Purification and Characterization of a Laccase with Inhibitory Activity Toward HIV-1 Reverse Transcriptase and Tumor Cells from an Edible Mushroom (Pleurotus cornucopiae)

2010 ◽  
Vol 17 (8) ◽  
pp. 1040-1047 ◽  
Author(s):  
Jack Ho Wong ◽  
Tzi Bun Ng ◽  
Yun Jiang ◽  
Fang Liu ◽  
Stephen Cho Wing Sze ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Tumor Cells ◽  
Inhibitory Activity ◽  
Edible Mushroom ◽  
Purification And Characterization ◽  
Hiv 1

A Novel Ribonuclease with HIV-1 Reverse Transcriptase Inhibitory Activity from the Edible Mushroom Hygrophorus russula

2013 ◽  
Vol 170 (1) ◽  
pp. 219-230 ◽  
Author(s):  
Mengjuan Zhu ◽  
Lijing Xu ◽  
Xiao Chen ◽  
Zengqiang Ma ◽  
Hexiang Wang ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Inhibitory Activity ◽  
Edible Mushroom ◽  
Hiv 1

Characterization of the Antiviral Activity of Highly Substituted Pyrroles: A Novel Class of Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitor

1995 ◽  
Vol 6 (2) ◽  
pp. 98-108 ◽  
Author(s):  
T. Antonucci ◽  
J. S. Warmus ◽  
J. C. Hodges ◽  
D. G. Nickell
Keyword(s):  
Reverse Transcriptase ◽  
Cell Lines ◽  
Inhibitory Activity ◽  
Nucleoside Reverse Transcriptase Inhibitor ◽  
Transcriptase Inhibitor ◽  
Peripheral Blood Lymphocytes ◽  
Transformed Cell Lines ◽  
Reverse Transcriptase Inhibitor ◽  
Hiv 1

As a result of mass screening of the Parke-Davis Pharmaceutical compound library for inhibitors of HIV-1 reverse transcriptase (RT) activity, a novel class of inhibitor, the pyrroles, was identified. Subsequently, a series of analogues was screened for inhibitory activity against HIV-1 and some structure-activity relationships were identified. Further characterization of the most potent pyrrole involved comparing its effects in peripheral blood lymphocytes (PBLs) with its effects in transformed cell lines; the pyrrole had the same efficacy (EC50 = approximately 2 μM) but was less toxic in PBLs (IC50 = 175 μM) than in the cell lines CEM-SS and MT-2 (IC50 = 60-70 μM). The pyrrole was active against a strain of HIV-1 resistant to AZT (strain G9106) but lost activity against both HIV-2 (strain ROD) and a strain of HIV-1 resistant to a non-nucleoside reverse transcriptase inhibitor (the pyridinone-resistant strain A17). Moreover, in direct enzymatic testing against HIV-1 RT purified from virus particles and against RT expressed recombinantly, the pyrrole showed potent inhibitory activity. We conclude that the pyrroles present a novel class of HIV-1 non-nucleoside reverse transcriptase inhibitor.

Purification and Characterization of HIV-1 Reverse Transcriptase Having a 1:1 Ratio of p66 and p51 Subunits

1994 ◽  
Vol 5 (6) ◽  
pp. 614-621 ◽  
Author(s):  
M. Stahlhut ◽  
Y. Li ◽  
J.H. Condra ◽  
J. Fu ◽  
L. Gotlib ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Purification And Characterization ◽  
Hiv 1

scholarly journals Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinantEscherichia coli

FEBS Letters ◽  
1990 ◽  
Vol 270 (1-2) ◽  
pp. 76-80 ◽  
Author(s):  
S.Patricia Becerra ◽  
G.Marius Clore ◽  
Angela M. Gronenborn ◽  
Anders R. Karlström ◽  
Stephen J. Stahl ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Rnase H ◽  
Purification And Characterization ◽  
Hiv 1

scholarly journals High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Betty Ha ◽  
Kevin P. Larsen ◽  
Jingji Zhang ◽  
Ziao Fu ◽  
Elizabeth Montabana ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Viral Entry ◽  
Reverse Transcription ◽  
Molecular Mechanisms ◽  
Dissociation Kinetics ◽  
Structural Mechanism ◽  
Medium Resolution ◽  
Kinetics Of ◽  
Hiv 1

AbstractReverse transcription of the HIV-1 viral RNA genome (vRNA) is an integral step in virus replication. Upon viral entry, HIV-1 reverse transcriptase (RT) initiates from a host tRNALys3 primer bound to the vRNA genome and is the target of key antivirals, such as non-nucleoside reverse transcriptase inhibitors (NNRTIs). Initiation proceeds slowly with discrete pausing events along the vRNA template. Despite prior medium-resolution structural characterization of reverse transcriptase initiation complexes (RTICs), higher-resolution structures of the RTIC are needed to understand the molecular mechanisms that underlie initiation. Here we report cryo-EM structures of the core RTIC, RTIC–nevirapine, and RTIC–efavirenz complexes at 2.8, 3.1, and 2.9 Å, respectively. In combination with biochemical studies, these data suggest a basis for rapid dissociation kinetics of RT from the vRNA–tRNALys3 initiation complex and reveal a specific structural mechanism of nucleic acid conformational stabilization during initiation. Finally, our results show that NNRTIs inhibit the RTIC and exacerbate discrete pausing during early reverse transcription.

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