ArticleProceedings of the National Academy of Sciences of the United States of America2004
Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: facilitated trafficking to the inner nuclear membrane.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Identification of the nucleolar localization signal inThe Journal of general virology · 2026Article
- Autographa californica multiple nucleopolyhedrovirusJournal of virology · 2026Article
- Autographa californica multiple nucleopolyhedrovirusJournal of virology · 2024Article
- The Membrane-Anchoring Region of the AcMNPV P74 Protein Is Expendable or Interchangeable with Homologs from Other Species.Viruses · 2021Article
- Lamin is essential for nuclear localization of the GPI synthesis enzyme PIG-B and GPI-anchored protein production inJournal of cell science · 2020Article
- Autographa Californica Multiple Nucleopolyhedrovirus P48 (Ac103) Is Required for the Efficient Formation of Virus-Induced Intranuclear Microvesicles.Virologica Sinica · 2019Article
- The first clawed lobster virus Homarus gammarus nudivirus (HgNV n. sp.) expands the diversity of the Nudiviridae.Scientific reports · 2019Article
- BaculovirusJournal of virology · 2019Article
- An Advanced View on BaculovirusInsects · 2018Review
- Baculovirus infection induces disruption of the nuclear lamina.Scientific reports · 2017Article
- Live imaging and modeling of inner nuclear membrane targeting reveals its molecular requirements in mammalian cells.The Journal of cell biology · 2015Article
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- Autographa californica Nucleopolyhedrovirus Ac76: a dimeric type II integral membrane protein that contains an inner nuclear membrane-sorting motif.Journal of virology · 2014Article
- The baculovirus core gene ac83 is required for nucleocapsid assembly and per os infectivity of Autographa californica nucleopolyhedrovirus.Journal of virology · 2013Article
- Effects of Early or Overexpression of the Autographa californica Multiple Nucleopolyhedrovirus orf94 (ODV-e25) on Virus Replication.PloS one · 2013Article
- Identification and characterization of host factors interacting with Bombyx mori nucleopolyhedrovirus ORF8.Journal of microbiology (Seoul, Korea) · 2012Article
- Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway.The Journal of biological chemistry · 2012Article
- Complete sequence, analysis and organization of the Orgyia leucostigma nucleopolyhedrovirus genome.Viruses · 2011Article
- Baculovirus envelope protein ODV-E66 is a novel chondroitinase with distinct substrate specificity.The Journal of biological chemistry · 2011Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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