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Background The mechanisms responsible for the HCV escape to the immune system remain largely unknown. A strict interaction between NS3, a non-structural protein of HCV, and the LMP-7, a subunit of the immunoproteasome, has been described suggesting that this may result in an impaired antigen presentation. Proteasomes are intracellular multicatalytic complexes whose primary function is the degradation of abnormal or foreign proteins. In particular, they regulate the presentation of viral antigens onto MHC I molecules. The 26S proteasome has a 20S catalytic core and two 19S regulatory complexes. Three subunits (β1, β2 and β5) are responsible for the main proteasomal peptidase activities (PGPH, trypsin-like, and chymotrypsin-like activity, respectively). With certain cytokines, such as interferon-γ (IFN-γ), the three β subunits of the standard proteasome (PS) are replaced by inducible subunits (LMP-2, MECL-1 and LMP-7) to form the immunoproteasome (IP), which improves the antigen processing and presentation.

The switch from the standard proteasome to the immuno proteasome in the mononuclear cells of children with vertically acquired HCV infection