Comparison of Proposed Putative Active Conformations of Myelin Basic Protein Epitope 87−99 Linear Altered Peptide Ligands by Spectroscopic and Modelling Studies:  The Role of Positions 91 and 96 in T-Cell Receptor Activation

2006 ◽  
Vol 49 (23) ◽  
pp. 6683-6691 ◽  
Author(s):  
Efthimia D. Mantzourani ◽  
Theodore V. Tselios ◽  
Simona Golic Grdadolnik ◽  
James A. Platts ◽  
Andrea Brancale ◽  
...  
Keyword(s):  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Cell Receptor ◽  
Receptor Activation ◽  
Peptide Ligands ◽  
Altered Peptide Ligands ◽  
Modelling Studies

Selection for T-cell receptor Vβ–Dβ–Jβ gene rearrangements with specificity for a myelin basic protein peptide in brain lesions of multiple sclerosis

Nature ◽  
1993 ◽  
Vol 362 (6415) ◽  
pp. 68-70 ◽  
Author(s):  
Jorge R. Oksenberg ◽  
Michael A. Panzara ◽  
Ann B. Begovich ◽  
Dennis Mitchell ◽  
Henry A. Erlich ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Cell Receptor ◽  
Brain Lesions ◽  
Gene Rearrangements ◽  
Selection For ◽  
T Cell Receptor Vβ

Preferential but Not Exclusive T Cell Receptor Vβ Chain Utilization of Myelin Basic Protein and Peptide-Specific T Cell Clones in Mice

1994 ◽  
Vol 153 (1) ◽  
pp. 206-213 ◽  
Author(s):  
Bernadette Kalman ◽  
Robert L. Knobler ◽  
Fred D. Lublin
Keyword(s):  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Cell Receptor ◽  
T Cell Clones ◽  
Cell Clones ◽  
T Cell Receptor Vβ

Diversity of T cell receptor α and β chain genes expressed by human T cells specific for similar myelin basic protein peptide/major histocompatibility complexes

1992 ◽  
Vol 22 (3) ◽  
pp. 753-758 ◽  
Author(s):  
Gerhard Giegerich ◽  
Martin Pette ◽  
Edgar Meinl ◽  
Jörg T. Epplen ◽  
Hartmut Wekerle ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Cell Receptor ◽  
Major Histocompatibility ◽  
Human T Cells ◽  
Major Histocompatibility Complexes ◽  
Β Chain

Diversity of T-cell receptor Valpha, Vbeta, and CDR3 expression by myelin basic protein-specific human T-cell clones

Neurology ◽  
1995 ◽  
Vol 45 (10) ◽  
pp. 1919-1922 ◽  
Author(s):  
J. R. Richert ◽  
E.D. Robinson ◽  
K. Camphausen ◽  
R. Martin ◽  
R. R. Voskuhl ◽  
...  
Keyword(s):  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Cell Receptor ◽  
T Cell Clones ◽  
Human T Cell ◽  
Cell Clones

Clonal expansion of myelin basic protein-reactive T cells in patients with multiple sclerosis: Restricted T cell receptor V gene rearrangements and CDR3 sequence

1995 ◽  
Vol 25 (4) ◽  
pp. 958-968 ◽  
Author(s):  
Caroline Vandevyver ◽  
Nadja Mertens ◽  
Peter van den Elsen ◽  
Robert Medaer ◽  
Jef Raus ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
T Cells ◽  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Clonal Expansion ◽  
Cell Receptor ◽  
Gene Rearrangements ◽  
V Gene

Effects of vaccination with T cell receptor peptides: Epitope switching to a possible disease-protective determinant of myelin basic protein that is cross-reactive with a TCR BV peptide

1998 ◽  
Vol 76 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Arthur A Vandenbark ◽  
Yuan K Chou ◽  
Ruth Whitham ◽  
Dennis N Bourdette ◽  
Halina Offner
Keyword(s):  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Cell Receptor

scholarly journals Structural basis for T cell recognition of altered peptide ligands: a single T cell receptor can productively recognize a large continuum of related ligands.

1996 ◽  
Vol 184 (4) ◽  
pp. 1259-1268 ◽  
Author(s):  
G J Kersh ◽  
P M Allen
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Cell Clone ◽  
Cell Receptor ◽  
Peptide Ligands ◽  
Structural Basis ◽  
Side Chain ◽  
Contact Residue ◽  
Altered Peptide Ligands ◽  
T Cell Clone

T cells recognize short linear peptides bound to major histocompatibility complex (MHC)-encoded molecules. Subtle molecular changes in peptide antigens produce altered peptide ligands (APLs), which induce different T cell responses from those induced by the antigenic ligand. A molecular basis for how these slight molecular variations lead to such different consequences for the T cell has not been described. To address this issue, we have made amino acid substitutions at the primary T cell receptor (TCR) contact residue of the murine hemoglobin determinant, Hb(64-76)/I-Ek and produced 12 peptides that interact with the TCR of the T cell clone 3.L2. The 3.L2 T cell responds to these peptides, which vary 1 million-fold in their activity, and enables them to be ranked according to their relative ability to signal through the 3.L2 TCR. Such a ranking reveals that the ability of the 3.L2 T cell to respond to these peptides depends on how well the structure of the side chain at the primary TCR contact site mimics that of the Asn residue present in the antigenic ligand. The reactivity of the 3.L2 T cell also depends on an MHC contact residue that is next to the primary TCR contact residue, suggesting that conformation of the Asn side chain is also important. By using nonnatural amino acids at a TCR contact residue, we have demonstrated that APLs can be rationally designed based on structure. These data are consistent with a model in which the affinity of a peptide-MHC complex for the TCR determines how the T cell will respond.

T Cell Receptor Gene Rearrangements in the Human Response to Myelin Basic Protein

1991 ◽  
Vol 636 (1 Antigen and C) ◽  
pp. 396-399 ◽  
Author(s):  
J. R. RICHERT ◽  
E. D. ROBINSON ◽  
R. MARTIN ◽  
H. F. McFARLANDb ◽  
C. K. HURLEY
Keyword(s):  
T Cell ◽  
Myelin Basic Protein ◽  
T Cell Receptor ◽  
Basic Protein ◽  
Receptor Gene ◽  
Cell Receptor ◽  
Gene Rearrangements ◽  
Human Response ◽  
T Cell Receptor Gene ◽  
Cell Receptor Gene
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