 |
PDBsum entry 3tid
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
3tid
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Disparate epitopes mediating protective heterologous immunity to unrelated viruses share peptide-Mhc structural features recognized by cross-Reactive t cells.
|
 |
|
Authors
|
 |
Z.T.Shen,
T.T.Nguyen,
K.A.Daniels,
R.M.Welsh,
L.J.Stern.
|
 |
|
Ref.
|
 |
J Immunol, 2013,
191,
5139-5152.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
Abstract
|
 |
|
Closely related peptide epitopes can be recognized by the same T cells and
contribute to the immune response against pathogens encoding those epitopes, but
sometimes cross-reactive epitopes share little homology. The degree of
structural homology required for such disparate ligands to be recognized by
cross-reactive TCRs remains unclear. In this study, we examined the mechanistic
basis for cross-reactive T cell responses between epitopes from unrelated and
pathogenic viruses, lymphocytic choriomeningitis virus (LCMV) and vaccinia
virus. Our results show that the LCMV cross-reactive T cell response toward
vaccinia virus is dominated by a shared asparagine residue, together with other
shared structural elements conserved in the crystal structures of K(b)-VV-A11R
and K(b)-LCMV-gp34. Based on analysis of the crystal structures and the
specificity determinants for the cross-reactive T cell response, we were able to
manipulate the degree of cross-reactivity of the T cell response, and to predict
and generate a LCMV cross-reactive response toward a variant of a null
OVA-derived peptide. These results indicate that protective heterologous immune
responses can occur for disparate epitopes from unrelated viruses.
|
 |
|
|
|
|
 |