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Volume 272, Number 13, Issue of March 28, 1997 pp. 8505-8514
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Differential Roles of T Cell Receptor  and  Chains in Ligand Binding Among H-2K^d-restricted Cytolytic T Lymphocyte Clones Specific for a Photoreactive Plasmodium berghei Circumsporozoite Peptide Derivative

(Received for publication, October 7, 1996)

Fabienne Anjuère , Dmitry Kuznetsov , Pedro Romero , Jean-Charles Cerottini , C. Victor Jongeneel and Immanuel F. Luescher

From the  Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, 1066 Epalinges, Switzerland

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-2K^d-restricted cytolytic T lymphocyte clones from mice immunized with a Plasmodium berghei circumsporozoite peptide (PbCS) 252-260 (SYIPSAEKI) derivative containing photoreactive N-[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  chains along with specific complementary determining region (CDR) 3 regions but diverse  chain sequences. Surprisingly, all T cell receptors were preferentially photoaffinity labeled on the  chain. For a representative T cell receptor, the photoaffinity labeled site was located in the V C-strand. Computer modeling suggested the presence of a hydrophobic pocket, which is formed by parts of the V/J C-, F-, and G-strands and adjacent CDR3 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.

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