: Background: Cytotoxic T lymphocytes and Kupffer cells are essential components of the immune response during liver diseases. Recent studies have highlighted the role of cytotoxic T lymphocytes using Fas and its ligand in induced hepatocyte death during acute and chronic hepatitis. Methods: In the present work, the main purpose was to investigate perforin and granzyme B expression in liver biopsies of patients with chronic hepatitis (10 HBV, 14 HCV and 10 autoimmune hepatitis) using immunohistochemistry. The liver biopsies of two normal individuals were also studied in the same conditions. Results: Few intrahepatic T lymphocytes expressed perforin and granzyme B, while a large number of Kupffer cells were positive for both proteins in all the patients tested. The co‐localization of perforin and granzyme B, and CD3 or CD68 antigens was visualized, respectively, in T cells and Kupffer cells, using confocal microscopy. In situ hybridization assays confirmed that perforin and granzyme B mRNAs were present in the liver during chronic hepatitis. The results were similar among the three groups of patients and whatever the activity of the disease. Perforin and granzyme B expression was lacking in liver samples from normal individuals. Conclusions: These data suggest a minor role for the T cell‐mediated perforin/granzyme B death pathway, and a putative role for Kuppfer cells via lytic protein release, during chronic hepatitis.
Three monoclonal antibodies, termed 4E10, lE11:10, and 2D9:1, were generated against rubella virus. lmmunoblot analysis with purified authentic rubella virus or recombinant baculovirus-expressed rubella virus structural proteins El, E2, and C demonstrated that they were directed against the El envelope glycoprotein of the rubella virus particle. By using the yeast Ty virus-like particle system, it was possible to map the binding site of lE11:10 within amino acids 236 to 286 of the El protein and the binding sites of 2D9:1 and 4E10 outside this region. Immunoaffinity purification with these monoclonal antibodies made it evident that they are useful for obtaining large quantities of pure baculovirus-expressed rubella virus envelope protein El. The diagnostic potential of this immunoaffinity-purified recombinant rubella virus El protein compared with that of authentic rubella virus is demonstrated.
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