demonstrated in a selectively bred rabbit family. The IAS of the antibodies from 3 proband rabbits were also observed in the Group C antibodies in as many as 7 out of 42 related rabbits, but in none of the Group C antibodies from 48 unrelated rabbits, Immunodiffusion analyses and quantitative radioprecipitin experiments revealed that this cross-specificity may be either partial or complete. Quantitative inhibition of the precipitin reaction between the proband antibody and its antiserum by preimmune IgG revealed 30-fold differences in the proportion of molecules with cross-specificity for the proband antibody. This proportion is higher in the preimmune IgG of the proband rabbit and of those relatives which produced cross-precipitating antibodies than it is in the IgG of rabbits which had the same group a allotype, but did not produce cross-precipitating antibodies. The proportion is much lower in the IgG of rabbits with a group a allotype different from that of the proband antibody. These data suggest that serologically detected individual antigenic specificities are inherited markers of immunoglobulins.

Amino Acid Sequence↗
PubMed1971

Influence of genetic factors on the magnitude and the heterogeneity of the immune response in the rabbit.

Selective breeding of rabbits immunized with Group C and Group A streptococcal vaccines was employed to reveal genetic influences on the magnitude and on the restriction in heterogeneity of the immune response to the group-specific carbohydrates. After two generations of selective breeding, complete segregation was achieved between a high-response population (>18 mg precipitins/ml serum, average 33 mg/ml) and a low-response population (<13 mg precipitins/ml serum, average 7.5 mg/ml) to Group C carbohydrate. This suggests that a limited number of genes controls the magnitude of the immune response to this antigen. Selective breeding of rabbits which were representative of heterogeneous, restricted, and monoclonal responses revealed that the degree of antibody heterogeneity in the parental rabbits is reflected in the offspring. More than 95% of the offspring derived from rabbits which had a heterogeneous immune response developed heterogeneous antibodies. 33% of the offspring derived from rabbits which had restricted and monoclonal immune responses developed monoclonal antibodies. This suggests that the degree of heterogeneity of the antibody response to the streptococcal carbohydrates is under genetic control. The degree of heterogeneity and the magnitude of the immune response appear to be independent variables.

Animals↗
PubMed1971

Relationships between relative binding affinity and electrophoretic behavior of rabbit antibodies to streptococcal carbohydrates.

After repeated intravenous injections with Group C streptococcal vaccine, most rabbit antisera were shown to contain one or more IgG antibody components, as revealed by microzone electrophoresis. A procedure for the fractionation of multiple IgG antibody components from such streptococcal antisera is described. Separation is achieved on the basis of differences in relative binding affinities of the antibody components to immunoabsorbent columns. The evidence suggests that the electrophoretic mobility, and thus the net charge of an antibody, bears a reciprocal relationship to its binding affinity for the streptococcal Group C antigens. Furthermore, the relative binding affinity affords another means to assess the functional homogeneity of streptococcal antibodies. A possible relationship between light chain variable-region subclasses and binding affinities of streptococcal antibodies is discussed.

Adsorption↗
PubMed1970

The emergence of antibodies with either identical or unrelated individual antigenic specificity during repeated immunizations with streptococcal vaccines.

Electrophoretically monodisperse antibody components in rabbit antisera to the carbohydrates of the Groups A and C streptococci have been examined for their individual antigenic specificity. In these antibody components which were isolated by preparative electrophoresis, individual antigenic specificity was confined to the specific antibody and was absent in the nonantibody gamma-globulin. Radioprecipitation experiments and the use of immune absorbent columns constructed from goat anti-antisera, which had been absorbed with fraction II, revealed that all the specific antibody in an electrophoretically monodisperse component was reactive with the homologous anti-antibody. Antibodies with either identical or distinct individual antigenic specificities may occur in the same rabbit with repeated immunizations. Antibodies with identical antigenic specificity had identical electrophoretic mobility, whereas antibodies with unrelated antigenic specificities had distinct electrophoretic mobilities. In the interval between immunizations, if antibody to the carbohydrate antigen was absent, there was no detectable antibody with individual antigenic specificity.

Animals↗
PubMed1970

Induction of rabbit antibody with molecular uniformity after immunization with group C streptococci.

Antibodies with uniform properties may occur in rabbits after immunization with Group C streptococci. These precipitating antibodies possess specificity for the group-specific carbohydrate. Not uncommonly, their concentration is between 20 and 40 mg/ml of antiserum. Evidence for molecular uniformity in the case of one of these antibodies, described in detail here, includes: individual antigenic specificity; monodisperse distribution of the light chains by alkaline urea polyacrylamide disc electrophoresis; and a single amino acid in each of the first three N-terminal positions of the light chains. When the amino acid sequence of rabbit antibody b+ light chains (kappa type) are aligned against their human kappa counterparts, a definite homology is observed between the N-terminus of the human and the rabbit variable region.

Amino Acid Sequence↗
PubMed1970

Allotype exclusion in uniform rabbit antibody to streptococcal carbohydrate.

Rabbit antibodies to streptococcal polysaccharide are described which show selectivity of expression of the allotypic specificities on both the heavy (H) and light (L) chains. One of these antibodies binds weakly to Sephadex. A purification method based on this binding has yielded antibody completely lacking any group a allotypic marker on its H chains.

Animals↗
PubMed1969

Rabbit antibodies to streptococcal carbohydrates. Influence of primary and secondary immunization and of possible genetic factors on the antibody response.

In a search for possible genetic factors which may influence the immune response to the streptococcal carbohydrates, over 100 rabbits have been immunized with streptococcal vaccines, and representative examples of high and low response pairs mated. The concentration of precipitins to the group-specific carbohydrates has been measured in the antisera following primary intravenous immunization with heat-killed streptococcal vaccines, Group A, Group A-variant, and Group C. For the majority of rabbits, the concentration of precipitins varied between 1 and 10 mg/ml of antiserum; while in the minority, it was between 11 and 32 mg/ml. The offspring of rabbits with high antibody levels had a significantly higher concentration of antibody than was seen in the offspring of rabbits of low response parents. Such data suggest that the magnitude of the immune response to these carbohydrate antigens is under some form of genetic control. Not uncommonly in rabbits with hyper-gamma-globulinemia following primary immunization, the group-specific precipitins are the predominant component of the gamma-globulin. An unusual feature of such components is that they are electrophoretically monodisperse, and possess individual antigenic specificity. In this respect they resemble the myeloma proteins. When a response of this sort is not seen after primary immunization, it may occur after secondary immunization. Therefore, prior exposure to the same or closely related antigen may also have an influence on the occurrence of high concentrations of such uniform antibodies.

Animals↗
PubMedDate not supplied

Gamma delta T cells in the peripheral blood of individuals from an area of holoendemic Plasmodium falciparum transmission.

gamma delta T cells bearing V gamma 9 T cell receptors from unexposed Caucasian donors make large responses to Plasmodium falciparum in vitro. This finding, together with observations of others showing high levels of V gamma 9+ T cells in the blood of infected non-immune individuals, led us to hypothesize that the response of these cells might contribute to the pathology of P. falciparum malaria. Acquisition of immunity to disease in people naturally exposed to infection may therefore be due in part to down-regulation or alteration of the function of gamma delta T cells. Supporting this view, and in contrast to infection in non-immune individuals, V gamma 9+ T cells are not elevated in peripheral blood of children or adults living in an endemic area despite constant exposure to P. falciparum. After in vitro stimulation with P. falciparum, however, the expansion of V gamma 9+ cells from the African donors is of similar magnitude to that observed for non-exposed Europeans. Thus, although these cells are not elevated in peripheral blood, they are still able to respond to P. falciparum antigens. In adult European donors the major gamma delta T cell population in peripheral blood is V gamma 9+ (approximately 70% of all gamma delta cells), whereas in the majority of adult Africans V delta 1+ V gamma 9- T cells predominated (approximately 70% of total gamma delta cells).

Adult↗
PubMedDate not supplied

Characterization of minor and major idiotopes associated with human antibodies to N-acetyl-D-glucosamine.

Human antibodies to N-acetyl-D-glucosamine (GlcNAc) were analysed by conventional and monoclonal antiidiotypic antibodies. These were prepared to the antibody secreted by the human lymphoblastoid cell line B17 and to the antibody isolated from an individual serum containing a prominent clonotype 1A, both with specificity for GlcNAc. Idiotypes and idiotopes associated with these antibodies have the following properties: 1) their frequency of expression in the human population varies between rare (approximately 1.5%) and frequent (greater than 80%); 2) they have a high degree of association with antibody specificity for GlcNAc (50-100%); 3) each idiotope appears to be expressed independently of others; 4) one idiotope may be associated with a variety of clonotypes; and 5) idiotopes can be identified which are both frequently expressed in the population and associated with major proportions of the antibodies in single individuals. These latter idiotopes may be useful for studies on the modulation of human immune responses by antiidiotypic antibodies.

Acetylglucosamine↗