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PDBsum entry 3tid

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Immune system PDB id
3tid
Contents
Protein chains
277 a.a.
99 a.a.
Ligands
ALA-VAL-TYR-ASN-
PHE-ALA-THR-MET
ACT ×3
Waters ×544

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: 10.4049/jimmunol.1300852]
PubMed id 24127554
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.
PROCHECK
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