Journal of Virology, June 2000, p. 5395-5402, Vol. 74, No. 12
Department of Cancer Immunology and AIDS,
Dana-Farber Cancer Institute,1 and
Program in Immunology2 and
Department of Pathology,3 Harvard
Medical School, Boston, Massachusetts 02115
Received 14 September 1999/Accepted 16 March 2000
The human immunodeficiency virus type 1 (HIV-1) Gag precursor
Pr55gag by itself is capable of assembling into
retrovirus-like particles (VLP). In the present study, we attempted to
identify the minimal Gag sequences required for the formation of VLP.
Our results show that about 80% of Pr55gag can
be either deleted or replaced by heterologous sequences without significantly compromising VLP production. The smallest chimeric molecule still able to efficiently form VLP was only about 16 kDa. This
minimal Gag construct contained the leucine zipper domain of the yeast
transcription factor GCN4 to substitute for the assembly function of
nucleocapsid (NC), followed by a P-P-P-P-Y motif to provide late
budding (L) domain function, and retained only the myristylation signal
and the C-terminal capsid-p2 domain of Pr55gag.
We also show that the L domain function of HIV-1
p6gag is not dependent on the presence of an
active viral protease and that the NC domain of
Pr55gag is dispensable for the incorporation of
Vpr into VLP.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Efficient Particle Production by Minimal Gag Constructs Which
Retain the Carboxy-Terminal Domain of Human Immunodeficiency Virus
Type 1 Capsid-p2 and a Late Assembly Domain
*
Corresponding author. Mailing address: Dana-Farber
Cancer Institute, 44 Binney St., Boston, MA 02115. Phone: (617)
632-3067. Fax: (617) 632-3113. E-mail:
Heinrich_Gottlinger{at}DFCI.harvard.edu.
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