ArticleJournal of virology2002
Mutation of the catalytic domain of the foamy virus reverse transcriptase leads to loss of processivity and infectivity.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Crystal Structure of a Retroviral Polyprotein: Prototype Foamy Virus Protease-Reverse Transcriptase (PR-RT).Viruses · 2021Article
- The impact of lentiviral vector genome size and producer cell genomic to gag-pol mRNA ratios on packaging efficiency and titre.Molecular therapy. Methods & clinical development · 2021Article
- Foamy Viruses, Bet, and APOBEC3 Restriction.Viruses · 2021Review
- M-MuLV reverse transcriptase: Selected properties and improved mutants.Computational and structural biotechnology journal · 2021Review
- Review
- Inhibition of foamy virus reverse transcriptase by human immunodeficiency virus type 1 RNase H inhibitors.Antimicrobial agents and chemotherapy · 2014Article
- Nuclear localization signals in prototype foamy viral integrase for successive infection and replication in dividing cells.Molecules and cells · 2014Article
- Review
- Foamy virus assembly with emphasis on pol encapsidation.Viruses · 2013Review
- Review
- Foamy retrovirus integrase contains a Pol dimerization domain required for protease activation.Journal of virology · 2011Article
- Influence of insulators on transgene expression from integrating and non-integrating lentiviral vectors.Genetic vaccines and therapy · 2011Article
- Molecular biology of foamy viruses.Medical microbiology and immunology · 2010Review
- Article
- Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases.Retrovirology · 2010Article
- Accuracy estimation of foamy virus genome copying.Retrovirology · 2009Article
- AZT-resistant foamy virus.Virology · 2008Article
- In vitro fidelity of the prototype primate foamy virus (PFV) RT compared to HIV-1 RT.Virology · 2007Article
- Role of the foamy virus Pol cleavage site in viral replication.Journal of virology · 2007Article
- Determination of the relative amounts of Gag and Pol proteins in foamy virus particles.Retrovirology · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Foamy virus (FV) replication is resistant to most nucleoside analog reverse transcriptase (RT) inhibitors. In an attempt to create a 2',3'-dideoxy-3'-thiacytidine (3TC)-sensitive virus, the second residue in the highly conserved YXDD motif of simian foamy virus-chimpanzee (human isolate) [SFVcpz(hu)] RT was changed from Val (V) to Met (M). Unexpectedly, the resultant virus, SFVcpz(hu) RT-V313M, replicated poorly, and Met rapidly reverted to Val. Despite the presence of approximately 50% of wild-type RT activity in RT-V313M virions, full-length DNA products were not detected in transfected cells. Using purified recombinant enzymes, we found that the wild-type FV RT is significantly more processive than human immunodeficiency virus type 1 RT. However, the V313M mutant has about 40% of the wild-type level of FV RT activity and has a lower processivity than the wild-type FV enzyme. The V313M mutant RT is also relatively resistant to 3TC. These results suggest that the decrease in RT activity and processivity of FV RT-V313M prevents completion of reverse transcription and greatly diminishes viral replication.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.