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*
Institute of Biochemistry, Charité, Humboldt University, Berlin, Germany; and
Department of Immunohematology and Blood Bank, Leiden University Medical Center, Leiden, The Netherlands
Proteasomes are the major source for the generation of peptides
bound by MHC class I molecules. To study the functional relevance of
the IFN-
-inducible proteasome subunits low molecular mass protein 2
(LMP2), LMP7, and mouse embryonal cell (MEC) ligand 1 in Ag processing
and concomitantly that of immunoproteasomes, we established the
tetracycline-regulated mouse cell line MEC217, allowing the titrable
formation of immunoproteasomes. Infection of MEC217 cells with
Adenovirus type 5 (Ad5) and analysis of Ag presentation with
Ad5-specific CTL showed that cells containing immunoproteasomes
processed the viral early 1B protein (E1B)-derived epitope
E1B192–200 with increased efficiency, thus allowing a
faster detection of viral entry in induced cells. Importantly, optimal
CTL activation was already achieved at submaximal immunosubunit
expression. In contrast, digestion of E1B-polypeptide with purified
proteasomes in vitro yielded E1B192–200 at quantities that
were proportional to the relative contents of immunosubunits. Our data
provide evidence that the IFN--inducible proteasome subunits, when
present at relatively low levels as at initial stages of infection,
already increase the efficiency of antigenic peptide generation and
thereby enhance MHC class I Ag processing in infected
cells.
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