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J. Exp. Med., Volume 189, Number 2, January 18, 1999 359-370

Structural Evidence of  T Cell Xeno-reactivity in the Absence of Molecular Mimicry

By Rui Zhao,* Douglas J. Loftus,Dagger Ettore Appella,Dagger and Edward J. Collins*

From the * Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599; and the Dagger  Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892

The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T lymphocyte clone AHIII12.2, recognizes murine H-2Db complexed with peptide p1027 (FAPGVFPYM), as well as human HLA-A2.1 complexed with peptide p1049 (ALWGFFPVL). A commonly proposed model (the molecular mimicry model) used to explain TCR cross-reactivity suggests that the molecular surfaces of the recognized complexes are similar in shape, charge, or both, in spite of the primary sequence differences. To examine the mechanism of xeno-reactivity of AHIII12.2, we have determined the crystal structures of A2/p1049 and Db/p1027 to 2.5 Å and 2.8 Å resolution, respectively. The crystal structures show that the TCR footprint regions of the two class I complexes are significantly different in shape and charge. We propose that rather than simple molecular mimicry, unpredictable arrays of common and differential contacts on the two class I complexes are used for their recognition by the same TCR.

Key words: major histocompatibility complex;  crystallography;  xeno-reactivity;  transplantation;  T cell receptor


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