Mutations at position 184 of human immunodeficiency virus type-1 reverse transcriptase affect virus titer and viral DNA synthesis

Virology. 2004 Apr 25;322(1):13-21. doi: 10.1016/j.virol.2004.01.004.

Abstract

Methionine at position 184 of human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) was changed to valine, isoleucine, threonine, or alanine in an HIV-1-based vector. The vectors were analyzed for replication capacity and for resistance to the nucleoside analog 2',3'-dideoxy-3'thiacytidine (3TC) using a single-cycle assay. Viruses containing the valine or isoleucine mutations were highly resistant to 3TC and replicated almost as well as the wild-type virus. The virus containing the threonine mutation was resistant to 3TC, but replicated about 30% as well as the wild-type. The alanine mutation conferred partial resistance to 3TC, but replicated poorly. The amounts of viral DNA synthesized decreased in 3TC-treated cells when the cells were infected with wild-type virus and the M184A mutant. The effect of these mutations on the generation of the ends of the linear viral DNA was determined using the sequence of the 2-LTR circle junctions. The M184T mutation increased the proportion of 2-LTR circle junctions containing a tRNA insertion, suggesting that the mutation affected the RNase H activity of RT.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • DNA, Viral / biosynthesis*
  • Dose-Response Relationship, Drug
  • Drug Resistance, Viral
  • HIV Reverse Transcriptase / chemistry
  • HIV Reverse Transcriptase / genetics*
  • HIV-1 / drug effects
  • HIV-1 / enzymology
  • HIV-1 / genetics*
  • Lamivudine / pharmacology
  • Methionine / chemistry
  • Point Mutation
  • Reverse Transcriptase Inhibitors / pharmacology
  • Ribonuclease H / metabolism
  • Terminal Repeat Sequences
  • Virus Replication

Substances

  • DNA, Viral
  • Reverse Transcriptase Inhibitors
  • Lamivudine
  • Methionine
  • HIV Reverse Transcriptase
  • Ribonuclease H