Characterization of a T Cell Receptor: Peptide/MHC Binding Interaction

Schlueter, Carol Joy

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Description

Title

Characterization of a T Cell Receptor: Peptide/MHC Binding Interaction

Author(s)

Schlueter, Carol Joy

Issue Date

1997

Doctoral Committee Chair(s)

Kranz, David M.

Department of Study

Biochemistry

Discipline

Biochemistry

Degree Granting Institution

University of Illinois at Urbana-Champaign

Degree Name

Ph.D.

Degree Level

Dissertation

Keyword(s)

Health Sciences, Immunology

Language

eng

Abstract

To begin to examine the 2C TCR residues which provide a significant thermodynamic contribution toward the binding energy of a variety of ligands, including monoclonal antibodies (mAb), superantigens, and peptide/MHC ligands, we have expressed a family of 2C scTCRs which contain alanine point mutations in the complementarity determining regions (CDR) and fourth hypervariable region of the $\beta$ chain. Using these mutant scTCRs, we have identified V$\beta$ residues which are energetically important in the interaction of the 2C TCR with the anti-V$\beta$8 mAb F23.2, the anti-clonotypic mAb 1B2, and the peptide/MHC ligand QL9/L$\rm\sp{d}.$ Residues from all three CDR$\beta$ loops were implicated in the binding of the 2C TCR to QL9/L$\rm\sp{d}.$ Furthermore, every residue identified as part of the QL9/L$\rm\sp{d}$ epitope was also identified as part of the 1B2 epitope, suggesting that these two TCR ligands may share certain features in their tertiary structure even though their primary and secondary sequences are quite different. The construction of this panel of V$\beta$ mutant scTCRs has also facilitated possible future identification of 2C TCR $\beta$ chain residues which contact other peptide/MHC, mAb, and superantigen ligands.

Graduation Semester

1997

Type of Resource

text

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http://hdl.handle.net/2142/84886

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