AI Article Synopsis
- The decameric peptide SALQNAASIA from Mycobacterium bovis is recognized by a specific murine T-cell receptor (UZ-3-4) when presented with the H-2D(b) major histocompatibility complex.
- This T-cell receptor can also cross-react with another peptide (KDIGNIISDA) from murine hsp60, but not with a related nonameric peptide (SALQNAASI).
- Analysis of the crystal structure of the SALQNAASIA/H-2D(b) complex reveals insights into the mechanisms behind T-cell receptor cross-reactivity and its potential role in autoimmune pathology.
Article Abstract
The decameric peptide SALQNAASIA from the Mycobacterium bovis heat shock protein (hsp) 60 is recognized by the murine T-cell receptor UZ-3-4 in complex with the murine class I major histocompatibility complex molecule H-2D(b). This T-cell receptor cross-reacts with the H-2D(b)-bound non-homologous decameric peptide KDIGNIISDA from the murine hsp60, but does not recognize the nonameric mycobacterial peptide SALQNAASI. Cross-recognition of the KDIGNIISDA/H-2D(b) complex induces autoimmune pathology in immunodeficient mice. We solved the X-ray crystal structure of the SALQNAASIA/H-2D(b) complex at 3.0 A resolution, and we modelled the KDIGNIISDA and SALQNAASI peptides in the H-2D(b) binding site. The structural analysis of the H-2D(b)-bound hsp60 epitopes offers insight into T-cell receptor cross-reactivity.
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| http://dx.doi.org/10.1016/s0014-5793(03)00325-9 | DOI Listing |
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