Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: facilitated trafficking to the inner nuclear membrane. Academic Article uri icon

abstract

  • The N-terminal 33 aa of the envelope protein ODV-E66 are sufficient to traffic fusion proteins to intranuclear membranes and the ODV envelope during infection with Autographa californica nucleopolyhedrovirus. This sequence has two distinct features: (i) an extremely hydrophobic sequence of 18 aa and (ii) positively charged amino acids close to the C-terminal end of the hydrophobic sequence. In the absence of infection, this sequence is sufficient to promote protein accumulation at the inner nuclear membrane. Covalent cross-linking results show that the lysines of the motif are proximal to FP25K and/or BV/ODV-E26 during transit from the endoplasmic reticulum to the nuclear envelope. We propose that the 33 aa comprise a signature for sorting proteins to the inner nuclear membrane (sorting motif) and that, unlike other resident proteins of the inner nuclear membrane, ODV-E66 and sortingmotif fusions do not randomly diffuse from their site of insertion at the endoplasmic reticulum to the nuclear envelope and viral-induced intranuclear membranes. Rather, during infection, trafficking is mediated by protein-protein interactions.

published proceedings

  • Proc Natl Acad Sci U S A

altmetric score

  • 3

author list (cited authors)

  • Braunagel, S. C., Williamson, S. T., Saksena, S., Zhong, Z., Russell, W. K., Russell, D. H., & Summers, M. D.

citation count

  • 76

complete list of authors

  • Braunagel, Sharon C||Williamson, Shawn T||Saksena, Suraj||Zhong, Zhenping||Russell, William K||Russell, David H||Summers, Max D

publication date

  • June 2004