Immunoprecipitation of Cell Surface Structures of Cloned Cytotoxic T Lymphocytes by Clone-Specific Antisera

Clones of cytotoxic T lymphocytes (CTL) differ in their specific reactivity with diverse target cell antigens. To learn about the uniqueness of individual CTL clones we injected rats and mice with cloned CTL in an effort to prepare clone-specific antisera and to analyze the CTL surface molecules tha...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1984, Vol.81 (2), p.573-577
Main Authors: Kranz, David M., Sherman, David H., Sitkovsky, Michail V., Pasternack, Mark S., Eisen, Herman N.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antigens
Antigens, Surface - immunology
Antiserum
Cell Membrane - immunology
cell surface
Clone Cells
Cytotoxicity, Immunologic
Dimers
Disulfides
Electrophoresis
Gels
immunoprecipitation
lymphocytes T
Mice
Molecular Weight
Molecules
Rats
Receptors
Receptors, Immunologic - immunology
Spleen cells
T lymphocytes
T-Lymphocytes, Cytotoxic - immunology
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Summary:Clones of cytotoxic T lymphocytes (CTL) differ in their specific reactivity with diverse target cell antigens. To learn about the uniqueness of individual CTL clones we injected rats and mice with cloned CTL in an effort to prepare clone-specific antisera and to analyze the CTL surface molecules that were immunoprecipitated by these antisera. Three clones were studied. They were all derived from BALB.B mice and were specific for antigens encoded by the major histocompatibility complex of the H-2dhaplotype. Antisera raised in rats against individual clones contained antibodies to lymphocyte function-associated antigen type 1 (LFA-1) and inhibited the cytotoxic activity of all of the clones. In contrast, BALB/c and BALB.K mice injected with individual clones consistently yielded alloantisera that were clone specific in their ability to inhibit CTL-mediated lysis of target cells (P815). In addition, these alloantisera immunoprecipitated from extracts of125I-radiolabeled CTL a disulfide-bonded dimer consisting of ≈ 45-kilodalton subunits. This dimer resembles the putative T-cell antigen-recognition receptor recently identified in several laboratories. The alloantisera also immunoprecipitated CTL surface molecules that were associated with β2-microglobulin and that differed in apparent molecular mass (37-38 kilodaltons) in different clones.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.81.2.573