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J Virol, April 1998, p. 3412-3417, Vol. 72, No. 4
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Mutations of the Human Immunodeficiency Virus Type 1 p6Gag Domain Result in Reduced Retention of Pol Proteins during Virus Assembly

Xiao-Fang Yu,1,* Liza Dawson,1 Chun-Juan Tian,1 Charles Flexner,2 and Markus Dettenhofer1

Department of Molecular Microbiology and Immunology, Johns Hopkins University School of Hygiene and Public Health,1 and Department of Medicine and Pharmacology and Molecular Sciences,2 Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Received 29 October 1997/Accepted 12 January 1998

One of the crucial steps in the assembly of the human immunodeficiency virus type 1 (HIV-1) and other retroviruses is the incorporation and retention of all the key viral enzymes in released virions. The viral enzymes protease, reverse transcriptase, and integrase of HIV-1 are initially synthesized as Gag-Pol fusion polyproteins. It has been shown that the incorporation of Gag-Pol polyproteins during virus assembly requires the Gag domains that are shared by the Gag and Gag-Pol precursors. We now report that truncation of the C-terminal p6 domain of HIV-1 Gag, which is present in the Gag precursor but not in the Gag-Pol precursor, drastically reduced the amount of Pol proteins in the mutant virions. Mutations in the lentivirus conserved motif P(T/S)APP in p6 also drastically reduced the amount of Pol proteins in mutant virions. The steady-state levels of Gag-Pol precursors and cleaved Pol proteins in the transfected cells were not affected by mutations in p6. The incorporation of unprocessed Gag-Pol precursors into p6 mutant virions was detected when the viral protease was mutated, suggesting that the interactions among mutant Gag molecules and Gag-Pol precursors were not significantly affected. These results suggest that the p6 domain of HIV-1 Gag may play an important role in recruiting or retaining cleaved Pol proteins during virus assembly.

* Corresponding author. Mailing address: Department of Molecular Microbiology and Immunology, The Johns Hopkins University School of Hygiene and Public Health, Baltimore, MD 21205. Phone: (410) 955-3768. Fax: (410) 614-8263. E-mail: xfyu{at}jhsph.edu.




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