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Departments of
*
Biochemistry and Molecular Biology, and
Immunology, Biochemistry, and Molecular Biology, Mayo Clinic/Foundation, Rochester, MN 55905
The influence of TAP-MHC class I interactions on peptide binding to
the class I heavy chain is assessed during TAP-dependent assembly using
Kb-specific Abs that recognize conformational changes
induced by assembly with ß2-microglobulin
(ß2m) and by peptide binding. A significant portion
(45%) of Kb molecules in TAP+, RMA-derived
microsomes are associated with the TAP complex as measured by
coimmunoisolation of Kb using anti-TAP1 Abs, while only
20% of the Kb heavy chain molecules are isolated as
Kbß2m complexes with the
-Kb-specific Abs, Y-3 or K-10-56. The amount of
Kb isolated with Y-3 and K-10-56 increases in proportion to
transport and binding of peptide to the Kb molecules within
the RMA microsomes. In contrast, less than 5% of the Kb
within TAP2-RMA-S microsomes associated with the remaining TAP1
subunit. However, greater than 60% of Kb heavy chain is
isolated as K-10-56- and Y-3-reactive Kbß2m
complexes. We propose that a TAP-MHC class I interaction serves to
stabilize the MHC class I:ß2m complex in an immature
conformation (Y-3 and K-10-56 nonreactive) prior to high affinity
peptide binding, preventing the export of class I molecules complexed
with low affinity peptide ligands from the ER.
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