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Journal of Virology, August 1999, p. 6691-6699, Vol. 73, No. 8
Departments of Entomology and Genetics, The
University of Georgia, Athens, Georgia 30602
Received 22 February 1999/Accepted 17 May 1999
While studying apoptosis induced by baculovirus transactivator IE1
in SF-21 cells, we found that the levels of IE1-induced apoptosis were
increased approximately twofold upon cotransfection with the
baculovirus early pe38 gene. However, no apoptotic activity was observed in cells transfected with pe38 alone, even
when placed under the control of a constitutive promoter. Thus,
pe38 was able to augment IE1-induced apoptosis but was
unable to induce apoptosis when expressed in SF-21 cells alone. PE38,
the full-length product of pe38, is a nuclear protein with
RING finger and leucine zipper motifs. Deletion of the amino-terminal
region, which contains a putative nuclear localization motif, resulted
in cytoplasmic localization of the PE38 mutants. These N-terminal
deletion mutants were unable to enhance IE1-induced apoptosis. Mutation
of a single conserved leucine (L242) of the leucine zipper motif also
eliminated the ability of PE38 to augment apoptosis induced by IE1. In
contrast, PE38 mutants with alanine substitutions for conserved
cysteine residues (C109 or C138) of the RING finger motif were able to increase IE1-induced apoptosis to levels equivalent to those of wild-type PE38. We propose that PE38 is one of at least two viral factors which collectively evoke a cellular apoptotic response during
baculovirus infection.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Baculovirus PE38 Protein Augments Apoptosis
Induced by Transactivator IE1
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Corresponding author. Mailing address: Department of
Entomology, University of Georgia, 413 Biological Science Building,
Athens, GA 30602-2603. Phone: (706) 542-2294. Fax: (706) 542-2279. E-mail: miller{at}arches.uga.edu.
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