The Campoletis sonorensis ichnovirus vankyrin protein P-vank-1 inhibits apoptosis in insect Sf9 cells.

The Campoletis sonorensis ichnovirus (CsIV) vankyrin genes encode proteins containing truncated ankyrin repeat domains with sequence homology to the inhibitory domains of NF-kappaB transcription factor inhibitors, IkappaBs. The CsIV vankyrin proteins are thought to be involved in the suppression of NF-kappaB activity during immune response and/or developmental events in the parasitized host. Here we report that when P-vank-1 was expressed stably from Sf9 cells, prolonged survival of these cells was observed after baculovirus infection, UV irradiation, and treatment with the apoptosis-inducing chemical camptothecin compared to untransformed Sf9 cells. Furthermore, P-vank-1 inhibited nuclear and internucleosomal degradation and caspase activity after induction of apoptosis in Sf9 cells stably expressing P-vank-1. This is the first report of a polydnavirus protein with anti-apoptotic function.