Tryptophan scanning mutagenesis of aromatic residues within the polymerase domain of HIV-1 reverse transcriptase: critical role of Phe-130 for p51 function and second-site revertant restoring viral replication capacity.
Tryptophan scanning mutagenesis of aromatic residues within the polymerase domain of HIV-1 reverse transcriptase: critical role of Phe-130 for p51 function and second-site revertant restoring viral replication capacity.
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HIV-1 逆转录酶聚合酶结构域内芳香族残基的色氨酸扫描诱变：Phe-130 对 p51 功能和第二位点恢复病毒复制能力的关键作用。
DOI：
10.1016/j.virol.2004.04.010
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发表时间：
2004
期刊：
影响因子：
3.7
通讯作者：
L. Menéndez
中科院分区：
文献类型：
--
作者：
I. Olivares;M. Gutiérrez;C. López;L. Menéndez
The effects on virus viability and reverse transcriptase (RT) function of substituting Trp for Tyr or Phe residues within the polymerase domain of human immunodeficiency virus type 1 (HIV-1) RT have been analyzed with an infectious HIV-1 clone. Viruses containing mutations Y56W, F61W, F87W, F116W, Y127W, Y144W, F171W, Y181W, Y183W, Y188W, F227W, or Y232W in their RT-coding regions were viable and showed replication capacities similar or slightly reduced in comparison with the wild-type HIV-1. However, RTs bearing mutations F77W or Y146W had a dNTP-binding defect, rendering nonviable viruses. HIV-1 carrying RT mutations F124W or F130W replicated very poorly, but compensatory changes (K83R for F124W, and T58S for F130W) were selected upon passaging the virus in cell culture. The amino acid substitution F130W diminishes the stability of the 51-kDa subunit of the RT (p51) and impairs polyprotein processing in virus-infected cells, an effect that can be mitigated when T58S is found in p51.
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DOI：
10.2174/1568005033481033
发表时间：
2003
期刊：
Current drug targets. Infectious disorders
影响因子：
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作者：
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DOI：
10.1021/bi9728452
发表时间：
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期刊：
Biochemistry.
影响因子：
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作者：
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