The role of single amino acids in the recognition of a T cell epitope

Suhrbier, A., Rodda, S. J., Ho, P. C., Csurhes, P., Dunckley, H., Saul, A., Geysen, H. M. and Rzepczyk, C. M. (1991) The role of single amino acids in the recognition of a T cell epitope. Journal of Immunology, 147 8: 2507-2513.

Author Suhrbier, A.
Rodda, S. J.
Ho, P. C.
Csurhes, P.
Dunckley, H.
Saul, A.
Geysen, H. M.
Rzepczyk, C. M.
Title The role of single amino acids in the recognition of a T cell epitope
Journal name Journal of Immunology   Check publisher's open access policy
ISSN 0022-1767
Publication date 1991-10-15
Sub-type Article (original research)
Volume 147
Issue 8
Start page 2507
End page 2513
Total pages 7
Place of publication Bethesda, MD, USA
Publisher American Association of Immunologists
Language eng
Subject 1107 Immunology
Abstract T cell epitopes can be defined by the use of synthetic peptides, which when added to APC efficiently mimic naturally processed Ag. Free peptide is thought to bind to cell-surface MHC glycoproteins and the TCR then recognizes the resulting complex. The specificity of a tetanus toxin-specific human Th cell clone was investigated using a complete replacement set of peptides in which every amino acid within the minimal T cell epitope was replaced by each of the 19 alternative genetically coded amino acids. Within the minimal epitope, found to be YSYFPSVI (tetanus toxin 593-600), a small number of substitutions could be made without significant loss of activity, defined as substitutions giving peptides whose activity fell within +/- 3 SD of the mean parent response. Y593 could be substituted with F, W, M, L, V, and I; S594 with G and T; Y595, F596, and P597 with no other amino acids; S598 with A; V599 with S, and I600 with L. Rank ordering of the substitutions allowed a precise description to be made of MHC and/or TCR interaction with each amino acid side chain within the epitope. Simplified theoretic calculations based on this study indicate that class II T cell recognition has a specificity greater than 1 in 10(8). Competition experiments indicate that Y595, F596, P597, and I600 are critical for binding of this epitope to its restricting element, HLA DR4Dw14.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
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Created: Thu, 08 Jul 2010, 10:13:59 EST by Laura McTaggart on behalf of Faculty Of Health Sciences