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J. Biol. Chem., Vol. 276, Issue 50, 47320-47328, December 14, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/50/47320    most recent M109231200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Buslepp, J. Articles by Collins, E. J. Search for Related Content PubMed PubMed Citation Articles by Buslepp, J. Articles by Collins, E. J. Social Bookmarking                      What's this?

T Cell Activity Correlates with Oligomeric Peptide-Major Histocompatibility Complex Binding on T Cell Surface^*

Jennifer Buslepp^§, Rui Zhao^§¶, Debora Donnini^**, Douglas Loftus, Mohamed Saad^¶, Ettore Appella, and Edward J. Collins^¶§§

From the ^¶ Department of Microbiology and Immunology,  Department of Biochemistry and Biophysics, and  Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 275992 and the  Laboratory of Cell Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892

Recognition of virally infected cells by CD8⁺ T cells requires differentiation between self and nonself peptide-class I major histocompatibility complexes (pMHC). Recognition of foreign pMHC by host T cells is a major factor in the rejection of transplanted organs from the same species (allotransplant) or different species (xenotransplant). AHIII12.2 is a murine T cell clone that recognizes the xenogeneic (human) class I MHC HLA-A2.1 molecule (A2) and the syngeneic murine class I MHC H-2 D^b molecule (D^b). Recognition of both A2 and D^b are peptide-dependent, and the sequences of the peptides recognized have been determined. Alterations in the antigenic peptides bound to A2 cause large changes in AHIII12.2 T cell responsiveness. Crystal structures of three representative peptides (agonist, null, and antagonist) bound to A2 partially explain the changes in AHIII12.2 responsiveness. Using class I pMHC octamers, a strong correlation is seen between T cell activity and the affinity of pMHC complexes for the T cell receptor. However, contrary to previous studies, we see similar half-lives for the pMHC multimers bound to the AHIII12.2 cell surface.

The atomic coordinates and the structure factors (code 1I7R (A2-p1058), 1I7T (A2-p1049-F5V), and 1I7U (A2-p1059-F6V)) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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