scholarly journals Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a Mouse T-cell Receptor β Chain

2010 ◽  
Vol 286 (2) ◽  
pp. 1189-1195 ◽  
Author(s):  
Marisa M. Fernández ◽  
Sangwoo Cho ◽  
Mauricio C. De Marzi ◽  
Melissa C. Kerzic ◽  
Howard Robinson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Staphylococcal Enterotoxin ◽  
Β Chain

scholarly journals Three-Dimensional Structure of the Complex between a T Cell Receptor β Chain and the Superantigen Staphylococcal Enterotoxin B

Immunity ◽  
1998 ◽  
Vol 9 (6) ◽  
pp. 807-816 ◽  
Author(s):  
Hongmin Li ◽  
Andrea Llera ◽  
Daisuke Tsuchiya ◽  
Lukas Leder ◽  
Xavier Ysern ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Three Dimensional ◽  
Cell Receptor ◽  
Staphylococcal Enterotoxin ◽  
Dimensional Structure ◽  
Staphylococcal Enterotoxin B ◽  
Three Dimensional Structure ◽  
Enterotoxin B ◽  
Β Chain

Superantigen natural affinity maturation revealed by the crystal structure of staphylococcal enterotoxin G and its binding to T-cell receptor Vβ8.2

2007 ◽  
Vol 68 (1) ◽  
pp. 389-402 ◽  
Author(s):  
Marisa M. Fernández ◽  
Suparna Bhattacharya ◽  
Mauricio C. De Marzi ◽  
Patrick H. Brown ◽  
Melissa Kerzic ◽  
...  
Keyword(s):  
Crystal Structure ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Affinity Maturation ◽  
Staphylococcal Enterotoxin

scholarly journals A Mutational Analysis of the Binding of Staphylococcal Enterotoxins B and C3 to the T Cell Receptor β Chain and Major Histocompatibility Complex Class II

1998 ◽  
Vol 187 (6) ◽  
pp. 823-833 ◽  
Author(s):  
Lukas Leder ◽  
Andrea Llera ◽  
Pascal M. Lavoie ◽  
Marina I. Lebedeva ◽  
Hongmin Li ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
T Cell Receptor ◽  
Hot Spot ◽  
Cell Receptor ◽  
Class Ii ◽  
Staphylococcal Enterotoxin ◽  
Sedimentation Equilibrium ◽  
Simple Relationship ◽  
Β Chain

The three-dimensional structure of the complex between a T cell receptor (TCR) β chain (mouse Vβ8.2Jβ2.1Cβ1) and the superantigen (SAG) staphylococcal enterotoxin C3 (SEC3) has been recently determined to 3.5 Å resolution. To evaluate the actual contribution of individual SAG residues to stabilizing the β–SEC3 complex, as well as to investigate the relationship between the affinity of SAGs for TCR and MHC and their ability to activate T cells, we measured the binding of a set of SEC3 and staphylococcal enterotoxin B (SEB) mutants to soluble recombinant TCR β chain and to the human MHC class II molecule HLA-DR1. Affinities were determined by sedimentation equilibrium and/or surface plasmon detection, while mitogenic potency was assessed using T cells from rearrangement-deficient TCR transgenic mice. We show that there is a clear and simple relationship between the affinity of SAGs for the TCR and their biological activity: the tighter the binding of a particular mutant of SEC3 or SEB to the TCR β chain, the greater its ability to stimulate T cells. We also find that there is an interplay between TCR–SAG and SAG–MHC interactions in determining mitogenic potency, such that a small increase in the affinity of a SAG for MHC can overcome a large decrease in the SAG's affinity for the TCR. Finally, we observe that those SEC3 residues that make the greatest energetic contribution to stabilizing the β–SEC3 complex (“hot spot” residues) are strictly conserved among enterotoxins reactive with mouse Vβ8.2, thereby providing a basis for understanding why SAGs having other residues at these positions show different Vβ-binding specificities.

Crystal structure of a T-cell receptor β-chain complexed with a superantigen

Nature ◽  
1996 ◽  
Vol 384 (6605) ◽  
pp. 188-192 ◽  
Author(s):  
Barry A. Fields ◽  
Emilio L. Malchiodi ◽  
Hongmin Li ◽  
Xavier Ysern ◽  
Cynthia V. Stauffacher ◽  
...  
Keyword(s):  
Crystal Structure ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Β Chain

Restricted usage of T-cell receptor α-chain variable region (TCRAV) and T-cell receptor β-chain variable region (TCRBV) repertoires after human allogeneic haematopoietic transplantation

2000 ◽  
Vol 109 (4) ◽  
pp. 759-769 ◽  
Author(s):  
Takaji Matsutani ◽  
Takeshi Yoshioka ◽  
Yuji Tsuruta ◽  
Shoji Iwagami ◽  
Tomoko Toyosaki-Maeda ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Variable Region ◽  
Cell Receptor ◽  
Α Chain ◽  
Β Chain

Specificity and T cell receptor β chain usage of a human collagen type II-reactive T cell clone derived from a healthy individual

1992 ◽  
Vol 22 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Tan Yan ◽  
Harald Burkhardt ◽  
Thomas Ritter ◽  
Barbara Bröker ◽  
Karl Heinz Mann ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Collagen Type ◽  
Cell Clone ◽  
Cell Receptor ◽  
Type Ii ◽  
Collagen Type Ii ◽  
T Cell Clone ◽  
Human Collagen ◽  
Β Chain

T-cell receptor variable region of the β-chain gene use in peripheral blood and multiple synovial membranes during rheumatoid arthritis

1995 ◽  
Vol 42 (4) ◽  
pp. 331-339 ◽  
Author(s):  
Antoine Alam ◽  
Jacqueline Lulé ◽  
Héléne Coppin ◽  
Nathalie Lambert ◽  
Bernard Maziéres ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
T Cell ◽  
T Cell Receptor ◽  
Peripheral Blood ◽  
Variable Region ◽  
Cell Receptor ◽  
Chain Gene ◽  
Synovial Membranes ◽  
Β Chain

scholarly journals Genomic Organization of the Chicken T-Cell Receptor β Chain D-J-C Region

2004 ◽  
Vol 66 (12) ◽  
pp. 1509-1515 ◽  
Author(s):  
Akiko SHIGETA ◽  
Masaharu SATO ◽  
Tsuyoshi KAWASHIMA ◽  
Hiroyuki HORIUCHI ◽  
Haruo MATSUDA ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Genomic Organization ◽  
Cell Receptor ◽  
Β Chain
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