title: Effects of deletion and overexpression of the Autographa californica nuclear polyhedrosis virus FP25K gene on synthesis of two occlusion-derived virus envelope proteins and their transport into virus-induced intranuclear membranes.
abstract: Partial deletions within Autographa californica open reading frame 61 (FP25K) alter the expression and accumulation profile of several viral proteins and the transport of occlusion-derived virus (ODV)-E66 to intranuclear membranes during infection (S. C. Braunagel et al., J. Virol. 73:8559-8570, 1999). Here we show the effects of a full deletion and overexpression of FP25K on the transport and expression of two ODV envelope proteins, ODV-E66 (E66) and ODV-E25 (E25). Deletion and overexpression of FP25K substantially altered the levels of expression of E66 during infection. Compared with cells infected with wild-type (wt) virus, the levels of E66 were reduced fivefold in cells infected with a viral mutant lacking FP25K (DeltaFP25K) and were slightly increased in cells infected with a viral mutant overexpressing FP25K (FP25K(polh)). In contrast, no significant changes were observed in the levels of E25 among wt-, DeltaFP25K-, and FP25K(polh)-infected cells. The changes observed in the levels of E66 among the different viral mutants were not accompanied by changes in either the time of synthesis, membrane association, protein turnover, or steady-state transcript abundance. Deletion of FP25K also substantially altered the transport and localization of E66 during infection. In cells infected with the DeltaFP25K mutant virus, E66 accumulated in localized regions at the nuclear periphery and the outer nuclear membrane and did not traffic to intranuclear membranes. In contrast, in cells infected with the FP25K(polh) mutant virus E66 trafficked to intranuclear membranes. For comparison, E25 was normally transported to intranuclear membranes in both DeltaFP25K- and FP25K(polh)-infected cells. Altogether these studies suggest that FP25K affects the synthesis of E66 at a posttranscriptional level, probably by altering the translation of E66; additionally, the block in transport of E66 at the nuclear envelope in DeltaFP25K-infected cells suggests that the pathway of E66 trafficking to the inner nuclear membrane and intranuclear microvesicles is specifically regulated and must be influenced by factors that do not control the traffic of E25.
authors.affiliation: Department of Entomology, Texas A&M University, College Station, Texas 77843-2475, USA.
authors.forename: G
authors.initials: G
authors.lastname: Rosas-Acosta
authors.forename: S C
authors.initials: SC
authors.lastname: Braunagel
authors.forename: M D
authors.initials: MD
authors.lastname: Summers
mesh_terms: D000818:Animals; D001483:Base Sequence; D001692:Biological Transport; D002478:Cells, Cultured; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000378:metabolism*; D019590:Nucleocapsid Proteins / Q000235:genetics* / Q000502:physiology; D017924:Nucleopolyhedroviruses / Q000235:genetics / Q000378:metabolism*; D011233:Precipitin Tests; D012333:RNA, Messenger / Q000032:analysis; D018411:Spodoptera; D014759:Viral Envelope Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*
chemical_list: C121638:FP25K protein, Autographa californica nucleopolyhedrovirus; D019590:Nucleocapsid Proteins; D012333:RNA, Messenger; D014759:Viral Envelope Proteins