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Gene Review:

ie2 - ORF131

Epiphyas postvittana nucleopolyhedrovirus

Prikhod'ko, E.A. et al., Murges, D. et al., Imai, N. et al., Prikhod'ko, E.A. et al., Imai, N. et al., et al.

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Disease relevance of ie2

Taken together our results provide first evidence that the early baculovirus protein IE2 associates at least with one component of mammalian PODs during virus infection, suggesting that POD-like structures can be formed in insect cells [1].
Due to its effect on virion occlusion, mutants of IE-2 were essentially noninfectious by the normal route of infection in both species tested [2].
It has previously been reported that Bombyx mori nucleopolyhedrovirus (BmNPV) IE2 has a ubiquitin ligase activity that is dependent on the RING finger domain and that IE2 can oligomerize through its C-terminal coiled-coil region [3].

High impact information on ie2

In vitro ubiquitination assay with the rabbit reticulocyte lysates and BmNPV RING finger proteins fused with maltose-binding protein (MBP) showed that four of them (IAP2, IE2, PE38, and CG30) were polyubiquitinated in the presence of zinc ion [4].
The ability of IE2 to trans stimulate DNA replication and coupled late gene expression is observed in a cell line derived from Spodoptera frugiperda but not in a cell line derived from Trichoplusia ni [2].
Moreover, mutation of a single conserved cysteine (C251) of the RING finger motif abolished the ability of IE2 to block cell cycle progression but had no apparent effect on its transregulatory activity [5].
In contrast, a mutant of IE2 containing a deletion of residues 94 to 173 was able to block cell division but lacked trans-regulatory activity [5].
Transactivation by the chimeric constructs is enhanced synergistically when cotransfected with IE2 into Lymantria dispar and Spodoptera frugiperda cells [6].

Biological context of ie2

Role of baculovirus IE2 and its RING finger in cell cycle arrest [5].
Cotransfection of p39cat and pIE1 with plasmids encoding ORF121, IE2, and P35 stimulated 39cat expression more than 100-fold compared to cells transfected with only p39cat and pIE1 [7].
The transactivator ie-2 stimulated gene expression in the presence of cis-linked enhancer elements and ie-1 in SF-21 cells [8].

Analytical, diagnostic and therapeutic context of ie2

Here, confocal microscopy analysis demonstrated that IE2 formed nuclear foci only during the early phase of infection (2-6 h post-infection) [3].

References

Dynamic nuclear localization of the baculovirus proteins IE2 and PE38 during the infection cycle: the promyelocytic leukemia protein colocalizes with IE2. Murges, D., Quadt, I., Schröer, J., Knebel-Mörsdorf, D. Exp. Cell Res. (2001) [Pubmed]
In vivo and in vitro analysis of baculovirus ie-2 mutants. Prikhod'ko, E.A., Lu, A., Wilson, J.A., Miller, L.K. J. Virol. (1999) [Pubmed]
Formation of Bombyx mori nucleopolyhedrovirus IE2 nuclear foci is regulated by the functional domains for oligomerization and ubiquitin ligase activity. Imai, N., Matsumoto, S., Kang, W. J. Gen. Virol. (2005) [Pubmed]
Ubiquitin ligase activities of Bombyx mori nucleopolyhedrovirus RING finger proteins. Imai, N., Matsuda, N., Tanaka, K., Nakano, A., Matsumoto, S., Kang, W. J. Virol. (2003) [Pubmed]
Role of baculovirus IE2 and its RING finger in cell cycle arrest. Prikhod'ko, E.A., Miller, L.K. J. Virol. (1998) [Pubmed]
Characterization of the acidic domain of the IE1 regulatory protein from Orgyia pseudotsugata multicapsid nucleopolyhedrovirus. Forsythe, I.J., Shippam, C.E., Willis, L.G., Stewart, S., Grigliatti, T., Theilmann, D.A. Virology (1998) [Pubmed]
Mapping of ORF121, a factor that activates baculovirus early gene expression. Gong, M., Jin, J., Guarino, L.A. Virology (1998) [Pubmed]
Effects of baculovirus transactivators IE-1 and IE-2 on the Drosophila heat shock 70 promoter in two insect cell lines. Crouch, E.A., Passarelli, A.L. Arch. Virol. (2005) [Pubmed]

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