Abstract
Perforin, a potent pore-forming protein, plays an important role in killer lymphocyte-mediated cytolysis. The studies on perforin, although already extensive, have been hampered by the limited amount of perforin naturally available from killer lymphocytes. In the present study, a full-length mouse perforin was expressed in insect cells using recombinant baculovirus. Recombinant perforin appeared to be functional in terms of lysing erythrocytes and nucleated target cells. These results suggest that the recombinant DNA approach developed in the present study may offer a new way for preparing sufficient amounts of engineered perforin for use in the studies aimed at dissecting the functional domains of the perforin molecule.
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