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*
Department of Molecular Immunology, German Cancer Research Center (Deutsches Krebsforschungszentrum), Heidelberg, Germany;
Basel Institute for Immunology, Basel, Switzerland; and
Department of Immunology, Hebrew University, Ein-Karem, Jerusalem, Israel
The ER protein tapasin (Tpn) forms a bridge between MHC
class I H chain (HC)/
2-microglobulin and the TAP peptide
transporter. The function of this TAP-associated complex was unclear
because it was reported that soluble Tpn that has lost TAP interaction
would be fully competent in terms of peptide loading and Ag
presentation. We found, however, that only wild-type human Tpn (hTpn),
but not three soluble hTpn variants, a transmembrane domain point
mutant of hTpn (L410
F), wild-type mouse Tpn, nor a mouse-human Tpn
hybrid, fully up-regulated peptide-dependent Bw4 epitopes when
expressed in Tpn-deficient .220.B*4402 cells. Consistent with
suboptimal peptide loading, the t1/2 of
class I molecules was considerably reduced in the presence of soluble
hTpn, hTpn-L410F, and murine Tpn. Furthermore, eluted peptide spectra
and the class I-mediated inhibition of NK clones showed distinct
differences to the hTpn transfectant. Only wild-type hTpn efficiently
recruited HC and calreticulin (Crt) into complexes with TAP and
endoplasmic reticulum p57 (ERp57). The L410F mutant was defective in
TAP association, but bound to class I molecules, Crt, and ERp57. Mouse
Tpn associated with human TAP and ERp57 on the one hand, and with HC
and Crt on the other, but failed to recruit normal amounts of HLA class
I molecules into the TAP complex. We conclude that the loading with
peptides conferring high stability requires the Tpn-mediated
introduction of HC into the TAP complex, whereas the mere interaction
with Tpn is not sufficient.
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