Effects of epitope modification on T cell receptor-ligand binding and antigen recognition by seven H-2Kd-restricted cytotoxic T lymphocyte clones specific for a photoreactive peptide derivative.

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Serval ID
serval:BIB_E6132910678C
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Effects of epitope modification on T cell receptor-ligand binding and antigen recognition by seven H-2Kd-restricted cytotoxic T lymphocyte clones specific for a photoreactive peptide derivative.
Journal
The Journal of experimental medicine
Author(s)
Kessler B.M., Bassanini P., Cerottini J.C., Luescher I.F.
ISSN
0022-1007
Publication state
Published
Issued date
1997
Peer-reviewed
Oui
Volume
185
Number
4
Pages
629-640
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
We tested for antigen recognition and T cell receptor (TCR)-ligand binding 12 peptide derivative variants on seven H-2Kd-restricted cytotoxic T lymphocytes (CTL) clones specific for a bifunctional photoreactive derivative of the Plasmodium berghei circumsporozoite peptide 252-260 (SYIPSAEKI). The derivative contained iodo-4-azidosalicylic acid in place of PbCS S-252 and 4-azidobenzoic acid on PbCS K-259. Selective photoactivation of the N-terminal photoreactive group allowed crosslinking to Kd molecules and photoactivation of the orthogonal group to TCR. TCR photoaffinity labeling with covalent Kd-peptide derivative complexes allowed direct assessment of TCR-ligand binding on living CTL. In most cases (over 80%) cytotoxicity (chromium release) and TCR-ligand binding differed by less than fivefold. The exceptions included (a) partial TCR agonists (8 cases), for which antigen recognition was five-tenfold less efficient than TCR-ligand binding, (b) TCR antagonists (2 cases), which were not recognized and capable of inhibiting recognition of the wild-type conjugate, (c) heteroclitic agonists (2 cases), for which antigen recognition was more efficient than TCR-ligand binding, and (d) one partial TCR agonist, which activated only Fas (C1)95), but not perforin/granzyme-mediated cytotoxicity. There was no correlation between these divergences and the avidity of TCR-ligand binding, indicating that other factors than binding avidity determine the nature of the CTL response. An unexpected and novel finding was that CD8-dependent clones clearly incline more to TCR antagonism than CD8-independent ones. As there was no correlation between CD8 dependence and the avidity of TCR-ligand binding, the possibility is suggested that CD8 plays a critical role in aberrant CTL function.
Keywords
Affinity Labels, Amino Acid Sequence, Antigens, CD95/immunology, CD8-Positive T-Lymphocytes, Cell Line, Clone Cells, H-2 Antigens/immunology, Membrane Glycoproteins/immunology, Molecular Sequence Data, Peptides/chemistry, Peptides/immunology, Perforin, Pore Forming Cytotoxic Proteins, Receptors, Antigen, T-Cell/antagonists &amp, inhibitors, Receptors, Antigen, T-Cell/immunology, T-Lymphocytes, Cytotoxic/immunology
Pubmed
Web of science
Open Access
Yes
Create date
28/01/2008 11:19
Last modification date
20/08/2019 16:09
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