{'fraction_non_alphanumeric': 0.025150905432595575, 'fraction_numerical': 0.008048289738430584, 'mean_word_length': 6.107142857142857, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
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‐κB transcription factor inhibitors, IκBs. The CsIV vankyrin proteins are thought to be involved in the suppression of NF‐κB 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.