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

The N-terminal hydrophobic sequence of Autographa californica nucleopolyhedrovirus PIF-3 is... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

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

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Publisher
Springer-Verlag
Copyright
Copyright © 2007 by Springer-Verlag
Subject
Biomedicine; Virology; Medical Microbiology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-007-1012-3
Publisher site
See Article on Publisher Site

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.

Journal

Archives of VirologySpringer Journals

Published: Oct 1, 2007

References

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