Properties of anti-idiotypic T cell lines propagated with syngeneic B lymphocytes. I. T cells bind intact idiotypes and discriminate between the somatic idiotypic variants in a manner similar to the anti-idiotopic antibodies.

The primary antibody response of C57BL/6 mice to phosphorylcholine (PC) is dominated by immunoglobulins of the T15 idiotype family. Using monoclonal antibodies that define individual idiotopes (Id) of T15, it has been shown that the antibody plaque-forming cells (PFC) arise from heterogeneous population of B cells that may express some but not all T15 Id. In the present study, we tested the ability of antigen (keyhole limpet hemocyanin, KLH)-specific CD4+ T cell clones (Th) to provide help for various T15 B cell subsets in response to PC-KLH in vitro. Four independently derived, KLH-specific Th clones were found to provide quantitative help (80-120 PFC/culture of 10(6) B cells) which was comparable to KLH-primed, unselected T cells. However, the response in the presence of the cloned T cells was idiotopically restricted: T15 idiotopes B24-44 and B36-75 were expressed on 60% to 90% PFC, whereas Id AB1-2 and B36-82 were not present (0%-20% PFC). All of these Id were highly expressed in cultures with KLH-primed, unselected splenic T cells. Evidently, the cloned Th cells provided help to only a subset of idiotypically distinct B cells. Bulk spleen T cells from unprimed donors by themselves did not provide any help for the primary response to PC-KLH. However, when these cells were added to the cultures containing B cells and KLH-specific Th clones, the repertoire of the response was fully restored, including the AB1-2/B36-82 Id (50%-80% PFC). These results suggest the existence of an auxiliary helper mechanism that may be required for activation of some B cells in addition to the antigen-specific Th cells.

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Major histocompatibility complex class I‐restricted presentation of influenza virus nucleoprotein peptide by B lymphoma cells harboring an antibody gene antigenized with the virus peptide

Billetta

Filaci

Zanetti

1995

Eur J Immunol

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We analyzed the capacity of B cells to process and present a peptide from the variable region of an endogenous immunoglobulin heavy (H) chain to a major histocompatibility complex (MHC) class I-restricted cytotoxic T lymphocyte (CTL) clone. The H-chain gene was engineered to express 14-amino acid peptide from the sequence of the influenza virus nucleoprotein (NP) antigen in the third complementarity-determining region (CDR3). This NP peptide is presented in association with the Db allele in H-2b mice. We demonstrate that B lymphoma cells (H-2b) harboring the antigenized H-chain gene process and present the NP peptide in association with the Db molecule and are lysed by a CTL clone specific for that peptide in an MHC-restricted way. In contrast, the soluble antigenized antibody failed to mediate lysis of H-2b target cells. The endogenously processed immunoglobulin CDR3 peptide could be eluted from surface Db molecules in transfected cells. This study formally demonstrates that peptides from the hypervariable loops of endogenous immunoglobulin are processed through the endogenous degradative pathway and are presented to CD8+ T cells in the context of MHC class I molecules. The implication of these findings for processing and presentation of endogenous immunoglobulin peptides in B cells and network regulation by idiopeptides is discussed.

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Properties of anti-idiotypic T cell lines propagated with syngeneic B lymphocytes. I. T cells bind intact idiotypes and discriminate between the somatic idiotypic variants in a manner similar to the anti-idiotopic antibodies.

Cited by 19 publications

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T-cell-epitope mapping of the idiotypic monoclonal IgG heavy and light chains in multiple myeloma

T-cell-epitope mapping of the idiotypic monoclonal IgG heavy and light chains in multiple myeloma

Restricted idiotypic profile of anti‐phosphorylcholine antibodies induced by carrier‐specific helper T cell clones

Major histocompatibility complex class I‐restricted presentation of influenza virus nucleoprotein peptide by B lymphoma cells harboring an antibody gene antigenized with the virus peptide

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