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A more recent version of this article appeared on December 7, 2001
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M109231200v1
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Papers In Press, published online ahead of print October 2, 2001
J. Biol. Chem, 10.1074/jbc.M109231200
Submitted on September 24, 2001
Revised on October 2, 2001
Accepted on October 2, 2001

T cell activity correlates with oligomeric peptide/MHC binding on T cell surface

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

Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7290

Corresponding Author: collins1{at}med.unc.edu

Recognition of virally infected cells by CD8+ T cells requires differentiation between self and non-self 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 (allo) or different species (xeno-transplant). 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 Db molecule (Db). Recognition of both A2 and Db 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 TcR. However, contrary to previous studies, we see similar half-lives for the pMHC multimers bound to the AHIII12.2 cell surface.


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