title: In vitro fidelity of the prototype primate foamy virus (PFV) RT compared to HIV-1 RT.
abstract: 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.
authors.affiliation: HIV Drug Resistance Program, National Cancer Institute at Frederick, Frederick, MD 21702, USA.
authors.forename: Paul L
authors.initials: PL
authors.lastname: Boyer
authors.forename: Carolyn R
authors.initials: CR
authors.lastname: Stenbak
authors.forename: David
authors.initials: D
authors.lastname: Hoberman
authors.forename: Maxine L
authors.initials: ML
authors.lastname: Linial
authors.forename: Stephen H
authors.initials: SH
authors.lastname: Hughes
mesh_terms: D000818:Animals; D003854:Deoxyribonucleotides / Q000378:metabolism; D054303:HIV Reverse Transcriptase / Q000235:genetics / Q000378:metabolism*; D015497:HIV-1 / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D011323:Primates; D012367:RNA, Viral / Q000235:genetics* / Q000378:metabolism; D016092:Spumavirus / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D003854:Deoxyribonucleotides; D012367:RNA, Viral; D054303:HIV Reverse Transcriptase