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Results for “Immunoglobulin Idiotypes”

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At least 19 recordsLinked to original sources
PubMed1978

Mediation of cytotoxic functions by classes and subclasses of sheep antibody reactive with cell surface immunoglobulin idiotypic and constant region determinants.

Sheep antibodies, reactive with either the idiotypic or constant region antigenic determinants of the immunoglobulin light chain on guinea-pig L2C leukaemic cells, were separated into IgM and into the two subclasses of IgG, IgG1 and IgG2. Antibody of both IgG subclasses inhibited the migration of L2C cells along plastic surfaces; IgM was only weakly inhibitory. Antibody of class IgM and of subclass IgG1 mediated complement cytotoxicity against the L2C cells whereas only that of subclass IgG2 mediated K-cell cytotoxicity; the effector arms were rabbit complement and sheep peripheral leucocytes, respectively.

Animals↗
PubMed1975

Recognition of immunoglobulin idiotypes by thymus-derived lymphocytes.

The ability of thymus-derived lymphocytes (T cells) from BALB/c mice to recognize the individually specific antigenic determinants (idiotypes) of BALB/c myeloma proteins was tested. Spleen cells from donor mice immunized with a given myeloma protein greatly augmented the response of hapten-specific bone marrow-derived, thymus-independent lymphocytes (cells) to a hapten conjugate of the immunizing myeloma protein. This helper effect was specific for the myeloma protein idiotype; responses to hapten conjugates of similar myeloma proteins, bearing different idiotypic determinants, were not augmented by these spleen cells. That the helper cell is a T cell was shown by its marked sensitivity to cytolysis with an isoantiserum specific for T cells (anti-Thy-1-2) and complement. The discrimination between idiotypes by such T cells is roughly comparable to that of the antibody produced by the donors of the helper cells.

Animals↗
PubMed1977

The inheritance of antibody V regions in the rabbit: linkage of an H-chain-specific idiotype to immunoglobulin allotypes.

Anti-idiotype antibodies specific for the H chain of an homogeneous antistreptococcal antibody (4135 Ab) were prepared by injection of recombinant molecules consisting of the H chains from 4135 Ab and L chains isolated from the injected rabbit. The antibodies prepared in this fashion (anti-HId) were specific for the VH region of 4135 Ab. Using this preparation in an inhibition of binding assay, sera from rabbits related and unrelated to 4135 were screened for the presence of the 4135 HId. It was found that about 45% of the related rabbits, when immunized with streptococcal Group C vaccine, produced antibodies with a cross-reactive idiotype, while less than 10% of similarly immunized unrelated rabbits produced molecules bearing HId. The expression of HId was linked to the a3 allotype present in the H chain allogroup J. Antibody molecules bearing the HId determinant were isolated from heterozygous (a1a3 and a2a3) rabbits and shown to express the a3 allotype. One rabbit lacking the a3 allotype produced significant amounts of antibodies expressing HId. These antibodies were found to express both VH and CH allo-types characteristic of the J allogroup, although neither allotype was found in a preimmune IgG sample from this rabbit.

Animals↗
PubMed1979

Idiotypic cross-reactivity of human and murine phosphorylcholine-binding immunoglobulins.

The idiotypic cross-reactivity of mouse and human monoclonal immunoglobulins with binding activity for phosphorylcholine (PC) was investigated, using an idiotypic antibody elicited against the PC-binding human IgMFR. The isolated FR heavy chain proved to be a better inhibitor for the reaction of IgMFR with anti-FR than the FR light chain, but the intact protein was necessary for full idiotypic expression. PC was an inhibitor only at concentrations greater than 10(-3) M indicating that the idiotypic antibody was not combining site-directed. Among the murine PC-binding IgA myeloma proteins, MOPC 167 was found to be the best inhibitor, but its inhibitory capacity was about 4 orders of magnitude lower than that of the homologous IgMFR. McPC 603 was an even weaker inhibitor, while TEPC 15 effected no better inhibition than human monoclonal immunoglobulins without PC-binding activity. MOPC 167 has a most similar binding specificity to IgMFR as indicated by the high affinity for choline of these two proteins. TEPC 15 and McPC 603, on the other hand, exhibit a much lower affinity for choline. In addition to their similarity in specificity, proteins FR and MOPC 167 show important structural similarities within parts of their heavy and light chain variable domains. The data provide some evidence for the existence of idiotypic cross-reactivity between the two species man and mouse.

Animals↗
PubMed1979

Immunoglobulin differentiation is dictated by repeated recombination sequences within the V region prototype gene: a hypothesis.

Analysis of the available DNA sequences of immunoglobulin light chain genes reveals a unique structural pattern. A stretch of about 15 nucleotides repeats five times within the variable (V) region gene, with few base changes. Identification of these homologous sequences is apparent in the embryonic V(lambda) gene and might also be recognized in V(kappa) genes isolated from a myeloma. Although different from each other, the V(lambda) and V(kappa) hyperhomologous sequences display a remarkable resemblance to different prokaryote sequences associated with recombinational events. The homologous sequences appear at all three sites where hypervariable regions of the mature peptide are encoded. In addition, they are located at the site where V/constant (C) recombination is supposed to take place. Consequently, a general model is proposed for immunoglobulin differentiation. The hyperhomologous loci are postulated to be comprised of recombination sequences which makes them available for a mechanism of single-stranded DNA exposure. B cell maturation begins with V/C recombination, a step that is rate limiting. The fidelity of the process is ensured by extensive DNA homology between the two embryonic subgenes of V and C. Next, an error-prone repair system is activated and thereby introduces changes into the content of the immunoglobulin gene at the exposed loci. The process ends when mutations make the recombination sequence unrecognizable as such. The model is consistent with large amounts of data and is compatible with the view that immunoglobulin diversity is being generated somatically.

Animals↗
PubMed1979

Intraembryonic origin of lymphoid stem cells in the chicken: studies with sex chromosome and IgG allotype markers in histocompatible yolk sac-embryo chimaeras.

Two-day-old chick embryonic bodies were transplanted onto the area vasculosa of age-matched histocompatible blastoderms, resulting in the development of yolk sac-embryo chimaeras. Eighteen of these succeeded in hatching and became adults. Differences in the sex chromosomes and in IgG allotype between the embryo and the yolk sac were used to study the contribution of these two components to the lymphoid cell development. At 5-7 weeks of age the chimaeras proved to be completely normal in the IgM and IgG antibody production against human gamma globulin and Brucella abortus and in the lymphocyte responses to phytohaemagglutinin and concanavalin A. For the sex chromosome analyses bursa cells and specifically stimulated B and T lymphocytes were used. The latter was achieved by stimulating thymus, spleen, and bone marrow cells in vitro with anti-Ig and Con A. Only four out of 1498 mitoses analysed belonged to the sex opposite to that of the bird. Among the chimaeras eleven were marked through IgG allotypes. At the age of 3-20 weeks all eleven chimaeras showed serum IgG of the embryo allotype and none of the yolk sac type. These results, based on the use of two different markers, indicate that lymphoid stem cells in the chicken are originally derived from an intraembryonic source and not from the yolk sac.

Animals↗