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Journal of Virology, November 2001, p. 10829-10842, Vol. 75, No. 22
Department of
Entomology1 and Department of
Biochemistry and Biophysics,3 Texas A&M
University, and Texas Agriculture Experimental
Station,2 College Station, Texas
77843-2475
Received 12 April 2001/Accepted 11 August 2001
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 (
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.22.10829-10842.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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
FP25K) and were slightly
increased in cells infected with a viral mutant overexpressing FP25K
(FP25Kpolh). In contrast, no significant
changes were observed in the levels of E25 among wt-,
FP25K-, and
FP25Kpolh-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
FP25K 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
FP25Kpolh mutant virus E66 trafficked to
intranuclear membranes. For comparison, E25 was normally transported to
intranuclear membranes in both
FP25K- and
FP25Kpolh-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
FP25K-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.
*
Corresponding author. Mailing address: Department of
Entomology, Texas A&M University, College Station, TX 77843-2475. Phone: (979) 847-9036. Fax: (979) 845-8934. E-mail:
m-summers{at}tamu.edu.
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