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*
Research Department and
Institute for Pathology, Cantonal Hospital St. Gallen, St. Gallen, Switzerland; and
Institute of Experimental Immunology, Department of Pathology, University Hospital Zurich, Zurich, Switzerland
The proteasome is critically involved in the production of MHC
class I-restricted T cell epitopes. Proteasome activity and epitope
production are altered by IFN-
treatment, which leads to a gradual
replacement of constitutive proteasomes by immunoproteasomes in vitro.
However, a quantitative analysis of changes in the steady state subunit
composition of proteasomes during an immune response against viruses or
bacteria in vivo has not been reported. Here we show that the infection
of mice with lymphocytic choriomeningitis virus or
Listeria monocytogenes leads to an almost
complete replacement of constitutive proteasomes by immunoproteasomes
in the liver within 7 days. Proteasome replacements were markedly
reduced in IFN--/- mice, but were only slightly
affected in IFN-
R-/- and perforin-/-
mice. The proteasome regulator PA28/
was up-regulated, whereas
PA28 was reduced in the liver of lymphocytic choriomeningitis
virus-infected mice. Proteasome replacements in the liver strongly
altered proteasome activity and were unexpected to this extent, since
an in vivo half-life of 12 days had been previously assigned to
constitutive proteasomes in the liver. Our results suggest that during
the peak phase of viral and bacterial elimination the antiviral
cytotoxic T lymphocyte response is directed mainly to
immunoproteasome-dependent T cell epitopes, which would be a novel
parameter for the design of vaccines.
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