Lyngdoh Denzelle L, Shukla Harish, Sonkar Amit, Anupam Rajaneesh, Tripathi Timir
Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India.
Department of Biotechnology, Dr. Harisingh Gour Central University, Sagar 470003, India.
ACS Omega. 2019 Jun 7;4(6):10003-10018. doi: 10.1021/acsomega.9b01017. eCollection 2019 Jun 30.
Intrinsically disordered proteins (IDPs) lack an ordered 3D structure. These proteins contain one or more intrinsically disordered protein regions (IDPRs). IDPRs interact promiscuously with other proteins, which leads to their structural transition from a disordered to an ordered state. Such interaction-prone regions of IDPs are known as molecular recognition features. Recent studies suggest that IDPs provide structural plasticity and functional diversity to viral proteins that are involved in rapid replication and immune evasion within the host cells. In the present study, we evaluated the prevalence of IDPs and IDPRs in human T lymphotropic virus type 1 (HTLV-1) proteome. We also investigated the presence of MoRF regions in the structural and nonstructural proteins of HTLV-1. We found abundant IDPRs in HTLV-1 bZIP factor, p30, Rex, and structural nucleocapsid p15 proteins, which are involved in diverse functions such as virus proliferation, mRNA export, and genomic RNA binding. Our study analyzed the HTLV-1 proteome with the perspective of intrinsic disorder identification. We propose that the intrinsic disorder analysis of HTLV-1 proteins may form the basis for the development of protein disorder-based drugs.
内在无序蛋白（IDP）缺乏有序的三维结构。这些蛋白质包含一个或多个内在无序蛋白区域（IDPR）。IDPR与其他蛋白质发生杂乱的相互作用，这导致它们从无序状态转变为有序状态。IDP的这种易于相互作用的区域被称为分子识别特征。最近的研究表明，IDP为参与宿主细胞内快速复制和免疫逃逸的病毒蛋白提供结构可塑性和功能多样性。在本研究中，我们评估了人类嗜T淋巴细胞病毒1型（HTLV-1）蛋白质组中IDP和IDPR的普遍性。我们还研究了HTLV-1结构蛋白和非结构蛋白中分子识别特征区域的存在情况。我们在HTLV-1 bZIP因子、p30、Rex和结构核衣壳p15蛋白中发现了丰富的IDPR，这些蛋白参与病毒增殖、mRNA输出和基因组RNA结合等多种功能。我们的研究从内在无序识别的角度分析了HTLV-1蛋白质组。我们提出，对HTLV-1蛋白质的内在无序分析可能为基于蛋白质无序的药物开发奠定基础。
