Differential roles of T cell receptor alpha and beta chains in ligand binding among H-2Kd-restricted cytolytic T lymphocyte clones specific for a photoreactive Plasmodium berghei circumsporozoite peptide derivative.

Détails

ID Serval
serval:BIB_2472AE28C6EF
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Differential roles of T cell receptor alpha and beta chains in ligand binding among H-2Kd-restricted cytolytic T lymphocyte clones specific for a photoreactive Plasmodium berghei circumsporozoite peptide derivative.
Périodique
The Journal of biological chemistry
Auteur(s)
Anjuère F., Kuznetsov D., Romero P., Cerottini J.C., Jongeneel C.V., Luescher I.F.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
1997
Peer-reviewed
Oui
Volume
272
Numéro
13
Pages
8505-8514
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
To study the interaction of T cell receptor with its ligand, a complex of a major histocompatibility complex molecule and a peptide, we derived H-2Kd-restricted cytolytic T lymphocyte clones from mice immunized with a Plasmodium berghei circumsporozoite peptide (PbCS) 252-260 (SYIPSAEKI) derivative containing photoreactive Nepsilon-[4-azidobenzoyl] lysine in place of Pro-255. This residue and Lys-259 were essential parts of the epitope recognized by these clones. Most of the clones expressed BV1S1A1 encoded beta chains along with specific complementary determining region (CDR) 3beta regions but diverse alpha chain sequences. Surprisingly, all T cell receptors were preferentially photoaffinity labeled on the alpha chain. For a representative T cell receptor, the photoaffinity labeled site was located in the Valpha C-strand. Computer modeling suggested the presence of a hydrophobic pocket, which is formed by parts of the Valpha/Jalpha C-, F-, and G-strands and adjacent CDR3alpha residues and structured to be able to avidly bind the photoreactive ligand side chain. We previously found that a T cell receptor specific for a PbCS peptide derivative containing this photoreactive side chain in position 259 similarly used a hydrophobic pocket located between the junctional CDR3 loops. We propose that this nonpolar domain in these locations allow T cell receptors to avidly and specifically bind epitopes containing non-peptidic side chains.
Mots-clé
Affinity Labels, Amino Acid Sequence, Animals, Apicomplexa, Clone Cells/immunology, Computer Simulation, H-2 Antigens/metabolism, Mice, Models, Molecular, Molecular Sequence Data, Peptide Fragments/metabolism, Peptide Mapping, Photochemistry, Plasmodium berghei, Protozoan Proteins/metabolism, Receptors, Antigen, T-Cell, alpha-beta/chemistry, Receptors, Antigen, T-Cell, alpha-beta/metabolism, T-Lymphocytes/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:39
Dernière modification de la notice
20/08/2019 14:02
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