Islatravir对HIV-1逆转录酶中Doravirine耐药相关替代突变增强抗病毒活性的动力学见解

IF 3 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Nikita Zalenski, Derek J Savoie, Amit Gaur, Neil A Patel, David J Suo, Turner W Seay, Daniel Betancourt, Zucai Suo
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引用次数: 0

摘要

Islatravir (ISL, EFdA)是一种核苷类似物,在病毒复制过程中抑制HIV-1逆转录酶(RT)易位。它的高效源于其独特的结构特征:在HIV-1 RT中,一个4'-乙基与疏水口袋(含有A114、Y115、F160、M184和D185)相互作用,阻碍易位;一个3'-羟基模仿天然核苷,有效结合。最近的3期临床试验,将ISL与非核苷类逆转录酶抑制剂Doravirine (DOR)联合使用,表明其不次于现有的治疗方法,由于其独特的耐药特征,提供了独特的优势。例如,DOR相关突变,V106I/F227C,在临床中赋予bb10105倍的DOR抗性,在已发表的基于细胞的抗性选择分析中意外地将ISL的效力提高了2.3倍。相比之下,单独使用V106I不影响Islatravir的效力,而单独使用F227C可将其增强5.6倍。为了从动力学上理解这些发现,我们使用预稳态动力学分析来确定EFdA 5'-三磷酸(EFdA- tp)和dATP掺入的动力学参数。我们发现EFdA-TP与F227C突变体在RNA模板上的结合效率比dATP高1.4倍,在DNA模板上的结合效率高1.7倍。然而,这种差异在F227C/V106I突变体中仅高出1.1- 1.3倍。我们的能量最小化模型显示,这些突变远程改变了疏水性4'-乙基基团结合口袋的结构,令人惊讶地加强了口袋与EFdA-TP的结合相互作用。除此之外,F227C突变降低了dATP与这两个模板的结合亲和力。我们的数据为已发表的基于细胞的耐药选择试验结果建立了动力学基础,强调了ISL/DOR联合疗法治疗HIV-1感染患者的巨大潜力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Kinetic Insights into the Enhanced Antiviral Activity of Islatravir against Doravirine Resistance-Associated Substitution Mutations in HIV-1 Reverse Transcriptase.

Islatravir (ISL, EFdA) is a nucleoside analog that inhibits HIV-1 reverse transcriptase (RT) translocation during viral replication. Its high potency stems from unique structural features: a 4'-ethynyl group that interacts with the hydrophobic pocket (containing A114, Y115, F160, M184, and D185) in HIV-1 RT, hindering translocation, and a 3'-hydroxyl group that mimics natural nucleosides for efficient incorporation. Recent phase 3 clinical trials, combining ISL with Doravirine (DOR), a non-nucleoside reverse transcriptase inhibitor, show that it is noninferior to existing treatments, offering a unique advantage due to their distinct resistance profiles. For instance, DOR-associated mutations, V106I/F227C, which confer >105-fold DOR resistance in clinics, unexpectedly boost ISL's potency by 2.3-fold in published cell-based resistance selection assays. In contrast, V106I alone does not affect Islatravir's potency, while F227C alone enhances it by 5.6-fold. To kinetically understand these findings, we used presteady-state kinetic assays to determine the kinetic parameters for EFdA 5'-triphosphate (EFdA-TP) and dATP incorporation. We found that the incorporation efficiency of EFdA-TP was 1.4-fold higher than that of dATP on an RNA template and 1.7-fold higher on a DNA template with the F227C mutant. However, this difference was only 1.1- to 1.3-fold higher with the F227C/V106I mutant. Our energy-minimized modeling revealed that these mutations remotely alter the hydrophobic 4'-ethynyl group-binding pocket's structure, surprisingly strengthening the pocket's binding interactions with EFdA-TP. Alongside this, the F227C mutation decreased dATP's binding affinity with both templates. Our data established a kinetic basis for the published cell-based resistance selection assay results, underscoring the significant potential of the ISL/DOR combination therapy in treating HIV-1 infected patients.

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来源期刊
Biochemistry Biochemistry
Biochemistry Biochemistry 生物-生化与分子生物学
CiteScore
5.50
自引率
3.40%
发文量
336
审稿时长
1-2 weeks
期刊介绍: Biochemistry provides an international forum for publishing exceptional, rigorous, high-impact research across all of biological chemistry. This broad scope includes studies on the chemical, physical, mechanistic, and/or structural basis of biological or cell function, and encompasses the fields of chemical biology, synthetic biology, disease biology, cell biology, nucleic acid biology, neuroscience, structural biology, and biophysics. In addition to traditional Research Articles, Biochemistry also publishes Communications, Viewpoints, and Perspectives, as well as From the Bench articles that report new methods of particular interest to the biological chemistry community.
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