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*
Department of Microbiology and Immunology and
School of Dental Science, University of Melbourne, and
Biomolecular Research Institute, Parkville, Victoria, Australia;
Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Facultad de Ciencias, Madrid, Spain;
¶ Queensland Institute of Medical Research, Brisbane, Queensland, Australia; and
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Department of Immunology, Allergy, and Arthritis, Flinders University of South Australia, Bedford Park, South Australia, Australia
Tapasin is critical for efficient loading and surface expression of
most HLA class I molecules. The high level surface expression of
HLA-B*2705 on tapasin-deficient 721.220 cells allowed the influence of
this chaperone on peptide repertoire to be examined. Comparison of
peptides bound to HLA-B*2705 expressed on tapasin-deficient and
-proficient cells by mass spectrometry revealed an overall reduction in
the recovery of B*2705-bound peptides isolated from tapasin-deficient
cells despite similar yields of B27 heavy chain and
2-microglobulin. This indicated that a proportion of
suboptimal ligands were associated with B27, and they were lost during
the purification process. Notwithstanding this failure to recover these
suboptimal peptides, there was substantial overlap in the repertoire
and biochemical properties of peptides recovered from B27 complexes
derived from tapasin-positive and -negative cells. Although many
peptides were preferentially or uniquely isolated from B*2705 in
tapasin-positive cells, a number of species were preferentially
recovered in the absence of tapasin, and some of these peptide ligands
have been sequenced. In general, these ligands did not exhibit
exceptional binding affinity, and we invoke an argument based on
lumenal availability and affinity to explain their tapasin
independence. The differential display of peptides in tapasin-negative
and -positive cells was also apparent in the reactivity of
peptide-sensitive alloreactive CTL raised against tapasin-positive and
-negative targets, demonstrating the functional relevance of the
biochemical observation of changes in peptide repertoire in the
tapasin-deficient APC. Overall, the data reveal that tapasin
quantitatively and qualitatively influences ligand selection by class I
molecules.
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