scholarly journals Viral protein R of human immunodeficiency virus types 1 and 2 is dispensable for replication and cytopathogenicity in lymphoid cells.

1989 ◽  
Vol 63 (7) ◽  
pp. 3205-3208 ◽  
Author(s):  
D Dedera ◽  
W Hu ◽  
N Vander Heyden ◽  
L Ratner
2014 ◽  
Vol 3 (4) ◽  
pp. 104
Author(s):  
Vivek Darapaneni

<p>The viral protein R (Vpr) plays a pivotal role in the infectious lifecycle of human immunodeficiency virus-1. The objective of this study is to find the degree of conservation of Vpr and to detect conserved binding sites, which might be used as target sites for potential anti-Vpr drugs. The conservation analysis was based on 5301 amino acid sequences identified novel conserved and highly conserved sites.  The novel conserved sites which have been identified are: Leu42, Gly43 and Val57; Arg73 and Cys76; Glu24, His33, Cys76 and Ser79.<strong> </strong>The outcome of this study provide the foundation for developing anti-Vpr drugs which have abridged potential to induce drug resistance through mutations.</p>


2000 ◽  
Vol 74 (12) ◽  
pp. 5424-5431 ◽  
Author(s):  
Antoine Kichler ◽  
Jean-Christophe Pages ◽  
Christian Leborgne ◽  
Sabine Druillennec ◽  
Christine Lenoir ◽  
...  

ABSTRACT Viral protein R (Vpr) of human immunodeficiency virus type 1 is produced late in the virus life cycle and is assembled into the virion through binding to the Gag protein. It is known to play a significant role early in the viral life cycle by facilitating the nuclear import of the preintegration complex in nondividing cells. Vpr is also able to interact with nucleic acids, and we show here that it induces condensation of plasmid DNA. We have explored the possibility of using these properties in DNA transfection experiments. We report that the C-terminal half of the protein (Vpr52–96) mediates DNA transfection in a variety of human and nonhuman cell lines with efficiencies comparable to those of the best-known transfection agents. Compared with polylysine, a standard polycationic transfection reagent, Vpr52–96 was 10- to 1,000-fold more active. Vpr52–96-DNA complexes were able to reach the cell nucleus through a pH-independent mechanism. These observations possibly identify an alternate pathway for DNA transfection.


2008 ◽  
Vol 01 (02) ◽  
pp. 073-076 ◽  
Author(s):  
Seenivasagan Renganathan ◽  
Kasimani Renganathan ◽  
Marimuthu Parthiban ◽  
Kalidoss Ramamoorthy ◽  
Shanmughavel Piramanayagam

2000 ◽  
Vol 74 (24) ◽  
pp. 12003-12003
Author(s):  
Antoine Kichler ◽  
Jean-Christophe Pages ◽  
Christian Leborgne ◽  
Sabine Druillennec ◽  
Christine Lenoir ◽  
...  

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