Stem of SL1 RNA in HIV-1:  Structure and Nucleocapsid Protein Binding for a 1 × 3 Internal Loop†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (18) ◽  
pp. 5259-5269 ◽  
Author(s):  
YiQiong Yuan ◽  
Deborah J. Kerwood ◽  
Andrew C. Paoletti ◽  
Michael F. Shubsda ◽  
Philip N. Borer
Biochemistry ◽  
2009 ◽  
Vol 48 (11) ◽  
pp. 2422-2430 ◽  
Author(s):  
Sergiy V. Avilov ◽  
Julien Godet ◽  
Etienne Piémont ◽  
Yves Mély

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e38905 ◽  
Author(s):  
Ali Bazzi ◽  
Loussiné Zargarian ◽  
Françoise Chaminade ◽  
Hugues De Rocquigny ◽  
Brigitte René ◽  
...  

Virology ◽  
2008 ◽  
Vol 375 (1) ◽  
pp. 148-158 ◽  
Author(s):  
David R. Morcock ◽  
James A. Thomas ◽  
Raymond C. Sowder ◽  
Louis E. Henderson ◽  
Bruce J. Crise ◽  
...  
Keyword(s):  

2002 ◽  
Vol 296 (5) ◽  
pp. 1228-1237 ◽  
Author(s):  
Andrew G Stephen ◽  
Karen M Worthy ◽  
Eric Towler ◽  
Judy A Mikovits ◽  
Shizuko Sei ◽  
...  

2010 ◽  
Vol 2010 ◽  
pp. 1-10 ◽  
Author(s):  
Iris Cadima-Couto ◽  
Joao Goncalves

APOBEC proteins appeared in the cellular battle against HIV-1 as part of intrinsic cellular immunity. The antiretroviral activity of some of these proteins is overtaken by the action of HIV-1 Viral Infectivity Factor (Vif) protein. Since the discovery of APOBEC3G (A3G) as an antiviral factor, many advances have been made to understand its mechanism of action in the cell and how Vif acts in order to counteract its activity. The mainstream concept is that Vif overcomes the innate antiviral activity of A3G by direct protein binding and promoting its degradation via the cellular ubiquitin/proteasomal pathway. Vif may also inhibit A3G through mechanisms independent of proteasomal degradation. Binding of Vif to A3G is essential for its degradation since disruption of this interaction is predicted to stimulate intracellular antiviral immunity. In this paper we will discuss the different binding partners between both proteins as one of the major challenges for the development of new antiviral drugs.


2018 ◽  
Vol 10 (4) ◽  
pp. 463-468 ◽  
Author(s):  
Mattia Mori ◽  
Maria Chiara Dasso Lang ◽  
Francesco Saladini ◽  
Nastasja Palombi ◽  
Lesia Kovalenko ◽  
...  
Keyword(s):  

Biochemistry ◽  
2018 ◽  
Vol 57 (30) ◽  
pp. 4562-4573 ◽  
Author(s):  
Volodymyr Shvadchak ◽  
Sarwat Zgheib ◽  
Beata Basta ◽  
Nicolas Humbert ◽  
Johannes Langedijk ◽  
...  

2002 ◽  
Vol 76 (20) ◽  
pp. 10444-10454 ◽  
Author(s):  
Jielin Zhang ◽  
Clyde S. Crumpacker

ABSTRACT An important aspect of the pathophysiology of human immunodeficiency virus type 1 (HIV-1) infection is the ability of the virus to replicate in the host vigorously without a latent phase and to kill cells with a dynamic turnover of 1.8 × 109 cells/day and 10.3 × 109 virions/24 h. The transcription of HIV-1 RNA in acute infection occurs at two stages; the transcription of viral spliced mRNA occurs early, and the transcription of viral genomic RNA occurs later. The HIV-1 Tat protein is translated from the early spliced mRNA and is critical for HIV-1 genomic RNA expression. The cellular transcription factors are important for HIV-1 early spliced mRNA expression. In this study we show that virion nucleocapsid protein (NC) has a role in expression of HIV-1 early spliced mRNA. The HIV-1 NC migrates from the cytoplasm to the nucleus and accumulates in the nucleus at 18 h postinfection. Mutations on HIV-1 NC zinc fingers change the pattern of early viral spliced mRNA expression and result in a delayed expression of early viral mRNA in HIV-infected cells. This delayed HIV-1 early spliced mRNA expression occurs after proviral DNA has been integrated into the cellular genome, as shown by a quantitative integration assay. These results show that virion NC plays an important role in inducing HIV-1 early mRNA expression and contributes to the rapid viral replication that occurs during HIV-1 infection.


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