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J. Virol., Feb 1996, 880-886, Vol 70, No. 2
Copyright © 1996, American Society for Microbiology

trans-acting proteins involved in RNA encapsidation and viral assembly in human immunodeficiency virus type 1

JF Kaye and AM Lever
Department of Medicine, Addenbrooke's Hospital, Cambridge, United Kingdom.

The human immunodeficiency virus type 1 gag gene product Pr55gag self- assembles when expressed on its own in a variety of eukaryotic systems. Assembly in T lymphocytes has not previously been studied, nor is it clear whether Pr55gag particles can package genomic RNA or if the Gag- Pol polyprotein is required. We have used a series of constructs that express Gag or Gag-Pol proteins with or without the viral protease in transient transfections in COS-1 cells and also expressed stably in CD4+ T cells to study this. Deletion of the p6 domain at the C terminus of protease-negative Pr55gag did not abolish particle release, while truncation of the nucleocapsid protein reduced it significantly, particularly in lymphocytes. Gag-Pol polyprotein was released from T cells in the absence of Pr55gag but did not encapsidate RNA. Pr55gag encapsidated human immunodeficiency virus type 1 RNA whether expressed in a protease-positive or protease-negative context. p6 was dispensable for RNA encapsidation. Marked differences in the level of RNA export were noted between the different cell lines.


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