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Journal of Virology, October 2000, p. 9727-9731, Vol. 74, No. 20
Heinrich-Pette-Institut, D-20251 Hamburg,
Germany,1 and Laboratory of Viral
Diseases, National Institute of Allergy and Infectious Diseases,
Bethesda, Maryland 0892-04602
Received 7 March 2000/Accepted 18 April 2000
Viral protein R (Vpr) of human immunodeficiency virus type 1 (HIV-1) is a small accessory protein involved in the nuclear import of
viral DNA and the growth arrest of host cells. Several studies have
demonstrated that a significant amount of Vpr is incorporated into the
virus particle via interaction with the p6 domain of Gag, and it is
generally assumed that Vpr is packaged in equimolar ratio to Gag. We
have quantitated the relative amount of Vpr in purified virions
following [35S]cysteine labeling of infected MT-4 cells,
as well as by quantitative immunoblotting and found that Vpr is present
in a molar ratio of approximately 1:7 compared to capsid. Analysis of
isolated core particles showed that Vpr is associated with the mature
viral core, despite quantitative loss of p6 from core preparations. Metabolic labeling of infected cells with
ortho[32P]phosphate revealed that a small fraction of Vpr
is phosphorylated in virions and infected cells.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Human Immunodeficiency Virus Type 1 Vpr Protein Is
Incorporated into the Virion in Significantly Smaller Amounts than Gag
and Is Phosphorylated in Infected Cells
*
Corresponding author. Present address: Abteilung
Virologie, Universität Heidelberg, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany. Phone: 49-6221-565002. Fax:
49-6221-565003. E-mail:Barbara_Mueller{at}med.uni-heidelberg.de.
Present address: Abteilung Virologie, Universität Heidelberg,
D-69120 Heidelberg, Germany.
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