Methods for the Analysis of HIV-1 Nucleocapsid Protein Interactions with Oligonucleotides

2009 ◽  
pp. 209-221 ◽  
Author(s):  
Andrew G. Stephen ◽  
Robert J. Fisher
Keyword(s):  
Protein Interactions ◽  
Nucleocapsid Protein ◽  
Hiv 1

scholarly journals HIV-1 inactivation by 4-vinylpyridine is enhanced by dissociating Zn2+ from nucleocapsid protein

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):  
Nucleocapsid Protein ◽  
Hiv 1

Identification of HIV-1 nucleocapsid protein: nucleic acid antagonists with cellular anti-HIV activity

2002 ◽  
Vol 296 (5) ◽  
pp. 1228-1237 ◽  
Author(s):  
Andrew G Stephen ◽  
Karen M Worthy ◽  
Eric Towler ◽  
Judy A Mikovits ◽  
Shizuko Sei ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleocapsid Protein ◽  
Protein Nucleic Acid ◽  
Anti Hiv ◽  
Hiv 1

scholarly journals Synthesis and Evaluation of Bifunctional Aminothiazoles as Antiretrovirals Targeting the HIV-1 Nucleocapsid Protein

2018 ◽  
Vol 10 (4) ◽  
pp. 463-468 ◽  
Author(s):  
Mattia Mori ◽  
Maria Chiara Dasso Lang ◽  
Francesco Saladini ◽  
Nastasja Palombi ◽  
Lesia Kovalenko ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Hiv 1

Rationally Designed Peptides as Efficient Inhibitors of Nucleic Acid Chaperone Activity of HIV-1 Nucleocapsid Protein

Biochemistry ◽  
2018 ◽  
Vol 57 (30) ◽  
pp. 4562-4573 ◽  
Author(s):  
Volodymyr Shvadchak ◽  
Sarwat Zgheib ◽  
Beata Basta ◽  
Nicolas Humbert ◽  
Johannes Langedijk ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleocapsid Protein ◽  
Chaperone Activity ◽  
Nucleic Acid Chaperone ◽  
Hiv 1

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.

Quantitative analysis of the interactions between HIV-1 integrase and retroviral reverse transcriptases

2008 ◽  
Vol 412 (1) ◽  
pp. 163-170 ◽  
Author(s):  
Alon Herschhorn ◽  
Iris Oz-Gleenberg ◽  
Amnon Hizi
Keyword(s):  
Conformational Changes ◽  
Protein Interactions ◽  
Molecular Mechanisms ◽  
Reaction Model ◽  
Protein Protein Interactions ◽  
Common Site ◽  
Leukaemia Virus ◽  
Reverse Transcriptases ◽  
Interaction Kinetics ◽  
Hiv 1

The RT (reverse transcriptase) of HIV-1 interacts with HIV-1 IN (integrase) and inhibits its enzymatic activities. However, the molecular mechanisms underling these interactions are not well understood. In order to study these mechanisms, we have analysed the interactions of HIV-1 IN with HIV-1 RT and with two other related RTs: those of HIV-2 and MLV (murine-leukaemia virus). All three RTs inhibited HIV-1 IN, albeit to a different extent, suggesting a common site of binding that could be slightly modified for each one of the studied RTs. Using surface plasmon resonance technology, which monitors direct protein–protein interactions, we performed kinetic analyses of the binding of HIV-1 IN to these three RTs and observed interesting binding patterns. The interaction of HIV-1 RT with HIV-1 IN was unique and followed a two-state reaction model. According to this model, the initial IN–RT complex formation was followed by a conformational change in the complex that led to an elevation of the total affinity between these two proteins. In contrast, HIV-2 and MLV RTs interacted with IN in a simple bi-molecular manner, without any apparent secondary conformational changes. Interestingly, HIV-1 and HIV-2 RTs were the most efficient inhibitors of HIV-1 IN activity, whereas HIV-1 and MLV RTs showed the highest affinity towards HIV-1 IN. These modes of direct protein interactions, along with the apparent rate constants calculated and the correlations of the interaction kinetics with the capacity of the RTs to inhibit IN activities, are all discussed.

scholarly journals A Class of Potent Inhibitors of the HIV-1 Nucleocapsid Protein Based on Aminopyrrolic Scaffolds

2020 ◽  
Vol 11 (5) ◽  
pp. 698-705
Author(s):  
Stefano Ciaco ◽  
Nicolas Humbert ◽  
Eléonore Real ◽  
Christian Boudier ◽  
Oscar Francesconi ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Hiv 1

scholarly journals Studies on HIV‐1 RNA‐protein interactions.

2017 ◽  
Vol 31 (S1) ◽  
Author(s):  
Nicole Hadler ◽  
Eryn Stockdale ◽  
Kenneth Wise ◽  
Ina O'Carroll
Keyword(s):  
Protein Interactions ◽  
Hiv 1
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