trans-acting proteins involved in RNA encapsidation and viral assembly in human immunodeficiency virus type 1.
AUTOR(ES)
Kaye, J F
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=189891Documentos Relacionados
- Analysis of trans-acting response decoy RNA-mediated inhibition of human immunodeficiency virus type 1 transactivation.
- Cell type specific trans-acting factors are involved in alternative splicing of human fibronectin pre-mRNA.
- cis elements and trans-acting factors involved in dimer formation of murine leukemia virus RNA.
- Subcellular localization of the human immunodeficiency virus trans-acting art gene product.
- cis- and trans-acting elements involved in reactivation of vaccinia virus early transcription.