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Journal of Virology, June 2000, p. 5395-5402, Vol. 74, No. 12
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

Molly A. Accola,1,2 Bettina Strack,1 and Heinrich G. Göttlinger1,3,*

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.

* 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.

Journal of Virology, June 2000, p. 5395-5402, Vol. 74, No. 12
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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