ArticleNucleic acids research2008
AZT resistance of simian foamy virus reverse transcriptase is based on the excision of AZTMP in the presence of ATP.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA.Nucleic acids research · 2019Article
- Review
- Structure and nucleic acid binding properties of KOW domains 4 and 6-7 of human transcription elongation factor DSIF.Scientific reports · 2018Article
- Review
- Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNase H inhibitors.Nucleic acids research · 2016Article
- AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase.Retrovirology · 2015Article
- Foamy virus Gag p71-p68 cleavage is required for template switch of the reverse transcriptase.Journal of virology · 2013Article
- The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.Retrovirology · 2012Article
- The prototype foamy virus protease is active independently of the integrase domain.Retrovirology · 2012Article
- Insights into the structure and activity of prototype foamy virus RNase H.Retrovirology · 2012Article
- Regulation of foamy virus protease activity by viral RNA: a novel and unique mechanism among retroviruses.Journal of virology · 2011Article
- Molecular biology of foamy viruses.Medical microbiology and immunology · 2010Review
- Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases.Retrovirology · 2010Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Azidothymidine (AZT, zidovudine) is one of the few nucleoside inhibitors known to inhibit foamy virus replication. We have shown previously that up to four mutations in the reverse transcriptase gene of simian foamy virus from macaque (SFVmac) are necessary to confer high resistance against AZT. To characterize the mechanism of AZT resistance we expressed two recombinant reverse transcriptases of highly AZT-resistant SFVmac in Escherichia coli harboring three (K211I, S345T, E350K) or four mutations (K211I, I224T, S345T, E350K) in the reverse transcriptase gene. Our analyses show that the polymerization activity of these mutants is impaired. In contrast to the AZT-resistant reverse transcriptase of HIV-1, the AZT resistant enzymes of SFVmac reveal differences in their kinetic properties. The SFVmac enzymes exhibit lower specific activities on poly(rA)/oligo(dT) and higher K(M)-values for polymerization but no change in K(D)-values for DNA/DNA or RNA/DNA substrates. The AZT resistance of the mutant enzymes is based on the excision of the incorporated inhibitor in the presence of ATP. The additional amino acid change of the quadruple mutant appears to be important for regaining polymerization efficiency.
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