scholarly journals Conditional Human Immunodeficiency Virus Transactivator of Transcription Protein Expression Induces Depression-like Effects and Oxidative Stress

2017 ◽  
Vol 2 (7) ◽  
pp. 599-609 ◽  
Author(s):  
Jay P. McLaughlin ◽  
Jason J. Paris ◽  
Dionyssios Mintzopoulos ◽  
Kristen A. Hymel ◽  
Jae K. Kim ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Human Immunodeficiency Virus ◽  
Protein Expression ◽  
Immunodeficiency Virus ◽  
Transactivator Of Transcription ◽  
And Oxidative Stress

scholarly journals Double-Stranded RNA Adenosine Deaminases Enhance Expression of Human Immunodeficiency Virus Type 1 Proteins

2008 ◽  
Vol 82 (21) ◽  
pp. 10864-10872 ◽  
Author(s):  
Angsana Phuphuakrat ◽  
Romchat Kraiwong ◽  
Chompunuch Boonarkart ◽  
Darat Lauhakirti ◽  
Tun-Hou Lee ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Protein Expression ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Structural Protein ◽  
Double Stranded Rna ◽  
Adenosine Deaminases ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT ADARs (adenosine deaminases that act on double-stranded RNA) are RNA editing enzymes that catalyze a change from adenosine to inosine, which is then recognized as guanosine by translational machinery. We demonstrate here that overexpression of ADARs but not of an ADAR mutant lacking editing activity could upregulate human immunodeficiency virus type 1 (HIV-1) structural protein expression and viral production. Knockdown of ADAR1 by RNA silencing inhibited HIV-1 production. Viral RNA harvested from transfected ADAR1-knocked-down cells showed a decrease in the level of unspliced RNA transcripts. Overexpression of ADAR1 induced editing at a specific site in the env gene, and a mutant with the edited sequence was expressed more efficiently than the wild-type viral genome. These data suggested the role of ADAR in modulation of HIV-1 replication. Our data demonstrate a novel mechanism in which HIV-1 employs host RNA modification machinery for posttranscriptional regulation of viral protein expression.

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