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Different strategies adopted by K(b) and L(d) to generate T cell specificity directed against their respective bound peptides.

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Different strategies adopted by K(b) and L(d) to generate T cell specificity directed against their respective bound peptides.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kranz, David M. Colf, Leremy A. Garcia, K. Christopher Bowerman, Natalie A.
Description	Author Affiliation: Bowerman NA ( Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.)
Abstract	Mouse T cell clone 2C recognizes two different major histocompatibility (MHC) ligands, the self MHC K(b) and the allogeneic MHC L(d). Two distinct peptides, SIY (SIYRYYGL) and QL9 (QLSPFPFDL), act as strong and specific agonists when bound to K(b) and L(d), respectively. To explore further the mechanisms involved in peptide potency and specificity, here we examined a collection of single amino acid peptide variants of SIY and QL9 for 1) T cell activity, 2) binding to their respective MHC, and 3) binding to the 2C T cell receptor (TCR) and high affinity TCR mutants. Characterization of SIY binding to MHC K(b) revealed significant effects of three SIY residues that were clearly embedded within the K(b) molecule. In contrast, QL9 binding to MHC L(d) was influenced by the majority of peptide side chains, distributed across the entire length of the peptide. Binding of the SIY-K(b) complex to the TCR involved three SIY residues that were pointed toward the TCR, whereas again the majority of QL9 residues influenced binding of TCRs, and thus the QL9 residues had impacts on both L(d) and TCR binding. In general, the magnitude of T cell activity mediated by a peptide variant was influenced more by peptide binding to MHC than by binding the TCR, especially for higher affinity TCRs. Findings with both systems, but QL9-L(d) in particular, suggest that many single-residue substitutions, introduced into peptides to improve their binding to MHC and thus their vaccine potential, could impair T cell reactivity due to their dual impact on TCR binding.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	47
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-11-20
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Major Histocompatibility Complex Peptides Chemistry Receptors, Antigen, T-Cell Animals Binding Sites Cell Membrane Metabolism Dose-Response Relationship, Drug Lymphocyte Activation Mice Molecular Conformation Oligopeptides Protein Binding Protein Structure, Tertiary T-Lymphocytes Cytology Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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