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M9640644.TXT
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1996-03-04
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Document 0644
DOCN M9640644
TI trans-acting proteins involved in RNA encapsidation and viral assembly
in human immunodeficiency virus type 1.
DT 9604
AU Kaye JF; Lever AM; Department of Medicine, Addenbrooke's Hospital,
Cambridge, United; Kingdom.
SO J Virol. 1996 Feb;70(2):880-6. Unique Identifier : AIDSLINE MED/96135198
AB 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.
DE Amino Acid Sequence Animal Binding Sites Cell Line Gene Products,
gag/GENETICS/*PHYSIOLOGY Gene Products, pol/GENETICS/PHYSIOLOGY Genes,
gag Human HIV-1/GENETICS/*PHYSIOLOGY Molecular Sequence Data
Mutation Protein Precursors/GENETICS/*PHYSIOLOGY RNA,
Viral/*METABOLISM Support, Non-U.S. Gov't
Trans-Activators/GENETICS/*PHYSIOLOGY Virion/METABOLISM Virus
Assembly/*PHYSIOLOGY JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).