Binding of the Nucleocapsid Protein of Type 1 Human Immunodeficiency Virus to Nucleic Acids Studied Using Phosphorescence and Optically Detected Magnetic Resonance†

Biochemistry ◽  
1997 ◽  
Vol 36 (41) ◽  
pp. 12506-12518 ◽  
Author(s):  
Jie Q. Wu ◽  
Andrzej Ozarowski ◽  
August H. Maki ◽  
Maria A. Urbaneja ◽  
Louis E. Henderson ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Magnetic Resonance ◽  
Nucleic Acids ◽  
Nucleocapsid Protein ◽  
Immunodeficiency Virus ◽  
Optically Detected Magnetic Resonance ◽  
Optically Detected

scholarly journals Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Nuclear Localization Mediates Early Viral mRNA Expression

2002 ◽  
Vol 76 (20) ◽  
pp. 10444-10454 ◽  
Author(s):  
Jielin Zhang ◽  
Clyde S. Crumpacker
Keyword(s):  
Human Immunodeficiency Virus ◽  
Mrna Expression ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Nucleocapsid Protein ◽  
Viral Mrna ◽  
Genomic Rna ◽  
Immunodeficiency Virus ◽  
Hiv 1

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.

The Vpr Protein of Human Immunodeficiency Virus Type 1 Binds to Nucleocapsid Protein p7in Vitro

1996 ◽  
Vol 218 (1) ◽  
pp. 352-355 ◽  
Author(s):  
Ming-Shi Li ◽  
Guillermo Garcia-Asua ◽  
Uma Bhattacharyya ◽  
Paolo Mascagni ◽  
Brian M. Austen ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Nucleocapsid Protein ◽  
Immunodeficiency Virus

Identification of a binding site for the human immunodeficiency virus type 1 nucleocapsid protein

Peptides ◽  
1994 ◽  
pp. 956-957
Author(s):  
K. Sakaguchi ◽  
N. Zambrano ◽  
E. T. Baldwin ◽  
B. A. Shapiro ◽  
J. W. Erickson ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Binding Site ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Nucleocapsid Protein ◽  
Immunodeficiency Virus

scholarly journals The human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein zinc ejection activity of disulfide benzamides and benzisothiazolones: correlation with anti-HIV and virucidal activities.

1997 ◽  
Vol 41 (2) ◽  
pp. 394-400 ◽  
Author(s):  
P J Tummino ◽  
P J Harvey ◽  
T McQuade ◽  
J Domagala ◽  
R Gogliotti ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Antiviral Activity ◽  
Nucleocapsid Protein ◽  
Nitrobenzoic Acid ◽  
Immunodeficiency Virus ◽  
Kinetic Rates ◽  
Thiol Reagent ◽  
Relative Kinetic

It has been shown previously by our group and others that a series of four disulfide benzamides with cellular anti-human immunodeficiency virus (HIV) activity can eject zinc from HIV type 1 nucleocapsid protein (NCp7) in vitro while analogs without antiviral activity do not. We also found that the zinc ejection activity correlates with the loss of the ability of NCp7 to bind to HIV psi RNA in vitro. These observations indicate that the antiviral disulfide benzamides may act at a novel retroviral target of action, i.e., the nucleocapsid protein. The present studies examine the relationship among disulfide benzamide structure, in vitro NCp7 zinc ejection activity, and antiviral activity for a larger series of compounds. All of the antiviral disulfide benzamides were found to eject NCp7 zinc, while some disulfide benzamides with zinc ejection activity are not antiviral. Utilizing the thiol reagent 5,5'-dithiobis(2-nitrobenzoic acid), it was determined that the o-amido-phenyl disulfides being studied cyclize in aqueous solution to form benzisothiazolones. A series of benzisothiazolones, which are stable in solution in the absence of dithiothreitol, were found to eject NCp7 zinc at a rate similar to that of their disulfide benzamide analogs and to possess similar antiviral activity. It was also found that the relative rates of HIV inactivation by various disulfide benzamides and benzisothiazolones correlate with their relative kinetic rates of NCp7 zinc ejection, which is consistent with the nucleocapsid protein being the target of action of these compounds.

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