The reverse transcriptase of HIV‐1: from enzymology to therapeutic intervention

@article{TarragoLitvak1994TheRT,
  title={The reverse transcriptase of HIV‐1: from enzymology to therapeutic intervention},
  author={Laura Tarrago-Litvak and Marie Line Andreola and Georgy A. Nevinsky and L Sarih-Cottin and Simon Litvak},
  journal={The FASEB Journal},
  year={1994},
  volume={8},
  pages={497 - 503}
}
The human immunodeficiency virus type 1 (HIV‐1) is the etiologic agent of AIDS. Replication of this virus requires the activity of a retrovirus encoded RNA‐dependent DNA polymerase, or reverse transcriptase (RT). HIV‐1 RT is required for the synthesis of the double‐stranded proviral DNA from the single‐stranded retroviral RNA genome. HIV‐1 RT has two subunits of 66 kDa and 51 kDa. The 66‐kDa subunit contains the DNA polymerase and RNase H domains whereas the 51‐kDa subunit, obtained by… 
Phosphorothioate oligonucleotides derived from human immunodeficiency virus type 1 (HIV-1) primer tRNALys3 are strong inhibitors of HIV-1 reverse transcriptase and arrest viral replication in infected cells
TLDR
It is shown that primer tRNA-derived oligodeoxynucleotides (ODNs) carrying a phosphorothioate (PS) modification are strong inhibitors of HIV-1 RT, and that the inhibitory effect of the PS-AS may be mediated via both a sense and an antisense mechanism.
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TLDR
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TLDR
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High-affinity interaction of human immunodeficiency virus type-1 reverse transcriptase with partially complementary primers.
TLDR
Comparisons of Km and Vmax values for various primers in the reaction of polymerization catalyzed by the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase suggest that HIV-1 reverse Transcriptase forms additional contacts with the 5'-end region of the non-complementary primer.
Immunogenic properties of reverse transcriptase of HIV type 1 assessed by DNA and protein immunization of rabbits.
TLDR
Rabbits immunized with a plasmid carrying the gene for reverse transcriptase HIV-1 (RT DNA) developed potent antibody and cellular responses to the gene product, and subdomains of reverse transcripts involved in the enzymatic activity of RT were highly immunogenic.
Interaction of HIV-1 Reverse Transcriptase with New Minor Groove Binders and Their Conjugates with Oligonucleotides
The effect on polymerization catalyzed by reverse transcriptase (RT) of the human immunodeficiency virus type 1 (HIV-1) was studied for new nonnatural regular minor groove binders (MGBs) containing
Cellular reservoirs of HIV-1 and their role in viral persistence.
TLDR
Cell populations of the monocyte-macrophage lineage, which originate in the bone marrow, are of particular importance in HIV-1 persistence due to their ability to cross the blood-brain barrier and spread HIV- 1 infection in the immunoprivileged central nervous system (CNS).
A neutravidin-based assay for reverse transcriptase suitable for high throughput screening of retroviral activity.
TLDR
A non-isotopic neutravidin-based reverse transcriptase (RT) assay adapted for high throughput screening of HIV activity was shown to be as sensitive as a radioactive assay and the RT activity correlated well with levels of cell-associated HIVp24.
Quinoxapeptins: novel chromodepsipeptide inhibitors of HIV-1 and HIV-2 reverse transcriptase. I. The producing organism and biological activity.
TLDR
Quinoxapeptin A and B are novel chromodepsipeptides which were isolated from a nocardioform actinomycete with indeterminant morphology and are specific inhibitors of HIV-1 and HIV-2 reverse transcriptase because they did not inhibit human DNA polymerase alpha, beta, gamma and delta.
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TLDR
It is demonstrated that the HIV‐1 RT p66/p51 specifically binds to its cognate primer tRNALys,3 even in the presence of a 100‐fold molar excess of other tRNAs.
Structure of HIV-1 reverse transcriptase/DNA complex at 7 Å resolution showing active site locations
TLDR
The structure at 7 Å resolution of a ternary complex of the HIV-1 reverse transcriptase heterodimer, a monoclonal antibody Fab fragment8, and a duplex DNA template-primer is reported, allowing tentative identification of the polymerase nucleoside triphosphate binding site.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
The DNA polymerase and RNase H activities of reverse transcriptase appear to be the only enzymes required to produce the linear double-stranded DNA copy of the RNA genome that is subsequently integrated into the retroviral genome RNA.
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