The N-terminal hydrophobic sequence of Autographa californica nucleopolyhedrovirus PIF-3 is essential for oral infection

Abstract

The Autographa californica nucleopolyhedrovirus (AcMNPV) open reading frame 115 has been identified as a per os infection factor (pif-3) and is essential for oral infection. Here, we have characterized the pif-3 of AcMNPV in more detail. The pif-3 transcripts were detected from 12 to 96 h post-infection (hpi) in Sf9 cells infected with AcMNPV. Polyclonal antiserum first recognized a 25-kDa protein at 36 hpi. Western blot analysis indicated that PIF-3 is a component of occlusion-derived virus but not of budded virus. The subcellular localization demonstrated that the 21-amino-acid (aa) N-terminal hydrophobic domain of PIF-3, which is conserved in PIF-1, PIF2 and PIF-3, acts as a nuclear location signal and is essential for trafficking the protein to the nucleus. Deletion of either pif-3 or the 21-aa N-terminal hydrophobic domain of pif-3 from AcMNPV abolished per os infectivity but had no effect on the infectivity of the budded virus phenotype.