Journal
VIROLOGY
Volume 367, Issue 2, Pages 253-264Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2007.05.034
Keywords
fidelity; reverse transcriptase; spumavirus; HIV-1; lentivirus
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Funding
- Intramural NIH HHS [Z01 BC010481-05] Funding Source: Medline
- NCI NIH HHS [CA18282, R01 CA018282] Funding Source: Medline
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We compared the in vitro fidelity of wild-type human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) and the prototype foamy virus (PFV) RT. Both enzymes had similar error rates for single nucleotide substitutions; however, PFV RT did not appear to make errors at specific hotspots, like HIV-1 RT. In addition, PFV RT made more deletions and insertions than HIV-1 RT. Although the majority of the missense errors made by HIV-1 RT and PFV RT are different, relatively few of the mutations caused by either enzyme can be explained by a misalignment/slippage mechanism. We suggest that the higher polymerase activity of PFV RT could contribute to the ability of the enzyme to jump to the same or a different template. Published by Elsevier Inc.
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