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Soluble Major Histocompatibility Complex-Peptide Octamers with Impaired CD8 Binding Selectively Induce Fas-dependent Apoptosis

Soluble Major Histocompatibility Complex-Peptide Octamers with Impaired CD8 Binding Selectively Induce Fas-dependent Apoptosis

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GUILLAUME, Philippe, Daniel F. LEGLER, Nicole BOUCHERON, Marie-Agnès DOUCEY, Jean-Charles CEROTTINI, Immanuel F. LUESCHER, 2003. Soluble Major Histocompatibility Complex-Peptide Octamers with Impaired CD8 Binding Selectively Induce Fas-dependent Apoptosis. In: Journal of Biological Chemistry. 278(7), pp. 4500-4509. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M208863200

@article{Guillaume2003Solub-36628, title={Soluble Major Histocompatibility Complex-Peptide Octamers with Impaired CD8 Binding Selectively Induce Fas-dependent Apoptosis}, year={2003}, doi={10.1074/jbc.M208863200}, number={7}, volume={278}, issn={0021-9258}, journal={Journal of Biological Chemistry}, pages={4500--4509}, author={Guillaume, Philippe and Legler, Daniel F. and Boucheron, Nicole and Doucey, Marie-Agnès and Cerottini, Jean-Charles and Luescher, Immanuel F.} }

Guillaume, Philippe 2017-01-12T09:43:41Z Boucheron, Nicole Doucey, Marie-Agnès Cerottini, Jean-Charles Soluble Major Histocompatibility Complex-Peptide Octamers with Impaired CD8 Binding Selectively Induce Fas-dependent Apoptosis Luescher, Immanuel F. Fluorescence-labeled soluble major histocompatibility complex class I-peptide "tetramers" constitute a powerful tool to detect and isolate antigen-specific CD8<sup>+</sup> T cells by flow cytometry. Conventional "tetramers" are prepared by refolding of heavy and light chains with a specific peptide, enzymatic biotinylation at an added C-terminal biotinylation sequence, and "tetramerization" by reaction with phycoerythrin- or allophycocyanin-labeled avidin derivatives. We show here that such preparations are heterogeneous and describe a new procedure that allows the preparation of homogeneous tetra- or octameric major histocompatibility complex-peptide complexes. These compounds were tested on T1 cytotoxic T lymphocytes (CTLs), which recognize the Plasmodium berghei circumsporzoite peptide 252-260 (SYIPSAEKI) containing photoreactive 4-azidobenzoic acid on Lys<sup>259</sup> in the context of H-2K<sup>d</sup>. We report that mutation of the CD8 binding site of K<sup>d</sup> greatly impairs the binding of tetrameric but not octameric or multimeric K<sup>d</sup>-PbCS(ABA) complexes to CTLs. This mutation abolishes the ability of the octamer to elicit significant phosphorylation of CD3, intracellular calcium mobilization, and CTL degranulation. Remarkably, however, this octamer efficiently activates CTLs for Fas (CD95)-dependent apoptosis. Boucheron, Nicole Legler, Daniel F. Doucey, Marie-Agnès 2017-01-12T09:43:41Z Guillaume, Philippe Legler, Daniel F. Luescher, Immanuel F. eng Cerottini, Jean-Charles 2003

Dateiabrufe seit 12.01.2017 (Informationen über die Zugriffsstatistik)

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